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2-ketocaproate + NH3 + NADH
2-aminocaproate + H2O + NAD+
2-oxo-3-methylbutanoate + NH3 + NADH
L-Val + NAD+ + H2O
-
-
-
-
?
2-oxobutanoate + NH3 + NADH
2-aminobutanoate + H2O + NAD+
2-oxobutyrate + NH3 + NADH + H+
L-2-aminobutyrate + H2O + NAD+
2-oxoglutarate + NH3 + NADH
L-Gln + NAD+ + H2O
2-oxoglutarate + NH3 + NADH + H+
L-glutamate + H2O + NAD+
-
-
-
r
2-oxopentanoate + NH3 + NADH + H+
L-norvaline + H2O + NAD+
-
-
-
r
3-bromopyruvate + NH3 + NADH
2-amino-3-bromopropanoate + NAD+ + H2O
-
5.3% of the activity with pyruvate
-
-
?
3-fluoropyruvate + NH3 + NADH
3-fluoro-L-alanine + H2O + NAD+
3-fluoropyruvate + NH3 + NADH
? + H2O + NAD+
3-fluoropyruvate + NH3 + NADH + H+
3-fluoro-L-alanine + H2O + NAD+
3-hydroxypyruvate + NH3 + NADH
L-Ser + H2O + NAD+
3-hydroxypyruvate + NH3 + NADH
Ser + H2O + NAD+
-
15.4% of the activity with pyruvate
-
-
?
3-hydroxypyruvate + NH3 + NADH + H+
L-serine + H2O + NAD+
-
-
-
r
4-methyl-2-oxopentanoate + NH3 + NADH
2-amino-4-methylpentanoate + NAD+ + H2O
D-Ala + H2O + NAD+
pyruvate + NH3 + NADH
D-Ser + H2O + NAD+
3-hydroxypyruvate + NH3 + NADH
DL-alanine + H2O + NAD+
pyruvate + NH3 + NADH + H+
-
-
-
-
r
Gly + H2O + NAD+
glyoxylate + NH3 + NADH
-
-
-
r
glycine + H2O + NAD+
glyoxylate + NH3 + NADH + H+
-
-
-
-
r
glyoxalate + NH3 + NADH + H+
aminoacetate + H2O + NAD+
-
-
-
-
r
glyoxylate + NH3 + NADH
aminoacetate + NAD+ + H2O
glyoxylate + NH3 + NADH + H+
glycine + H2O + NAD+
glyoxylate + NH3 + NADH + H+
glycine + NAD+
hydroxypyruvate + NH3 + NADH
L-Ser + NAD+ + H2O
ketovalerate + NH3 + NADH
2-aminovalerate + H2O + NAD+
-
-
-
-
?
L-2-amino-4-pentenoate + H2O + NAD+
2-oxo-4-pentenoate + NH3 + NADH
L-2-aminobutanoate + H2O + NAD+
2-oxobutanoate + NH3 + NADH + H+
L-2-aminobutyrate + H2O + NAD+
2-oxobutyrate + NH3 + NADH
-
-
-
-
r
L-2-aminobutyrate + H2O + NAD+
2-oxobutyrate + NH3 + NADH + H+
-
-
-
r
L-Ala + H2O + 1,N6-etheno-NAD+
pyruvate + NH3 + 1,N6-etheno-NADH
L-Ala + H2O + 3-acetylpyridine-NAD+
pyruvate + H2O + 3-acetylpyridine-NADH
L-Ala + H2O + 3-pyridinealdehyde-NAD+
?
-
5.0% of the activity with NAD+
-
-
?
L-Ala + H2O + deamino-NAD+
pyruvate + NH3 + deamino-NADH
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
L-Ala + H2O + NADP+
pyruvate + NH3 + NADPH
L-Ala + H2O + nicotinamide guanine dinucleotide
?
L-alanine + H2O + NAD+
pyruvate + NH3 + NADH + H+
L-alanine + NAD+ + H2O
pyruvate + NH3 + NADH + H+
L-Asp + H2O + NAD+
oxaloacetate + NH3 + NADH
-
-
-
-
r
L-homophenylalanine + H2O + NADH + H+
2-oxo-4-phenylbutanoate + NH3 + NAD+
-
-
-
?
L-homoserine + H2O + NAD+
4-hydroxy-2-oxobutanoate + NH3 + NADH
-
-
-
?
L-Ile + H2O + NAD+
2-oxo-3-methylpentanoate + NH3 + NADH
L-isoleucine + H2O + NAD+
2-oxo-3-methylpentanoate + NH3 + NADH + H+
-
-
-
-
r
L-leucine + H2O + NAD+
4-methyl-2-oxopentanoate + NH3 + NADH
-
-
-
?
L-methionine + H2O + NAD+
4-(methylsulfanyl)-2-oxobutanoate + NH3 + NADH
-
-
-
?
L-norleucine + H2O + NADH + H+
2-oxohexanoate + NH3 + NAD+
-
-
-
?
L-norvaline + H2O + NAD+
2-oxopentanoate + NH3 + NADH
L-norvaline + H2O + NAD+
2-oxopentanoate + NH3 + NADH + H+
-
-
-
r
L-Ser + H2O + NAD+
3-hydroxypyruvate + NH3 + NADH
L-serine + H2O + NAD+
3-hydroxypyruvate + NH3 + NADH
L-serine + H2O + NAD+
3-hydroxypyruvate + NH3 + NADH + H+
-
-
-
r
L-serine + H2O + NAD+
3-hydroxypyruvate + NH3 + NADH + NH3 + NADH + H+
-
-
-
-
r
L-Thr + H2O + NAD+
3-hydroxy-2-oxobutyrate + NH3 + NADH
-
-
-
-
?
L-threonine + H2O + NAD+
3-hydroxy-2-oxobutyrate + NH3 + NADH + H+
-
-
-
-
r
L-Val + H2O + NAD+
3-methyl-2-oxobutanoate + NH3 + NADH
L-valine + H2O + NAD+
3-methyl-2-oxobutanoate + NH3 + NADH
L-valine + H2O + NAD+
3-methyl-2-oxobutanoate + NH3 + NADH + H+
oxaloacetate + NH3 + NADH
L-Asp + H2O + NAD+
oxaloacetate + NH3 + NADH + H+
L-aspartate + H2O + NAD+
-
-
-
r
phenylpyruvate + NH3 + NADH
L-phenylalanine + H2O + NAD+
-
-
-
-
?
pyruvate + NH3 + NADH
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
L-Ala + NAD+ + H2O
-
primary route for alanine synthesis in isolated bacteroids, alanine synthesis and secretion contributes to the efficiency of N2-fixation and therefore biomass accumulation
-
-
?
pyruvate + NH3 + NADH
L-alanine + H2O + NAD+
pyruvate + NH3 + NADH + H+
L-Ala + H2O + NAD+
-
-
-
-
?
pyruvate + NH3 + NADH + H+
L-alanine + H2O + NAD+
pyruvate + NH3 + NADPH + H+
L-Ala + H2O + NADP+
-
NADPH is a poor cofactor for wild-type
-
-
?
additional information
?
-
2-ketocaproate + NH3 + NADH
2-aminocaproate + H2O + NAD+
-
-
-
-
?
2-ketocaproate + NH3 + NADH
2-aminocaproate + H2O + NAD+
-
-
-
-
?
2-oxobutanoate + NH3 + NADH
2-aminobutanoate + H2O + NAD+
-
-
-
-
r
2-oxobutanoate + NH3 + NADH
2-aminobutanoate + H2O + NAD+
-
-
-
-
r
2-oxobutanoate + NH3 + NADH
2-aminobutanoate + H2O + NAD+
-
-
-
-
?
2-oxobutanoate + NH3 + NADH
2-aminobutanoate + H2O + NAD+
-
-
-
-
r
2-oxobutanoate + NH3 + NADH
2-aminobutanoate + H2O + NAD+
-
62% of the activity with pyruvate
-
-
?
2-oxobutanoate + NH3 + NADH
2-aminobutanoate + H2O + NAD+
-
4.1% of the activity with pyruvate
-
-
?
2-oxobutanoate + NH3 + NADH
2-aminobutanoate + H2O + NAD+
-
no activity
-
-
?
2-oxobutanoate + NH3 + NADH
2-aminobutanoate + H2O + NAD+
-
3.7% of the activity with pyruvate
-
-
?
2-oxobutanoate + NH3 + NADH
2-aminobutanoate + H2O + NAD+
-
15% of maximal activity
-
-
?
2-oxobutanoate + NH3 + NADH
2-aminobutanoate + H2O + NAD+
-
15.8% of the activity with pyruvate
-
-
?
2-oxobutyrate + NH3 + NADH + H+
L-2-aminobutyrate + H2O + NAD+
-
-
-
r
2-oxobutyrate + NH3 + NADH + H+
L-2-aminobutyrate + H2O + NAD+
-
-
-
r
2-oxoglutarate + NH3 + NADH
L-Gln + NAD+ + H2O
-
no activity
-
-
?
2-oxoglutarate + NH3 + NADH
L-Gln + NAD+ + H2O
-
11.7% of the activity with pyruvate
-
-
?
3-fluoropyruvate + NH3 + NADH
3-fluoro-L-alanine + H2O + NAD+
-
-
-
?
3-fluoropyruvate + NH3 + NADH
3-fluoro-L-alanine + H2O + NAD+
-
97% of the activity with pyruvate
-
-
?
3-fluoropyruvate + NH3 + NADH
? + H2O + NAD+
-
-
-
-
?
3-fluoropyruvate + NH3 + NADH
? + H2O + NAD+
74% of the activity with pyruvate
-
-
?
3-fluoropyruvate + NH3 + NADH + H+
3-fluoro-L-alanine + H2O + NAD+
-
-
-
-
?
3-fluoropyruvate + NH3 + NADH + H+
3-fluoro-L-alanine + H2O + NAD+
recombinant enzyme in whole-cell catalysis at 25°C
-
-
r
3-hydroxypyruvate + NH3 + NADH
L-Ser + H2O + NAD+
-
-
-
-
?
3-hydroxypyruvate + NH3 + NADH
L-Ser + H2O + NAD+
-
123% of the activity with pyruvate
-
-
?
3-hydroxypyruvate + NH3 + NADH
L-Ser + H2O + NAD+
-
-
-
-
?
3-hydroxypyruvate + NH3 + NADH
L-Ser + H2O + NAD+
-
6.9% of the activity with pyruvate
-
-
?
3-hydroxypyruvate + NH3 + NADH
L-Ser + H2O + NAD+
-
32.3% of the activity with pyruvate
-
-
?
3-hydroxypyruvate + NH3 + NADH
L-Ser + H2O + NAD+
54% of the activity with pyruvate
-
-
?
4-methyl-2-oxopentanoate + NH3 + NADH
2-amino-4-methylpentanoate + NAD+ + H2O
-
-
-
-
?
4-methyl-2-oxopentanoate + NH3 + NADH
2-amino-4-methylpentanoate + NAD+ + H2O
-
-
-
-
?
4-methyl-2-oxopentanoate + NH3 + NADH
2-amino-4-methylpentanoate + NAD+ + H2O
-
1.6% of the activity with pyruvate
-
-
?
D-Ala + H2O + NAD+
pyruvate + NH3 + NADH
3.5% of the activity with L-Ala
-
-
?
D-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
32.3% of the activity with L-Ala
-
-
?
D-Ser + H2O + NAD+
3-hydroxypyruvate + NH3 + NADH
4.4% of the activity with L-Ala
-
r
D-Ser + H2O + NAD+
3-hydroxypyruvate + NH3 + NADH
in the reverse reaction the enzyme reacts at 9.3% of the activity with pyruvate
-
r
D-Ser + H2O + NAD+
3-hydroxypyruvate + NH3 + NADH
-
1.3% of the activity with L-Ser
-
-
?
glyoxylate + NH3 + NADH
aminoacetate + NAD+ + H2O
-
-
-
?
glyoxylate + NH3 + NADH
aminoacetate + NAD+ + H2O
-
-
-
-
?
glyoxylate + NH3 + NADH
aminoacetate + NAD+ + H2O
-
-
-
-
?
glyoxylate + NH3 + NADH
aminoacetate + NAD+ + H2O
-
1.2% of the activity with pyruvate
-
-
?
glyoxylate + NH3 + NADH
aminoacetate + NAD+ + H2O
-
6.2% of the activity with pyruvate
-
-
?
glyoxylate + NH3 + NADH
aminoacetate + NAD+ + H2O
-
-
-
-
?
glyoxylate + NH3 + NADH
aminoacetate + NAD+ + H2O
-
5.6% of the activity with pyruvate
-
-
?
glyoxylate + NH3 + NADH
aminoacetate + NAD+ + H2O
-
13.3% of the activity with pyruvate
-
-
?
glyoxylate + NH3 + NADH + H+
glycine + H2O + NAD+
-
-
-
ir
glyoxylate + NH3 + NADH + H+
glycine + H2O + NAD+
-
-
-
ir
glyoxylate + NH3 + NADH + H+
glycine + H2O + NAD+
-
-
-
r
glyoxylate + NH3 + NADH + H+
glycine + H2O + NAD+
-
-
-
r
glyoxylate + NH3 + NADH + H+
glycine + NAD+
-
the enzyme catalyzes the reductive amination of glyoxylate to glycine, but not the reverse reaction
-
-
ir
glyoxylate + NH3 + NADH + H+
glycine + NAD+
the enzyme catalyzes the reductive amination of glyoxylate to glycine, but not the reverse reaction
-
-
ir
glyoxylate + NH3 + NADH + H+
glycine + NAD+
the enzyme catalyzes the reductive amination of glyoxylate to glycine, but not the reverse reaction
-
-
ir
glyoxylate + NH3 + NADH + H+
glycine + NAD+
the enzyme catalyzes the reductive amination of glyoxylate to glycine, but not the reverse reaction
-
-
ir
glyoxylate + NH3 + NADH + H+
glycine + NAD+
the enzyme catalyzes the reductive amination of glyoxylate to glycine, but not the reverse reaction
-
-
ir
glyoxylate + NH3 + NADH + H+
glycine + NAD+
the enzyme catalyzes the reductive amination of glyoxylate to glycine, but not the reverse reaction
-
-
ir
glyoxylate + NH3 + NADH + H+
glycine + NAD+
the enzyme catalyzes the reductive amination of glyoxylate to glycine, but not the reverse reaction
-
-
ir
hydroxypyruvate + NH3 + NADH
L-Ser + NAD+ + H2O
-
-
-
-
?
hydroxypyruvate + NH3 + NADH
L-Ser + NAD+ + H2O
-
-
-
-
?
L-2-amino-4-pentenoate + H2O + NAD+
2-oxo-4-pentenoate + NH3 + NADH
-
-
-
?
L-2-amino-4-pentenoate + H2O + NAD+
2-oxo-4-pentenoate + NH3 + NADH
-
-
-
?
L-2-aminobutanoate + H2O + NAD+
2-oxobutanoate + NH3 + NADH + H+
-
-
-
-
?
L-2-aminobutanoate + H2O + NAD+
2-oxobutanoate + NH3 + NADH + H+
-
13.3% of the activity with L-Ala
-
r
L-2-aminobutanoate + H2O + NAD+
2-oxobutanoate + NH3 + NADH + H+
in the reverse reaction the enzyme reacts at 15.3% of the activity with pyruvate
-
-
r
L-2-aminobutanoate + H2O + NAD+
2-oxobutanoate + NH3 + NADH + H+
10.4% of the activity with L-Ala
-
-
r
L-2-aminobutanoate + H2O + NAD+
2-oxobutanoate + NH3 + NADH + H+
-
7.5% of the activity with L-Ala
-
r
L-2-aminobutanoate + H2O + NAD+
2-oxobutanoate + NH3 + NADH + H+
-
in the reverse reaction 2-oxobutanoate reacts with 79% of the activity with pyruvate
-
r
L-2-aminobutanoate + H2O + NAD+
2-oxobutanoate + NH3 + NADH + H+
-
-
-
r
L-2-aminobutanoate + H2O + NAD+
2-oxobutanoate + NH3 + NADH + H+
-
-
-
r
L-2-aminobutanoate + H2O + NAD+
2-oxobutanoate + NH3 + NADH + H+
-
8.7% of the activity with L-Ala
-
-
r
L-2-aminobutanoate + H2O + NAD+
2-oxobutanoate + NH3 + NADH + H+
-
in the reverse reaction 2-oxobutanoate reacts with 2.0% of the activity with pyruvate
-
-
r
L-2-aminobutanoate + H2O + NAD+
2-oxobutanoate + NH3 + NADH + H+
-
-
-
-
?
L-2-aminobutanoate + H2O + NAD+
2-oxobutanoate + NH3 + NADH + H+
-
-
-
r
L-2-aminobutanoate + H2O + NAD+
2-oxobutanoate + NH3 + NADH + H+
-
2.4% of the activity with L-Ala
-
-
?
L-2-aminobutanoate + H2O + NAD+
2-oxobutanoate + NH3 + NADH + H+
-
in the reverse reaction 2-oxobutanoate reacts with 1.2% of the activity with pyruvate
-
-
r
L-2-aminobutanoate + H2O + NAD+
2-oxobutanoate + NH3 + NADH + H+
-
0.7% of the activity with L-Ala
-
-
r
L-2-aminobutanoate + H2O + NAD+
2-oxobutanoate + NH3 + NADH + H+
-
1.6% of the activity with L-Ala
-
-
?
L-Ala + H2O + 1,N6-etheno-NAD+
pyruvate + NH3 + 1,N6-etheno-NADH
-
45% of the activity with NAD+
-
-
?
L-Ala + H2O + 1,N6-etheno-NAD+
pyruvate + NH3 + 1,N6-etheno-NADH
-
59% of the activity with NAD+
-
-
?
L-Ala + H2O + 3-acetylpyridine-NAD+
pyruvate + H2O + 3-acetylpyridine-NADH
-
as active as NAD+
-
-
?
L-Ala + H2O + 3-acetylpyridine-NAD+
pyruvate + H2O + 3-acetylpyridine-NADH
-
43% of the activity with NAD+
-
-
?
L-Ala + H2O + 3-acetylpyridine-NAD+
pyruvate + H2O + 3-acetylpyridine-NADH
-
62% of the activity with NAD+
-
-
?
L-Ala + H2O + deamino-NAD+
pyruvate + NH3 + deamino-NADH
-
90.2% of the activity with NAD+
-
-
?
L-Ala + H2O + deamino-NAD+
pyruvate + NH3 + deamino-NADH
-
4.4% of the activity with NAD+
-
-
?
L-Ala + H2O + deamino-NAD+
pyruvate + NH3 + deamino-NADH
-
77% of the activity with NAD+
-
-
?
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
-
-
r
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
-
-
r
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
-
-
r
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
highly specific for L-Ala
-
r
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
-
-
r
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
-
-
r
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
-
-
-
r
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
-
-
r
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
-
-
r
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
-
-
r
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
-
-
r
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
-
-
r
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
Bacillus japonicum
-
-
-
r
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
-
-
r
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
-
-
r
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
-
-
r
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
-
-
-
?
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
-
-
r
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
-
-
r
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
-
-
r
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
-
-
r
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
-
-
r
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
-
-
r
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
-
-
r
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
-
-
r
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
-
-
r
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
-
-
r
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
-
-
r
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
-
-
r
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
-
-
r
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
-
-
r
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
-
-
r
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
-
-
r
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
-
-
r
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
the physiological role is to catabolize L-Ala to pyruvate and NH3, inducible by L-Ala, D-Ala and 11 other D-amino acids. The enzyme catabolizes L-Ala, and thereby limits the amount of L-Ala available to alanine racemase for the synthesis of D-Ala
-
-
?
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
-
-
r
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
-
-
r
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
-
r
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
-
-
r
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
enzyme is involved in primary ammonium assimilation and the rapid formation of key metabolites pyruvate and NH3 from L-Ala and also in cell differentiation
-
-
?
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
-
-
r
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
-
-
r
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
absolutely specific for L-Ala in oxidative deamination
-
r
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
Desulforamulus ruminis
-
-
-
r
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
-
-
r
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
-
-
r
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
-
-
r
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
-
-
r
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
-
-
r
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
NH4+ assimilating enzyme
-
-
?
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
-
-
-
?
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
-
-
r
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
-
-
r
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
-
-
r
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
-
-
r
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
-
-
r
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
-
-
?
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
-
-
?
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
-
-
r
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
-
-
r
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
-
-
r
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
-
-
r
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
-
-
r
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
-
-
r
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
-
-
r
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
-
-
r
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
-
-
r
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
highly specific for L-Ala
-
r
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
physiological role in nitrogen metabolism in Streptomycetes
-
-
?
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
-
-
r
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
-
-
r
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
-
-
r
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
-
-
r
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
-
-
r
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
-
-
r
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
-
-
r
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
the reaction rate for deamination of pyruvate at the optimum is about 2.8times higher than that for amination of L-Ala at the optimum
-
r
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
specific for L-Ala
-
-
r
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
Micromonospora melanosporea
-
-
-
r
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
-
-
r
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
-
-
r
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
-
-
-
r
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
highly specific for L-Ala
-
r
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
since the physiological environment of the organism has a neutral pH, it can be assumed that the enzyme catalyzes exclusively the formation of L-Ala
-
-
?
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
Mycobacterium tuberculosis displays less Ald activity than the complemented Mycobacterium bovis BCG strain
-
-
?
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
-
-
r
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
-
-
r
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
-
-
r
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
enzyme is required for utilization of alanine as a sole nitrogen source, enzyme is required for optimal growth under anaerobic conditions
-
-
?
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
-
-
r
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
-
-
r
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
-
-
r
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
-
-
?
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
-
-
?
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
-
-
r
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
-
-
-
r
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
-
-
-
r
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
-
-
r
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
key enzyme in the metabolism of alanine, Ala is onyl fermented after lactate exhaustion and then at a slow rate
-
-
?
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
-
-
r
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
-
-
r
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
rate of the deaminating reaction is only 2.2% of the aminating reaction
-
r
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
role in NH3 assimilation and alanine catabolism
-
-
?
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
-
-
r
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
rate of the deaminating reaction is only 2.2% of the aminating reaction
-
r
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
role in NH3 assimilation and alanine catabolism
-
-
?
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
-
-
r
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
-
-
r
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
-
-
r
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
-
-
r
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
-
-
r
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
no function in NH4+-assimilation but rather is required to supply the cells with the appropriate quantities of organic carbon when the organism grows at the expense of L-Ala as C-source and N-source
-
-
?
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
alternative route for ammonia assimilation when glutamine synthetase is inactivated
-
-
?
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
involved in taurine catabolism
-
-
?
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
-
-
r
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
enzyme formation is effectively induced by Ala
-
-
?
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
NH4+ assimilating enzyme
-
-
?
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
-
-
-
?
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
-
-
r
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
-
-
r
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
-
-
?
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
-
-
r
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
-
-
-
?
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
-
-
?
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
-
-
r
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
-
-
r
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
-
-
r
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
-
-
r
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
-
-
r
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
-
-
r
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
-
-
r
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
-
-
r
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
-
-
r
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
-
-
r
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
-
-
r
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
-
-
r
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
-
-
r
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
-
-
r
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
-
-
r
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
-
-
r
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
-
-
r
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
-
-
r
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
-
-
r
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
-
-
-
r
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
-
-
-
r
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
-
-
r
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
highly specific for L-Ala
-
r
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
-
-
r
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
-
-
r
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
-
-
r
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
-
-
r
L-Ala + H2O + NADP+
pyruvate + NH3 + NADPH
-
7% of the activity with NAD+
-
-
?
L-Ala + H2O + NADP+
pyruvate + NH3 + NADPH
-
in the reverse direction NADPH reacts at 1.6% of the activity with NADH
-
-
r
L-Ala + H2O + NADP+
pyruvate + NH3 + NADPH
-
2.5% of the activity with NAD+
-
-
r
L-Ala + H2O + NADP+
pyruvate + NH3 + NADPH
wild-type enzyme and mutant enzyme R199I acts specifically on NAD+, mutant enzyme I198R is also active with NADP+
-
-
?
L-Ala + H2O + NADP+
pyruvate + NH3 + NADPH
wild-type enzyme and mutant enzyme R199I acts specifically on NAD+, mutant enzyme I198R is also active with NADP+
-
-
?
L-Ala + H2O + NADP+
pyruvate + NH3 + NADPH
-
wild-type enzyme shows high activity with NAD+ and low activity with NADP+. The mutant enzymes D198G, D198A, D198V and D198L show higher efficiency with NADP+ than with NAD+ as coenzyme
-
-
?
L-Ala + H2O + NADP+
pyruvate + NH3 + NADPH
-
wild-type enzyme shows high activity with NAD+ and low activity with NADP+. The mutant enzymes D198G, D198A, D198V and D198L show higher efficiency with NADP+ than with NAD+ as coenzyme
-
-
?
L-Ala + H2O + nicotinamide guanine dinucleotide
?
-
59.9% of the activity with NAD+
-
-
?
L-Ala + H2O + nicotinamide guanine dinucleotide
?
-
69.7% of the activity with NAD+
-
-
?
L-Ala + H2O + nicotinamide guanine dinucleotide
?
-
71% of the activity with NAD+
-
-
?
L-alanine + H2O + NAD+
pyruvate + NH3 + NADH + H+
Alkalihalophilus pseudofirmus
-
-
-
r
L-alanine + H2O + NAD+
pyruvate + NH3 + NADH + H+
Alkalihalophilus pseudofirmus ATCC BAA-2126
-
-
-
r
L-alanine + H2O + NAD+
pyruvate + NH3 + NADH + H+
Alkalihalophilus pseudofirmus JCM 17055
-
-
-
r
L-alanine + H2O + NAD+
pyruvate + NH3 + NADH + H+
Alkalihalophilus pseudofirmus OF4
-
-
-
r
L-alanine + H2O + NAD+
pyruvate + NH3 + NADH + H+
-
-
-
r
L-alanine + H2O + NAD+
pyruvate + NH3 + NADH + H+
-
-
-
?
L-alanine + H2O + NAD+
pyruvate + NH3 + NADH + H+
-
-
-
?
L-alanine + H2O + NAD+
pyruvate + NH3 + NADH + H+
-
-
-
?
L-alanine + H2O + NAD+
pyruvate + NH3 + NADH + H+
-
-
-
r
L-alanine + H2O + NAD+
pyruvate + NH3 + NADH + H+
-
-
-
?
L-alanine + H2O + NAD+
pyruvate + NH3 + NADH + H+
-
-
-
r
L-alanine + H2O + NAD+
pyruvate + NH3 + NADH + H+
-
-
-
r
L-alanine + H2O + NAD+
pyruvate + NH3 + NADH + H+
-
-
-
r
L-alanine + H2O + NAD+
pyruvate + NH3 + NADH + H+
-
-
-
r
L-alanine + H2O + NAD+
pyruvate + NH3 + NADH + H+
-
-
-
-
r
L-alanine + H2O + NAD+
pyruvate + NH3 + NADH + H+
-
-
-
-
r
L-alanine + H2O + NAD+
pyruvate + NH3 + NADH + H+
-
-
-
?
L-alanine + H2O + NAD+
pyruvate + NH3 + NADH + H+
-
-
-
-
?
L-alanine + H2O + NAD+
pyruvate + NH3 + NADH + H+
-
-
-
r
L-alanine + H2O + NAD+
pyruvate + NH3 + NADH + H+
-
-
-
r
L-alanine + H2O + NAD+
pyruvate + NH3 + NADH + H+
-
-
-
-
r
L-alanine + H2O + NAD+
pyruvate + NH3 + NADH + H+
-
-
-
?
L-alanine + H2O + NAD+
pyruvate + NH3 + NADH + H+
-
-
-
r
L-alanine + H2O + NAD+
pyruvate + NH3 + NADH + H+
-
-
-
r
L-alanine + H2O + NAD+
pyruvate + NH3 + NADH + H+
-
-
-
-
r
L-alanine + H2O + NAD+
pyruvate + NH3 + NADH + H+
-
-
-
r
L-alanine + H2O + NAD+
pyruvate + NH3 + NADH + H+
-
-
-
r
L-alanine + H2O + NAD+
pyruvate + NH3 + NADH + H+
-
-
-
?
L-alanine + H2O + NAD+
pyruvate + NH3 + NADH + H+
-
-
-
r
L-alanine + H2O + NAD+
pyruvate + NH3 + NADH + H+
-
-
-
r
L-alanine + H2O + NAD+
pyruvate + NH3 + NADH + H+
-
-
-
r
L-alanine + H2O + NAD+
pyruvate + NH3 + NADH + H+
-
-
-
r
L-alanine + H2O + NAD+
pyruvate + NH3 + NADH + H+
-
-
-
r
L-alanine + H2O + NAD+
pyruvate + NH3 + NADH + H+
reversible oxidative deamination and reductive amination reactions
-
-
r
L-alanine + H2O + NAD+
pyruvate + NH3 + NADH + H+
-
-
-
r
L-alanine + H2O + NAD+
pyruvate + NH3 + NADH + H+
reversible oxidative deamination and reductive amination reactions
-
-
r
L-alanine + H2O + NAD+
pyruvate + NH3 + NADH + H+
-
-
-
r
L-alanine + H2O + NAD+
pyruvate + NH3 + NADH + H+
reversible oxidative deamination and reductive amination reactions
-
-
r
L-alanine + H2O + NAD+
pyruvate + NH3 + NADH + H+
-
-
-
r
L-alanine + H2O + NAD+
pyruvate + NH3 + NADH + H+
reversible oxidative deamination and reductive amination reactions
-
-
r
L-alanine + H2O + NAD+
pyruvate + NH3 + NADH + H+
-
-
-
-
r
L-alanine + NAD+ + H2O
pyruvate + NH3 + NADH + H+
-
-
-
-
r
L-alanine + NAD+ + H2O
pyruvate + NH3 + NADH + H+
-
-
-
-
r
L-alanine + NAD+ + H2O
pyruvate + NH3 + NADH + H+
-
-
-
-
r
L-Ile + H2O + NAD+
2-oxo-3-methylpentanoate + NH3 + NADH
-
-
-
-
?
L-Ile + H2O + NAD+
2-oxo-3-methylpentanoate + NH3 + NADH
-
5% of the activity with L-Ala
-
-
?
L-Ile + H2O + NAD+
2-oxo-3-methylpentanoate + NH3 + NADH
-
-
-
?
L-Ile + H2O + NAD+
2-oxo-3-methylpentanoate + NH3 + NADH
-
0.1% of the activity with L-Ala
-
-
?
L-norvaline + H2O + NAD+
2-oxopentanoate + NH3 + NADH
-
-
-
-
?
L-norvaline + H2O + NAD+
2-oxopentanoate + NH3 + NADH
-
-
-
r
L-norvaline + H2O + NAD+
2-oxopentanoate + NH3 + NADH
at 4.6% of the activity with L-Ala
-
-
?
L-norvaline + H2O + NAD+
2-oxopentanoate + NH3 + NADH
-
1.5% of the activity with L-Ala
-
r
L-norvaline + H2O + NAD+
2-oxopentanoate + NH3 + NADH
-
in the reverse reaction 2-oxopentanoate reacts with 6.6% of the activity of pyruvate
-
r
L-norvaline + H2O + NAD+
2-oxopentanoate + NH3 + NADH
-
in the reverse reaction 2-oxopentanoate reacts with 0.12% of the activity of pyruvate
-
r
L-norvaline + H2O + NAD+
2-oxopentanoate + NH3 + NADH
-
-
-
-
r
L-norvaline + H2O + NAD+
2-oxopentanoate + NH3 + NADH
-
-
-
r
L-norvaline + H2O + NAD+
2-oxopentanoate + NH3 + NADH
-
-
-
?
L-norvaline + H2O + NAD+
2-oxopentanoate + NH3 + NADH
-
-
-
?
L-Ser + H2O + NAD+
3-hydroxypyruvate + NH3 + NADH
-
-
-
-
r
L-Ser + H2O + NAD+
3-hydroxypyruvate + NH3 + NADH
-
-
-
-
?
L-Ser + H2O + NAD+
3-hydroxypyruvate + NH3 + NADH
-
3.5% of the activity with L-Ala
-
r
L-Ser + H2O + NAD+
3-hydroxypyruvate + NH3 + NADH
-
in the reverse reaction 3-hydroxypyruvate reacts with 0.4% of the activity with pyruvate
-
r
L-Ser + H2O + NAD+
3-hydroxypyruvate + NH3 + NADH
-
in the reverse reaction 3-hydroxypyruvate reacts with 14.2% of the activity with pyruvate
-
-
r
L-Ser + H2O + NAD+
3-hydroxypyruvate + NH3 + NADH
-
4.1% of the activity with L-Ala
-
-
r
L-Ser + H2O + NAD+
3-hydroxypyruvate + NH3 + NADH
-
-
-
-
?
L-Ser + H2O + NAD+
3-hydroxypyruvate + NH3 + NADH
-
-
-
r
L-Ser + H2O + NAD+
3-hydroxypyruvate + NH3 + NADH
-
no activity
-
-
?
L-Ser + H2O + NAD+
3-hydroxypyruvate + NH3 + NADH
-
7.9% of the activity with L-Ala
-
-
?
L-Ser + H2O + NAD+
3-hydroxypyruvate + NH3 + NADH
-
no activity
-
-
?
L-Ser + H2O + NAD+
3-hydroxypyruvate + NH3 + NADH
-
2.4% of the activity with L-Ala
-
-
?
L-Ser + H2O + NAD+
3-hydroxypyruvate + NH3 + NADH
-
-
-
-
?
L-serine + H2O + NAD+
3-hydroxypyruvate + NH3 + NADH
-
-
-
?
L-serine + H2O + NAD+
3-hydroxypyruvate + NH3 + NADH
-
-
-
?
L-Val + H2O + NAD+
3-methyl-2-oxobutanoate + NH3 + NADH
-
-
-
-
?
L-Val + H2O + NAD+
3-methyl-2-oxobutanoate + NH3 + NADH
-
9% of the activity with L-Ala
-
-
?
L-Val + H2O + NAD+
3-methyl-2-oxobutanoate + NH3 + NADH
4.8% of the activity with L-Ala
-
-
?
L-Val + H2O + NAD+
3-methyl-2-oxobutanoate + NH3 + NADH
-
1.5% of the activity with L-Ala
-
-
?
L-Val + H2O + NAD+
3-methyl-2-oxobutanoate + NH3 + NADH
-
-
-
-
?
L-Val + H2O + NAD+
3-methyl-2-oxobutanoate + NH3 + NADH
-
0.2% of the activity with L-Ala
-
-
?
L-valine + H2O + NAD+
3-methyl-2-oxobutanoate + NH3 + NADH
-
-
-
?
L-valine + H2O + NAD+
3-methyl-2-oxobutanoate + NH3 + NADH
-
-
-
?
L-valine + H2O + NAD+
3-methyl-2-oxobutanoate + NH3 + NADH + H+
-
-
-
r
L-valine + H2O + NAD+
3-methyl-2-oxobutanoate + NH3 + NADH + H+
-
-
-
r
L-valine + H2O + NAD+
3-methyl-2-oxobutanoate + NH3 + NADH + H+
-
-
-
r
L-valine + H2O + NAD+
3-methyl-2-oxobutanoate + NH3 + NADH + H+
-
-
-
r
oxaloacetate + NH3 + NADH
L-Asp + H2O + NAD+
-
-
-
-
?
oxaloacetate + NH3 + NADH
L-Asp + H2O + NAD+
-
-
-
?
oxaloacetate + NH3 + NADH
L-Asp + H2O + NAD+
-
-
-
-
?
oxaloacetate + NH3 + NADH
L-Asp + H2O + NAD+
-
-
-
-
?
oxaloacetate + NH3 + NADH
L-Asp + H2O + NAD+
-
-
-
-
?
oxaloacetate + NH3 + NADH
L-Asp + H2O + NAD+
-
99% of the activity with pyruvate
-
-
?
oxaloacetate + NH3 + NADH
L-Asp + H2O + NAD+
-
94% of maximal activity
-
-
?
oxaloacetate + NH3 + NADH
L-Asp + H2O + NAD+
-
43.1% of the activity with pyruvate
-
-
?
pyruvate + NH3 + NADH
L-Ala + H2O + NAD+
-
-
-
?
pyruvate + NH3 + NADH
L-Ala + H2O + NAD+
-
-
-
r
pyruvate + NH3 + NADH
L-alanine + H2O + NAD+
-
-
-
?
pyruvate + NH3 + NADH
L-alanine + H2O + NAD+
the structural analysis leads to the identification of a water molecule which is hydrogen bonded to the active site His 96 and probably drives the conversion of the iminopyruvate intermediate to a carbinolamine
-
-
?
pyruvate + NH3 + NADH
L-alanine + H2O + NAD+
the structural analysis leads to the identification of a water molecule which is hydrogen bonded to the active site His 96 and probably drives the conversion of the iminopyruvate intermediate to a carbinolamine
-
-
?
pyruvate + NH3 + NADH + H+
L-alanine + H2O + NAD+
-
-
-
r
pyruvate + NH3 + NADH + H+
L-alanine + H2O + NAD+
-
-
-
r
pyruvate + NH3 + NADH + H+
L-alanine + H2O + NAD+
-
-
-
-
?
pyruvate + NH3 + NADH + H+
L-alanine + H2O + NAD+
-
-
-
-
?
pyruvate + NH3 + NADH + H+
L-alanine + H2O + NAD+
-
-
-
r
pyruvate + NH3 + NADH + H+
L-alanine + H2O + NAD+
-
-
-
-
r
pyruvate + NH3 + NADH + H+
L-alanine + H2O + NAD+
-
-
-
-
r
pyruvate + NH3 + NADH + H+
L-alanine + H2O + NAD+
-
-
-
r
additional information
?
-
Alkalihalophilus pseudofirmus
the activity assay includes L-alanine, NAD+, phenazine methosulfate and 0.24 mM nitroblue tetrazolium in carbonate buffer (50 mn, pH 10.5)
-
-
-
additional information
?
-
Alkalihalophilus pseudofirmus ATCC BAA-2126
the activity assay includes L-alanine, NAD+, phenazine methosulfate and 0.24 mM nitroblue tetrazolium in carbonate buffer (50 mn, pH 10.5)
-
-
-
additional information
?
-
Alkalihalophilus pseudofirmus JCM 17055
the activity assay includes L-alanine, NAD+, phenazine methosulfate and 0.24 mM nitroblue tetrazolium in carbonate buffer (50 mn, pH 10.5)
-
-
-
additional information
?
-
Alkalihalophilus pseudofirmus OF4
the activity assay includes L-alanine, NAD+, phenazine methosulfate and 0.24 mM nitroblue tetrazolium in carbonate buffer (50 mn, pH 10.5)
-
-
-
additional information
?
-
-
Aspecific enzyme with regard to stereochemistry of the hydrogen transfer to NAD+
-
-
?
additional information
?
-
-
the enzyme is required for normal sporulation
-
-
?
additional information
?
-
-
transfer of hydride is a partially limiting step and the reaction rate is limited by the release of product NADH. The fluorine constituent doesn't cause a significant change in the area of bonds that are being converted, and deuteriated solvent present in the reaction medium only slightly affects the conversion of [E-S] complex into [E-P] complex
-
-
?
additional information
?
-
one-pot preparation of D-amino acids through biocatalytic deracemization using alanine dehydrogenase and omega-transaminase. AlaDH produces pyruvate from L-alanine with NAD+, NOX oxidizes NADH to NAD+, and reductive amination of the resulting pyruvate back to the amino acid in an enantiomerically opposite form by D-selective omega-transaminase (omega-TA) using isopropylamine as an amino donor cosubstrate
-
-
-
additional information
?
-
one-pot preparation of D-amino acids through biocatalytic deracemization using alanine dehydrogenase and omega-transaminase. AlaDH produces pyruvate from L-alanine with NAD+, NOX oxidizes NADH to NAD+, and reductive amination of the resulting pyruvate back to the amino acid in an enantiomerically opposite form by D-selective omega-transaminase (omega-TA) using isopropylamine as an amino donor cosubstrate
-
-
-
additional information
?
-
no activity with taurine
-
-
?
additional information
?
-
-
no activity with taurine
-
-
?
additional information
?
-
enzyme is involved in taurine metabolism
-
-
?
additional information
?
-
-
enzyme is involved in taurine metabolism
-
-
?
additional information
?
-
-
circadian oscillations in alanine dehydrogenase
-
-
?
additional information
?
-
-
circadian oscillations in alanine dehydrogenase
-
-
?
additional information
?
-
isozyme HAADH2 has no oxidation activity for 20 amino acids, 3-fluoroalanine, D/L-lactic acid, D/L -DOPA and L-2-aminobutyric acid. It also has no reduction activity for all tested 2-oxo acids
-
-
-
additional information
?
-
isozyme HAADH2 has no oxidation activity for 20 amino acids, 3-fluoroalanine, D/L-lactic acid, D/L -DOPA and L-2-aminobutyric acid. It also has no reduction activity for all tested 2-oxo acids
-
-
-
additional information
?
-
-
isozyme HAADH2 has no oxidation activity for 20 amino acids, 3-fluoroalanine, D/L-lactic acid, D/L -DOPA and L-2-aminobutyric acid. It also has no reduction activity for all tested 2-oxo acids
-
-
-
additional information
?
-
L-alanine and pyruvate are the preferred substrates of the enzyme for the deamination and amination reaction, respectively. Oxaloacetate, 2-oxobutyrate, 3-fluoropyruvate, 2-oxoglutarate, and glyoxylate show 93.30%, 8.93%, 5.62%, 2.57%, 2.51% activity compared to pyruvate, respectively
-
-
-
additional information
?
-
L-alanine and pyruvate are the preferred substrates of the enzyme for the deamination and amination reaction, respectively. Oxaloacetate, 2-oxobutyrate, 3-fluoropyruvate, 2-oxoglutarate, and glyoxylate show 93.30%, 8.93%, 5.62%, 2.57%, 2.51% activity compared to pyruvate, respectively
-
-
-
additional information
?
-
-
L-alanine and pyruvate are the preferred substrates of the enzyme for the deamination and amination reaction, respectively. Oxaloacetate, 2-oxobutyrate, 3-fluoropyruvate, 2-oxoglutarate, and glyoxylate show 93.30%, 8.93%, 5.62%, 2.57%, 2.51% activity compared to pyruvate, respectively
-
-
-
additional information
?
-
-
enzyme Ald has both pyruvate and glyoxylate aminating activities
-
-
?
additional information
?
-
Ald catalyzes the reductive amination reaction faster and more efficiently than the oxidative deamination reaction
-
-
-
additional information
?
-
-
Ald catalyzes the reductive amination reaction faster and more efficiently than the oxidative deamination reaction
-
-
-
additional information
?
-
Ald catalyzes the reductive amination reaction faster and more efficiently than the oxidative deamination reaction
-
-
-
additional information
?
-
-
enzyme Ald has both pyruvate and glyoxylate aminating activities
-
-
?
additional information
?
-
Ald catalyzes the reductive amination reaction faster and more efficiently than the oxidative deamination reaction
-
-
-
additional information
?
-
-
strong induction immediately after deflection from aerobic growth suggests that alanine dehydrogenase may be required for the adaption from aerobic growth to anaerobic dormacy, the induction of alanine dehydrogenase may also support the maintenance of the NAD+ pool when oxygen as the terminal electron acceptor becomes limiting
-
-
?
additional information
?
-
an enzymatic assay system to eliminate or measure D-Ala is constructed using alanine racemase (L-AlaR from Synechocystis sp. PCC6803) and L-alanine dehydrogenase (L-AlaDH from Phormidium lapideum). D-Ala is converted to L-Ala by alanine racemase and then deaminated by L-alanine dehydrogenase with the reduction of NAD+ to NADH, which is determined with water-soluble tetrazolium. NADH nonenzymatically reduces WST-1 to form water soluble formazan.Using the assay system, the D-Ala contents of 7 crustaceans are determined. Method evaluation, overview
-
-
-
additional information
?
-
the enzyme is induced by carboxylic acids (succinate, malate and pyruvate), although the best induer is alanine. The role of the enzyme may be to balance the alanine level for optimal functioning of bacteroid metabolism rather than to synthesize alanine as the sole product of N2 reduction
-
-
?
additional information
?
-
the enzyme is induced by carboxylic acids (succinate, malate and pyruvate), although the best induer is alanine. The role of the enzyme may be to balance the alanine level for optimal functioning of bacteroid metabolism rather than to synthesize alanine as the sole product of N2 reduction
-
-
?
additional information
?
-
-
important role in biosynthesis of erythromycin
-
-
?
additional information
?
-
the natural substrates of ALD enzymes for oxidative deamination and reductive amination reactions are believed to be L-alanine and pyruvate, respectively
-
-
-
additional information
?
-
-
the natural substrates of ALD enzymes for oxidative deamination and reductive amination reactions are believed to be L-alanine and pyruvate, respectively
-
-
-
additional information
?
-
substrate specificity of ScALD: in the reductive amination reaction the enzyme shows low activity with 3-hydroxypyruvate, and glyoxylate, higher activity with 2-oxobutyrate and 2-oxovalerate, best substrate is pyruvate. In the oxidative deamination reaction, ScALD shows low activity with L-2-aminobutyrate, L-serine, L-valine, and L-norvaline, and highest activity with substrate L-alanine. No activity with D-alanine
-
-
-
additional information
?
-
-
substrate specificity of ScALD: in the reductive amination reaction the enzyme shows low activity with 3-hydroxypyruvate, and glyoxylate, higher activity with 2-oxobutyrate and 2-oxovalerate, best substrate is pyruvate. In the oxidative deamination reaction, ScALD shows low activity with L-2-aminobutyrate, L-serine, L-valine, and L-norvaline, and highest activity with substrate L-alanine. No activity with D-alanine
-
-
-
additional information
?
-
the natural substrates of ALD enzymes for oxidative deamination and reductive amination reactions are believed to be L-alanine and pyruvate, respectively
-
-
-
additional information
?
-
-
the natural substrates of ALD enzymes for oxidative deamination and reductive amination reactions are believed to be L-alanine and pyruvate, respectively
-
-
-
additional information
?
-
substrate specificity of ScALD: in the reductive amination reaction the enzyme shows low activity with 3-hydroxypyruvate, and glyoxylate, higher activity with 2-oxobutyrate and 2-oxovalerate, best substrate is pyruvate. In the oxidative deamination reaction, ScALD shows low activity with L-2-aminobutyrate, L-serine, L-valine, and L-norvaline, and highest activity with substrate L-alanine. No activity with D-alanine
-
-
-
additional information
?
-
-
substrate specificity of ScALD: in the reductive amination reaction the enzyme shows low activity with 3-hydroxypyruvate, and glyoxylate, higher activity with 2-oxobutyrate and 2-oxovalerate, best substrate is pyruvate. In the oxidative deamination reaction, ScALD shows low activity with L-2-aminobutyrate, L-serine, L-valine, and L-norvaline, and highest activity with substrate L-alanine. No activity with D-alanine
-
-
-
additional information
?
-
the natural substrates of ALD enzymes for oxidative deamination and reductive amination reactions are believed to be L-alanine and pyruvate, respectively
-
-
-
additional information
?
-
substrate specificity of ScALD: in the reductive amination reaction the enzyme shows low activity with 3-hydroxypyruvate, and glyoxylate, higher activity with 2-oxobutyrate and 2-oxovalerate, best substrate is pyruvate. In the oxidative deamination reaction, ScALD shows low activity with L-2-aminobutyrate, L-serine, L-valine, and L-norvaline, and highest activity with substrate L-alanine. No activity with D-alanine
-
-
-
additional information
?
-
the natural substrates of ALD enzymes for oxidative deamination and reductive amination reactions are believed to be L-alanine and pyruvate, respectively
-
-
-
additional information
?
-
substrate specificity of ScALD: in the reductive amination reaction the enzyme shows low activity with 3-hydroxypyruvate, and glyoxylate, higher activity with 2-oxobutyrate and 2-oxovalerate, best substrate is pyruvate. In the oxidative deamination reaction, ScALD shows low activity with L-2-aminobutyrate, L-serine, L-valine, and L-norvaline, and highest activity with substrate L-alanine. No activity with D-alanine
-
-
-
additional information
?
-
-
enzyme activity during production phase of the antibiotic A 6599, enzyme induction by an excess of alanine or ammonia
-
-
?
additional information
?
-
-
substrate specifiicty, overview. The enzyme is also active with substrates DL-alanine, L-serine, L-isoleucine, L-threonine, and glycine, with L-serine giving the highest activity rate
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
DL-alanine + H2O + NAD+
pyruvate + NH3 + NADH + H+
-
-
-
-
r
glycine + H2O + NAD+
glyoxylate + NH3 + NADH + H+
-
-
-
-
r
glyoxylate + NH3 + NADH + H+
glycine + H2O + NAD+
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
L-alanine + H2O + NAD+
pyruvate + NH3 + NADH + H+
L-alanine + NAD+ + H2O
pyruvate + NH3 + NADH + H+
L-isoleucine + H2O + NAD+
2-oxo-3-methylpentanoate + NH3 + NADH + H+
-
-
-
-
r
L-serine + H2O + NAD+
3-hydroxypyruvate + NH3 + NADH + NH3 + NADH + H+
-
-
-
-
r
L-threonine + H2O + NAD+
3-hydroxy-2-oxobutyrate + NH3 + NADH + H+
-
-
-
-
r
pyruvate + NH3 + NADH
L-Ala + NAD+ + H2O
-
primary route for alanine synthesis in isolated bacteroids, alanine synthesis and secretion contributes to the efficiency of N2-fixation and therefore biomass accumulation
-
-
?
pyruvate + NH3 + NADH + H+
L-alanine + H2O + NAD+
additional information
?
-
glyoxylate + NH3 + NADH + H+
glycine + H2O + NAD+
-
-
-
ir
glyoxylate + NH3 + NADH + H+
glycine + H2O + NAD+
-
-
-
ir
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
the physiological role is to catabolize L-Ala to pyruvate and NH3, inducible by L-Ala, D-Ala and 11 other D-amino acids. The enzyme catabolizes L-Ala, and thereby limits the amount of L-Ala available to alanine racemase for the synthesis of D-Ala
-
-
?
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
enzyme is involved in primary ammonium assimilation and the rapid formation of key metabolites pyruvate and NH3 from L-Ala and also in cell differentiation
-
-
?
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
NH4+ assimilating enzyme
-
-
?
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
-
-
-
?
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
physiological role in nitrogen metabolism in Streptomycetes
-
-
?
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
since the physiological environment of the organism has a neutral pH, it can be assumed that the enzyme catalyzes exclusively the formation of L-Ala
-
-
?
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
enzyme is required for utilization of alanine as a sole nitrogen source, enzyme is required for optimal growth under anaerobic conditions
-
-
?
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
key enzyme in the metabolism of alanine, Ala is onyl fermented after lactate exhaustion and then at a slow rate
-
-
?
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
role in NH3 assimilation and alanine catabolism
-
-
?
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
role in NH3 assimilation and alanine catabolism
-
-
?
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
no function in NH4+-assimilation but rather is required to supply the cells with the appropriate quantities of organic carbon when the organism grows at the expense of L-Ala as C-source and N-source
-
-
?
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
alternative route for ammonia assimilation when glutamine synthetase is inactivated
-
-
?
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
involved in taurine catabolism
-
-
?
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
enzyme formation is effectively induced by Ala
-
-
?
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
NH4+ assimilating enzyme
-
-
?
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
-
-
?
L-Ala + H2O + NAD+
pyruvate + NH3 + NADH
-
-
-
?
L-alanine + H2O + NAD+
pyruvate + NH3 + NADH + H+
Alkalihalophilus pseudofirmus
-
-
-
r
L-alanine + H2O + NAD+
pyruvate + NH3 + NADH + H+
Alkalihalophilus pseudofirmus ATCC BAA-2126
-
-
-
r
L-alanine + H2O + NAD+
pyruvate + NH3 + NADH + H+
Alkalihalophilus pseudofirmus JCM 17055
-
-
-
r
L-alanine + H2O + NAD+
pyruvate + NH3 + NADH + H+
Alkalihalophilus pseudofirmus OF4
-
-
-
r
L-alanine + H2O + NAD+
pyruvate + NH3 + NADH + H+
-
-
-
r
L-alanine + H2O + NAD+
pyruvate + NH3 + NADH + H+
-
-
-
?
L-alanine + H2O + NAD+
pyruvate + NH3 + NADH + H+
-
-
-
?
L-alanine + H2O + NAD+
pyruvate + NH3 + NADH + H+
-
-
-
?
L-alanine + H2O + NAD+
pyruvate + NH3 + NADH + H+
-
-
-
r
L-alanine + H2O + NAD+
pyruvate + NH3 + NADH + H+
-
-
-
?
L-alanine + H2O + NAD+
pyruvate + NH3 + NADH + H+
-
-
-
r
L-alanine + H2O + NAD+
pyruvate + NH3 + NADH + H+
-
-
-
r
L-alanine + H2O + NAD+
pyruvate + NH3 + NADH + H+
-
-
-
r
L-alanine + H2O + NAD+
pyruvate + NH3 + NADH + H+
-
-
-
r
L-alanine + H2O + NAD+
pyruvate + NH3 + NADH + H+
-
-
-
-
r
L-alanine + H2O + NAD+
pyruvate + NH3 + NADH + H+
-
-
-
-
r
L-alanine + H2O + NAD+
pyruvate + NH3 + NADH + H+
-
-
-
r
L-alanine + H2O + NAD+
pyruvate + NH3 + NADH + H+
-
-
-
r
L-alanine + H2O + NAD+
pyruvate + NH3 + NADH + H+
-
-
-
-
r
L-alanine + H2O + NAD+
pyruvate + NH3 + NADH + H+
-
-
-
r
L-alanine + H2O + NAD+
pyruvate + NH3 + NADH + H+
-
-
-
r
L-alanine + H2O + NAD+
pyruvate + NH3 + NADH + H+
-
-
-
-
r
L-alanine + H2O + NAD+
pyruvate + NH3 + NADH + H+
-
-
-
r
L-alanine + H2O + NAD+
pyruvate + NH3 + NADH + H+
-
-
-
r
L-alanine + H2O + NAD+
pyruvate + NH3 + NADH + H+
-
-
-
?
L-alanine + H2O + NAD+
pyruvate + NH3 + NADH + H+
-
-
-
r
L-alanine + H2O + NAD+
pyruvate + NH3 + NADH + H+
-
-
-
r
L-alanine + H2O + NAD+
pyruvate + NH3 + NADH + H+
-
-
-
r
L-alanine + H2O + NAD+
pyruvate + NH3 + NADH + H+
-
-
-
r
L-alanine + H2O + NAD+
pyruvate + NH3 + NADH + H+
-
-
-
r
L-alanine + H2O + NAD+
pyruvate + NH3 + NADH + H+
-
-
-
r
L-alanine + H2O + NAD+
pyruvate + NH3 + NADH + H+
-
-
-
r
L-alanine + H2O + NAD+
pyruvate + NH3 + NADH + H+
-
-
-
r
L-alanine + H2O + NAD+
pyruvate + NH3 + NADH + H+
-
-
-
-
r
L-alanine + NAD+ + H2O
pyruvate + NH3 + NADH + H+
-
-
-
-
r
L-alanine + NAD+ + H2O
pyruvate + NH3 + NADH + H+
-
-
-
-
r
L-alanine + NAD+ + H2O
pyruvate + NH3 + NADH + H+
-
-
-
-
r
pyruvate + NH3 + NADH + H+
L-alanine + H2O + NAD+
-
-
-
r
pyruvate + NH3 + NADH + H+
L-alanine + H2O + NAD+
-
-
-
r
pyruvate + NH3 + NADH + H+
L-alanine + H2O + NAD+
-
-
-
-
?
pyruvate + NH3 + NADH + H+
L-alanine + H2O + NAD+
-
-
-
-
?
pyruvate + NH3 + NADH + H+
L-alanine + H2O + NAD+
-
-
-
-
r
pyruvate + NH3 + NADH + H+
L-alanine + H2O + NAD+
-
-
-
-
r
additional information
?
-
-
the enzyme is required for normal sporulation
-
-
?
additional information
?
-
enzyme is involved in taurine metabolism
-
-
?
additional information
?
-
-
enzyme is involved in taurine metabolism
-
-
?
additional information
?
-
-
circadian oscillations in alanine dehydrogenase
-
-
?
additional information
?
-
-
circadian oscillations in alanine dehydrogenase
-
-
?
additional information
?
-
-
enzyme Ald has both pyruvate and glyoxylate aminating activities
-
-
?
additional information
?
-
-
enzyme Ald has both pyruvate and glyoxylate aminating activities
-
-
?
additional information
?
-
-
strong induction immediately after deflection from aerobic growth suggests that alanine dehydrogenase may be required for the adaption from aerobic growth to anaerobic dormacy, the induction of alanine dehydrogenase may also support the maintenance of the NAD+ pool when oxygen as the terminal electron acceptor becomes limiting
-
-
?
additional information
?
-
the enzyme is induced by carboxylic acids (succinate, malate and pyruvate), although the best induer is alanine. The role of the enzyme may be to balance the alanine level for optimal functioning of bacteroid metabolism rather than to synthesize alanine as the sole product of N2 reduction
-
-
?
additional information
?
-
the enzyme is induced by carboxylic acids (succinate, malate and pyruvate), although the best induer is alanine. The role of the enzyme may be to balance the alanine level for optimal functioning of bacteroid metabolism rather than to synthesize alanine as the sole product of N2 reduction
-
-
?
additional information
?
-
-
important role in biosynthesis of erythromycin
-
-
?
additional information
?
-
the natural substrates of ALD enzymes for oxidative deamination and reductive amination reactions are believed to be L-alanine and pyruvate, respectively
-
-
-
additional information
?
-
-
the natural substrates of ALD enzymes for oxidative deamination and reductive amination reactions are believed to be L-alanine and pyruvate, respectively
-
-
-
additional information
?
-
the natural substrates of ALD enzymes for oxidative deamination and reductive amination reactions are believed to be L-alanine and pyruvate, respectively
-
-
-
additional information
?
-
-
the natural substrates of ALD enzymes for oxidative deamination and reductive amination reactions are believed to be L-alanine and pyruvate, respectively
-
-
-
additional information
?
-
the natural substrates of ALD enzymes for oxidative deamination and reductive amination reactions are believed to be L-alanine and pyruvate, respectively
-
-
-
additional information
?
-
the natural substrates of ALD enzymes for oxidative deamination and reductive amination reactions are believed to be L-alanine and pyruvate, respectively
-
-
-
additional information
?
-
-
enzyme activity during production phase of the antibiotic A 6599, enzyme induction by an excess of alanine or ammonia
-
-
?
additional information
?
-
-
substrate specifiicty, overview. The enzyme is also active with substrates DL-alanine, L-serine, L-isoleucine, L-threonine, and glycine, with L-serine giving the highest activity rate
-
-
?
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1-(isonicotinamido)-N2,N4-bis(benzo[d]thiazol-2-yl)azetidine-2,4-dicarboxamide
1-(isonicotinamido)-N2,N4-bis(phenyl)azetidine-2,4-dicarboxamide
lead compound for inhibitor screening, involved in hydrophobic interactions with residues Pro242, Val241, Ala176, Leu130, Ile267, Ala179, Ile199 and Ile174
2,4,6-Trinitrobenzenesulfonic acid
-
inactivation follows pseudo first-order kinetics with a 1:1 stoichiometric ratio between the reagent and the enzyme subunit. Partial protection by each of the substrates, NADH or pyruvate. Complete protection only in presence of the ternary complex enzyme-NADH-pyruvate
2-ethyl-N-phenethyl-5,6,7,8-tetrahydrobenzo[4,5]thieno[2,3-d]pyrimidin-4-amine
the molecule shows activity against nutrient-starved nonreplicating Mycobacterium tuberculosis, resulting in a 2.7 log reduction of bacterial loads at 0.010 mg/ml, and is shown to be more potent than the first-line antitubercular drugs, isoniazid and rifampicin, at the same dose. compound is cytotoxic
-
3-(2-pyridyldithio)propionate
-
inactivation follows pseudo first-order kinetics with a 1:1 stoichiometric ratio between the reagent and the enzyme subunit. Partial protection by each of the substrates, NADH or pyruvate. Complete protection only in presence of the ternary complex enzyme-NADH-pyruvate
3-hydroxypyruvate
-
competitive with respect to pyruvate
4-(furan-2-ylmethylene)-1-phenylpyrazolidine-3,5-dione
the compound exhibited potent antitubercular activity against log-phase cultures of Mycobacterium tuberculosis with a MIC of 0.0245 mM, but is found to be less active than the lead compound 1-(4-chlorophenyl)-4-(4-hydroxy-3-methoxy-5-nitrobenzylidene) pyrazolidine-3,5-dione (CD59). The compound is cytotoxic
-
5'-(p-(fluorosulfonyl)-benzoyl)adenosine
-
inactivation follows pseudo-first-order kinetics, complete inactivation of the enzyme can not be obtained even at high reagent concentration
5,5'-dithiobis(2-nitrobenzoate)
-
-
5-(4-(benzyloxy)benzylidene)-3-(2,5-dimethylphenyl)-2-iminothiazolidin-4-one
compound shows potency, selectivity, and no cytotoxicity up to 50 microM in a mouse macrophage cell line
5-(4-(benzyloxy)benzylidene)-3-(2,6-dimethylphenyl)-2-iminothiazolidin-4-one
compound shows potency, selectivity, and no cytotoxicity up to 50 microM in a mouse macrophage cell line
6-acetyl-2-(4-chlorobenzamido)-4,5,6,7-tetrahydrothieno[2,3-c]pyridine-3-carboxamide
compound shows potency, selectivity, and no cytotoxicity up to 50 microM in a mouse macrophage cell line
AgNO3
-
0.1 mM, 57% inhibition
Ca2+
Alkalihalophilus pseudofirmus
80% inhibition at 10 mM, 71% at 1 mM, 21% at 0.1 mM
Cibacron blue F3GA
0.1 mM, 70% inhibition
D-alanine
AlaDH enzyme activity is completely inhibited by D-alanine in a competitive manner
DTNB
7% inhibition with 0.01 M and 40% inhibition with 0.1 mM
DTT
Alkalihalophilus pseudofirmus
39% inhibition at 10 mM
Fe3+
-
10 mM, 85% inhibition of reductive amination
KCl
slightly enhances PvRA activity and it moderately promotes ALD activity. In contrast, increasing amounts of KCl gradually inhibits GxRA activity
L-alanine
the PvRA activity of ApAlaDH is strongly inhibited by 2 mM L-alanine, 68% inhibition. The GxRA activity is completely inhibited in the presence of L-alanine (100% inhibition at 10 and 20 mM L-alanine)
L-Phe
-
reductive amination of pyruvate, 10 mM, 28% inhibition
L-Trp
-
reductive amination of pyruvate, 10 mM, 29% inhibition
methyl p-nitrobenzenesulfonate
0.1 mM, complete inhibition
MnSO4
-
10 mM, 50% inhibition
NaCl
NaCl does not inhibit PvRA activity up to 1 M, but inhibition is observed at 2.5 M. The activities of ALD and GxRA are significantly increased in the presence of NaCl at concentrations of 0.1-0.25 M
NADPH
-
inhibition of reductive amination
Ni2+
-
10 mM, 60% inhibition of reductive amination
p-hydroxymercuribenzoate
-
no effect on aminating activity, inhibition of deaminating activity
pyridoxal 5'-phosphate
-
-
tert-butyl 3-carbamoyl-2-(4-chlorobenzamido)-4,5-dihydrothieno[2,3-c]pyridine-6(7H)-carboxylate
compound shows potency, selectivity, and no cytotoxicity up to 50 microM in a mouse macrophage cell line
1-(isonicotinamido)-N2,N4-bis(benzo[d]thiazol-2-yl)azetidine-2,4-dicarboxamide
compound shows 100fold reduction in nutrient starved dormant Mycobacterium tuberculosis model and MIC of 11.81 microM in actively replicative Mycobacterium tuberculosis
1-(isonicotinamido)-N2,N4-bis(benzo[d]thiazol-2-yl)azetidine-2,4-dicarboxamide
-
CaCl2
-
10 mM, 22% inhibition
CaCl2
1 mM, 15% inhibition
Cd2+
-
10 mM, 36% inhibition of reductive amination
Cibacron blue
-
-
Co2+
Alkalihalophilus pseudofirmus
complete inhibition at 10 mM, 27% at 0.1 mM
Co2+
-
10 mM, 60% inhibition of reductive amination
Co2+
-
17% inhibition at 10 mM, 23.75% at 20 mM
CoCl2
-
0.1 mM, 53% inhibition
Cu2+
Alkalihalophilus pseudofirmus
complete inhibition at 10 mM, 34% at 0.1 mM
Cu2+
-
10 mM, 60% inhibition of reductive amination
CuCl2
-
1 mM, 52% inhibition
CuSO4
-
10 mM, 36% inhibition
CuSO4
-
50.7% inhibition by 1 mM, 96.3% inhibition by 20 mM, EDTA in a 10fold molar excess restores activity almost completely, recombinant enzyme
D-Ala
-
-
D-Ala
-
aminating reaction, competitive with respect to NADH, noncompetitive with respect to NH4+ and pyruvate
D-Cys
-
-
EDTA
Alkalihalophilus pseudofirmus
34% inhibition at 10 mM
Fe2+
-
10 mM, 85% inhibition of reductive amination
glycine
-
-
glycine
GxRA activity is inhibited by 60% in presence of 20 mM glycine, but glycine does not inhibit the PvRA activity
Hg2+
-
-
HgCl2
-
0.003 mM, complete inhibition
HgCl2
-
1 mM, 38% inhibition
HgCl2
complete inhibition
HgCl2
1 mM, complete inhibition
Hydroxypyruvate
-
-
iodoacetate
-
-
iodoacetate
-
23.75% inhibition at 10 mM
L-Ala
-
-
L-Ala
-
reductive amination of pyruvate
L-Ala
-
uncompetitive inhibition with respect to NADH
L-Ala
-
substrate inhibition
L-Ala
-
5 mM, 34% inhibition
L-Ala
-
reductive amination of pyruvate
L-Cys
-
-
L-Cys
10 mM, 40% inhibition
L-Ser
-
-
L-Ser
-
inhibition of aminating activity
L-Ser
-
inhibition of aminating activity
L-Ser
-
reductive amination of pyruvate
L-Ser
-
10 mM, 26% inhibition; inhibition of aminating activity
L-Ser
-
inhibition of aminating activity
L-Thr
-
inhibition of aminating activity
L-Thr
-
reductive amination of pyruvate, 10 mM, 37% inhibition
Mercurials
-
-
-
MgCl2
-
inhibitory at a concentration above 2.13 mM
Mn2+
Alkalihalophilus pseudofirmus
complete inhibition at 10 mM, 25% at 1 mM
Mn2+
-
10 mM, 60% inhibition of reductive amination
MnCl2
-
10 mM, 12% inhibition
MnCl2
1 mM, 10% inhibition
NAD+
-
product inhibition
NAD+
-
0.1 mM, 35% inhibition
NADH
-
-
NADH
-
product inhibition
NADH
-
product inhibition
NH4+
-
-
NH4+
-
product inhibition
NH4+
-
inhibition of aminating activity
Pb2+
Alkalihalophilus pseudofirmus
protein OF4Ald completely loses its activity in the presence of 0.1-10 mM Pb2+
PCMB
-
-
PCMB
-
0.3 mM, 52% inhibition
PCMB
0.1 mM, 97% inhibition
pyruvate
the ALD activity of ApAlaDH is strongly inhibited by 2 mM L-alanine, 45% inhibition
pyruvate
-
product inhibition
pyruvate
-
substrate inhibition
pyruvate
-
inhibition at pH 7.5 greater than at pH 9.5; product inhibition
pyruvate
-
substrate inhibition
pyruvate
-
product inhibition
Zn2+
-
-
Zn2+
-
10 mM, 62% inhibition
Zn2+
-
allosteric competitive inhibitor, reversible, inducing conformational change through the intersubunit interaction, positive cooperative binding of the substrate in presence of Zn2+
Zn2+
-
26.5% inhibition by 1 mM ZnCl2, 90.1% inhibition by 20 mM ZnCl2, EDTA in a 10fold molar excess restores activity almost completely, recombinant enzyme
Zn2+
-
57% inhibition at 10 mM, 72.75% at 20 mM
additional information
all enzyme reactions are inhibited to varying degrees by their products
-
additional information
-
all enzyme reactions are inhibited to varying degrees by their products
-
additional information
development and optimization of compounds that inhibits the enzyme and can act as anti-tuberculosis drug, overview
-
additional information
-
development and optimization of compounds that inhibits the enzyme and can act as anti-tuberculosis drug, overview
-
additional information
no inhibition by L-serine and L-valine
-
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0.61
2-oxobutyrate
pH 9.0, 30°C, reductive amination reaction
0.032
3-hydroxypyruvate
pH 9.0, 30°C, reductive amination reaction
0.11
3-oxovalerate
pH 9.0, 30°C, reductive amination reaction
0.041
glyoxylate
pH 9.0, 30°C, reductive amination reaction
0.0015 - 0.005
L-2-amino-4-pentenoate
0.06
L-2-aminobutyrate
pH 9.0, 30°C, reductive amination reaction
0.019 - 0.037
L-homophenylalanine
0.015
L-homoserine
wild-type, pH 10.2, temperature not specified in the publication
0.00088 - 0.0027
L-leucine
0.0016 - 0.0026
L-methionine
0.006 - 0.013
L-norleucine
0.0004 - 0.04
L-norvaline
0.0015
L-2-amino-4-pentenoate
wild-type, pH 10.2, temperature not specified in the publication
0.004
L-2-amino-4-pentenoate
mutant F94S, pH 10.2, temperature not specified in the publication
0.005
L-2-amino-4-pentenoate
mutant F94S/Y117L, pH 10.2, temperature not specified in the publication
0.00035
L-alanine
mutant F94S/Y117L, pH 10.2, temperature not specified in the publication
0.0022
L-alanine
mutant F94S, pH 10.2, temperature not specified in the publication
0.67
L-alanine
Alkalihalophilus pseudofirmus
recombinant His-tagged mutant K73Q, pH 10.5, 40°C
1
L-alanine
Alkalihalophilus pseudofirmus
recombinant His-tagged mutants K73R, K73S, and K73F, pH 10.5, 40°C
1.33
L-alanine
Alkalihalophilus pseudofirmus
recombinant His-tagged mutant K73Y, pH 10.5, 40°C
1.4
L-alanine
wild-type, pH 10.2, temperature not specified in the publication
1.5
L-alanine
Alkalihalophilus pseudofirmus
recombinant His-tagged mutant K73E, pH 10.5, 40°C
2
L-alanine
pH 9.0, 30°C, reductive amination reaction
2.5
L-alanine
Alkalihalophilus pseudofirmus
recombinant His-tagged wild-type enzyme, pH 10.5, 40°C
6.52
L-alanine
pH 10.5, 25°C, recombinant enzyme
8.1
L-alanine
recombinant enzyme, pH 8.0, 55°C
18
L-alanine
Alkalihalophilus pseudofirmus
recombinant His-tagged mutant K73A, pH 10.5, 40°C
0.019
L-homophenylalanine
mutant F94S, pH 10.2, temperature not specified in the publication
0.037
L-homophenylalanine
mutant F94S/Y117L, pH 10.2, temperature not specified in the publication
0.00088
L-leucine
mutant F94S, pH 10.2, temperature not specified in the publication
0.0027
L-leucine
mutant F94S/Y117L, pH 10.2, temperature not specified in the publication
0.0016
L-methionine
mutant F94S, pH 10.2, temperature not specified in the publication
0.0026
L-methionine
mutant F94S/Y117L, pH 10.2, temperature not specified in the publication
0.006
L-norleucine
mutant F94S, pH 10.2, temperature not specified in the publication
0.013
L-norleucine
mutant F94S/Y117L, pH 10.2, temperature not specified in the publication
0.0004
L-norvaline
wild-type, pH 10.2, temperature not specified in the publication
0.0017
L-norvaline
mutant F94S, pH 10.2, temperature not specified in the publication
0.0017
L-norvaline
pH 9.0, 30°C, reductive amination reaction
0.04
L-norvaline
mutant F94S/Y117L, pH 10.2, temperature not specified in the publication
0.01
L-serine
wild-type, pH 10.2, temperature not specified in the publication
0.044
L-serine
pH 9.0, 30°C, reductive amination reaction
0.003
L-valine
pH 9.0, 30°C, reductive amination reaction
0.0046
L-valine
wild-type, pH 10.2, temperature not specified in the publication
7
NAD+
Alkalihalophilus pseudofirmus
recombinant His-tagged mutant K73S, pH 10.5, 40°C
12.5
NAD+
Alkalihalophilus pseudofirmus
recombinant His-tagged mutant K73E and K73Y, pH 10.5, 40°C
17.5
NAD+
Alkalihalophilus pseudofirmus
recombinant His-tagged mutant K73R, pH 10.5, 40°C
20
NAD+
Alkalihalophilus pseudofirmus
recombinant His-tagged mutant K73F, pH 10.5, 40°C
20
NAD+
Alkalihalophilus pseudofirmus
recombinant His-tagged wild-type enzyme, pH 10.5, 40°C
25
NAD+
Alkalihalophilus pseudofirmus
recombinant His-tagged mutant K73Q, pH 10.5, 40°C
26.67
NAD+
Alkalihalophilus pseudofirmus
recombinant His-tagged mutant K73A, pH 10.5, 40°C
50
NADH
-
mutant D196A/L197R, pH 8.3, 30°C
83
NADH
-
mutant D196A, pH 8.3, 30°C
998
NADH
-
wild-type, pH 8.3, 30°C
25
NADPH
-
wild-type, pH 8.3, 30°C
58
NADPH
-
mutant D196A/L197R/R201A, pH 8.3, 30°C
103
NADPH
-
mutant D196A, pH 8.3, 30°C
140
NADPH
-
mutant D196A/L197R/N198S/R201A, pH 8.3, 30°C
901
NADPH
-
mutant D196A/L197R, pH 8.3, 30°C
1.9
pyruvate
pH 9.0, 30°C, reductive amination reaction
364
pyruvate
recombinant enzyme, pH 9.0, 55°C
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evolution
-
distribution of Alds in mycobacteria, phylogenetic analysis and tree, overview. Alds of slow-growing mycobacteria are mostly distinct from those of fast-growing mycobacteria
evolution
distribution of Alds in mycobacteria, phylogenetic analysis and tree, overview. Alds of slow-growing mycobacteria are mostly distinct from those of fast-growing mycobacteria. Structure of Ald and phylogenetic relevance of mycobacterial Alds
evolution
distribution of Alds in mycobacteria, phylogenetic analysis and tree, overview. Alds of slow-growing mycobacteria are mostly distinct from those of fast-growing mycobacteria. Structure of Ald and phylogenetic relevance of mycobacterial Alds
evolution
distribution of Alds in mycobacteria, phylogenetic analysis and tree, overview. Alds of slow-growing mycobacteria are mostly distinct from those of fast-growing mycobacteria. Structure of Ald and phylogenetic relevance of mycobacterial Alds
evolution
sequence comparisons and phylogenetic analysis
evolution
sequence comparisons and phylogenetic analysis indicate that enzyme HAADH1 is a distinct type of alanine dehydrogenase
evolution
-
distribution of Alds in mycobacteria, phylogenetic analysis and tree, overview. Alds of slow-growing mycobacteria are mostly distinct from those of fast-growing mycobacteria. Structure of Ald and phylogenetic relevance of mycobacterial Alds
-
evolution
-
distribution of Alds in mycobacteria, phylogenetic analysis and tree, overview. Alds of slow-growing mycobacteria are mostly distinct from those of fast-growing mycobacteria. Structure of Ald and phylogenetic relevance of mycobacterial Alds
-
evolution
-
distribution of Alds in mycobacteria, phylogenetic analysis and tree, overview. Alds of slow-growing mycobacteria are mostly distinct from those of fast-growing mycobacteria. Structure of Ald and phylogenetic relevance of mycobacterial Alds
-
evolution
-
distribution of Alds in mycobacteria, phylogenetic analysis and tree, overview. Alds of slow-growing mycobacteria are mostly distinct from those of fast-growing mycobacteria. Structure of Ald and phylogenetic relevance of mycobacterial Alds
-
evolution
-
distribution of Alds in mycobacteria, phylogenetic analysis and tree, overview. Alds of slow-growing mycobacteria are mostly distinct from those of fast-growing mycobacteria. Structure of Ald and phylogenetic relevance of mycobacterial Alds
-
malfunction
-
an ald knockout strain grows without alanine or glycine and is able to utilize glycine but not alanine as a nitrogen source
malfunction
an ald mutant of Mycolicibacterium smegmatis is much more sensitive to the bcc1 complex inhibitor Q203 than the isogenic wild-type strain. Another ald mutant of Mycolicibacterium smegmatis reportedly displays decreased survival under oxygen depletion conditions compared with the wild-type strain. When Mycolicibacterium smegmatis strains are treated with KCN under aerobic conditions, expression of the ald gene in a bd quinol oxidase mutant strain of Mycolicibacterium smegmatis expressing only the aa3 cytochrome c oxidase as a terminal oxidase is more induced than that in the corresponding wild-type strain expressing both terminal oxidases. Reduced functionality of the ETC, rather than direct regulation of ald by an O2-sensing regulatory system, is most relevant to hypoxic induction of ald expression
malfunction
growth of Streptomyces coelicolor A3(2) is impacted by the deletion of the alanine dehydrogenase (ALD), an essential enzyme that plays a central role in the carbon and nitrogen metabolism. A long lagphase growth followed by a slow exponential growth of Streptomyces coelicolor due to ALD gene deletion is observed in liquid yeast extract mineral salt culture. The slow lag-phase growth is replaced by the normal wild-type like growth by ALD complementation engineering. Deletion mutant SCDELTAALD spores have a paler appearance compared to the standard brownish gray pigmentation for the wild-type SCWT spores. This reduced pigmentation is complemented, and the standard brownish gray pigmentation reappeares during SC-ALD sporulation
malfunction
Alkalihalophilus pseudofirmus
mutations at four conserved residue Arg15, Lys75, His-6, and Asp269 (except residue Lys73) result in a complete loss in enzymatic activity, which signifies that these predicted active sites are indispensable for OF4Ald activity
malfunction
the inactivation of ald in Mycobacterium tuberculosis confers a low level of DCS resistance. The mechanism underlying DCS resistance resulting from ald inactivation is suggested as follows: Mycobacterium tuberculosis strains lacking the functional Ald cannot convert L-alanine to pyruvate, resulting in an increase in cellular levels of L-alanine. As DCS is a competitive inhibitor of alanine racemase, inhibition of alanine racemase by DCS might be overcome by increased concentrations of L-alanine that is a substrate of alanine racemase
malfunction
the inhibition of electron flux through the respiratory electron transport chain (ETC) by either the disruption of the gene for the major terminal oxidase (aa3 cytochrome c oxidase) or treatment with KCN results in the induction of ald encoding alanine dehydrogenase in Mycolicibacterium smegmatis. A decrease in functionality of the ETC shifts the redox state of the NADH/NAD+x02pool toward a more reduced state, which in turn leads to an increase in cellular levels of alanine by Ald catalyzing the conversion of pyruvate to alanine with the concomitant oxidation of NADH to NAD+. The induction of ald expression under respiration-inhibitory conditions in Mycolicibacterium smegmatis is mediated by the alanine-responsive AldR transcriptional regulator. The growth defect of the bacteria by respiration inhibition is exacerbated by inactivation of the ald gene
malfunction
-
growth of Streptomyces coelicolor A3(2) is impacted by the deletion of the alanine dehydrogenase (ALD), an essential enzyme that plays a central role in the carbon and nitrogen metabolism. A long lagphase growth followed by a slow exponential growth of Streptomyces coelicolor due to ALD gene deletion is observed in liquid yeast extract mineral salt culture. The slow lag-phase growth is replaced by the normal wild-type like growth by ALD complementation engineering. Deletion mutant SCDELTAALD spores have a paler appearance compared to the standard brownish gray pigmentation for the wild-type SCWT spores. This reduced pigmentation is complemented, and the standard brownish gray pigmentation reappeares during SC-ALD sporulation
-
malfunction
Alkalihalophilus pseudofirmus OF4
-
mutations at four conserved residue Arg15, Lys75, His-6, and Asp269 (except residue Lys73) result in a complete loss in enzymatic activity, which signifies that these predicted active sites are indispensable for OF4Ald activity
-
malfunction
Alkalihalophilus pseudofirmus ATCC BAA-2126
-
mutations at four conserved residue Arg15, Lys75, His-6, and Asp269 (except residue Lys73) result in a complete loss in enzymatic activity, which signifies that these predicted active sites are indispensable for OF4Ald activity
-
malfunction
-
the inhibition of electron flux through the respiratory electron transport chain (ETC) by either the disruption of the gene for the major terminal oxidase (aa3 cytochrome c oxidase) or treatment with KCN results in the induction of ald encoding alanine dehydrogenase in Mycolicibacterium smegmatis. A decrease in functionality of the ETC shifts the redox state of the NADH/NAD+x02pool toward a more reduced state, which in turn leads to an increase in cellular levels of alanine by Ald catalyzing the conversion of pyruvate to alanine with the concomitant oxidation of NADH to NAD+. The induction of ald expression under respiration-inhibitory conditions in Mycolicibacterium smegmatis is mediated by the alanine-responsive AldR transcriptional regulator. The growth defect of the bacteria by respiration inhibition is exacerbated by inactivation of the ald gene
-
malfunction
-
an ald mutant of Mycolicibacterium smegmatis is much more sensitive to the bcc1 complex inhibitor Q203 than the isogenic wild-type strain. Another ald mutant of Mycolicibacterium smegmatis reportedly displays decreased survival under oxygen depletion conditions compared with the wild-type strain. When Mycolicibacterium smegmatis strains are treated with KCN under aerobic conditions, expression of the ald gene in a bd quinol oxidase mutant strain of Mycolicibacterium smegmatis expressing only the aa3 cytochrome c oxidase as a terminal oxidase is more induced than that in the corresponding wild-type strain expressing both terminal oxidases. Reduced functionality of the ETC, rather than direct regulation of ald by an O2-sensing regulatory system, is most relevant to hypoxic induction of ald expression
-
malfunction
Alkalihalophilus pseudofirmus JCM 17055
-
mutations at four conserved residue Arg15, Lys75, His-6, and Asp269 (except residue Lys73) result in a complete loss in enzymatic activity, which signifies that these predicted active sites are indispensable for OF4Ald activity
-
malfunction
-
growth of Streptomyces coelicolor A3(2) is impacted by the deletion of the alanine dehydrogenase (ALD), an essential enzyme that plays a central role in the carbon and nitrogen metabolism. A long lagphase growth followed by a slow exponential growth of Streptomyces coelicolor due to ALD gene deletion is observed in liquid yeast extract mineral salt culture. The slow lag-phase growth is replaced by the normal wild-type like growth by ALD complementation engineering. Deletion mutant SCDELTAALD spores have a paler appearance compared to the standard brownish gray pigmentation for the wild-type SCWT spores. This reduced pigmentation is complemented, and the standard brownish gray pigmentation reappeares during SC-ALD sporulation
-
malfunction
-
an ald knockout strain grows without alanine or glycine and is able to utilize glycine but not alanine as a nitrogen source
-
malfunction
-
the inactivation of ald in Mycobacterium tuberculosis confers a low level of DCS resistance. The mechanism underlying DCS resistance resulting from ald inactivation is suggested as follows: Mycobacterium tuberculosis strains lacking the functional Ald cannot convert L-alanine to pyruvate, resulting in an increase in cellular levels of L-alanine. As DCS is a competitive inhibitor of alanine racemase, inhibition of alanine racemase by DCS might be overcome by increased concentrations of L-alanine that is a substrate of alanine racemase
-
malfunction
-
the inactivation of ald in Mycobacterium tuberculosis confers a low level of DCS resistance. The mechanism underlying DCS resistance resulting from ald inactivation is suggested as follows: Mycobacterium tuberculosis strains lacking the functional Ald cannot convert L-alanine to pyruvate, resulting in an increase in cellular levels of L-alanine. As DCS is a competitive inhibitor of alanine racemase, inhibition of alanine racemase by DCS might be overcome by increased concentrations of L-alanine that is a substrate of alanine racemase
-
malfunction
-
the inhibition of electron flux through the respiratory electron transport chain (ETC) by either the disruption of the gene for the major terminal oxidase (aa3 cytochrome c oxidase) or treatment with KCN results in the induction of ald encoding alanine dehydrogenase in Mycolicibacterium smegmatis. A decrease in functionality of the ETC shifts the redox state of the NADH/NAD+x02pool toward a more reduced state, which in turn leads to an increase in cellular levels of alanine by Ald catalyzing the conversion of pyruvate to alanine with the concomitant oxidation of NADH to NAD+. The induction of ald expression under respiration-inhibitory conditions in Mycolicibacterium smegmatis is mediated by the alanine-responsive AldR transcriptional regulator. The growth defect of the bacteria by respiration inhibition is exacerbated by inactivation of the ald gene
-
malfunction
-
an ald mutant of Mycolicibacterium smegmatis is much more sensitive to the bcc1 complex inhibitor Q203 than the isogenic wild-type strain. Another ald mutant of Mycolicibacterium smegmatis reportedly displays decreased survival under oxygen depletion conditions compared with the wild-type strain. When Mycolicibacterium smegmatis strains are treated with KCN under aerobic conditions, expression of the ald gene in a bd quinol oxidase mutant strain of Mycolicibacterium smegmatis expressing only the aa3 cytochrome c oxidase as a terminal oxidase is more induced than that in the corresponding wild-type strain expressing both terminal oxidases. Reduced functionality of the ETC, rather than direct regulation of ald by an O2-sensing regulatory system, is most relevant to hypoxic induction of ald expression
-
malfunction
-
growth of Streptomyces coelicolor A3(2) is impacted by the deletion of the alanine dehydrogenase (ALD), an essential enzyme that plays a central role in the carbon and nitrogen metabolism. A long lagphase growth followed by a slow exponential growth of Streptomyces coelicolor due to ALD gene deletion is observed in liquid yeast extract mineral salt culture. The slow lag-phase growth is replaced by the normal wild-type like growth by ALD complementation engineering. Deletion mutant SCDELTAALD spores have a paler appearance compared to the standard brownish gray pigmentation for the wild-type SCWT spores. This reduced pigmentation is complemented, and the standard brownish gray pigmentation reappeares during SC-ALD sporulation
-
metabolism
by catalyzing the NAD+-dependent reversible interconversion of alanine and pyruvate, enzyme ALD plays a central role in the carbon and nitrogen metabolism in all microorganisms. This enzymatic process not only provides alanine as an energy source through the tricarboxylic acid cycle for most bacterial species but it is also the key pathway for de novo alanine synthesis for some microorganisms. The oxidative deamination reaction catalyzed by ALD is required for microorganisms to utilize alanine as a nitrogen source
metabolism
expression of the ald gene is strongly upregulated in Mycolicibacterium smegmatis grown in the presence of alanine. Alanine-dependent regulation of ald is mediated by the AldR transcriptional regulator that belongs to the Lrp/AsnC (leucine-responsive regulatory protein/asparagine synthase C) family
metabolism
regulation mechanism of ald expression by the AldR transcription factor in response to alanine availability, model for the regulation of ald expression by AldR, overview
metabolism
regulation mechanism of ald expression by the AldR transcription factor in response to alanine availability, model for the regulation of ald expression by AldR, overview
metabolism
-
regulation mechanism of ald expression by the AldR transcription factor in response to alanine availability, model for the regulation of ald expression by AldR, overview
metabolism
regulation mechanism of ald expression by the AldR transcription factor in response to alanine availability, model for the regulation of ald expression by AldR, overview. AldR exerts its regulatory effect on ald expression by binding AldR binding sites (O1, O2, O3, and O4) bearing a consensus sequence of GA/T-N2-NWW/WWN-N2-T/AC (W = A or T; / = or) in both Mycolicibacterium smegmatis. Three-dimensional structure of AldR and phylogenetic analysis of AldRs from mycobacteria
metabolism
-
by catalyzing the NAD+-dependent reversible interconversion of alanine and pyruvate, enzyme ALD plays a central role in the carbon and nitrogen metabolism in all microorganisms. This enzymatic process not only provides alanine as an energy source through the tricarboxylic acid cycle for most bacterial species but it is also the key pathway for de novo alanine synthesis for some microorganisms. The oxidative deamination reaction catalyzed by ALD is required for microorganisms to utilize alanine as a nitrogen source
-
metabolism
-
regulation mechanism of ald expression by the AldR transcription factor in response to alanine availability, model for the regulation of ald expression by AldR, overview
-
metabolism
-
expression of the ald gene is strongly upregulated in Mycolicibacterium smegmatis grown in the presence of alanine. Alanine-dependent regulation of ald is mediated by the AldR transcriptional regulator that belongs to the Lrp/AsnC (leucine-responsive regulatory protein/asparagine synthase C) family
-
metabolism
-
regulation mechanism of ald expression by the AldR transcription factor in response to alanine availability, model for the regulation of ald expression by AldR, overview. AldR exerts its regulatory effect on ald expression by binding AldR binding sites (O1, O2, O3, and O4) bearing a consensus sequence of GA/T-N2-NWW/WWN-N2-T/AC (W = A or T; / = or) in both Mycolicibacterium smegmatis. Three-dimensional structure of AldR and phylogenetic analysis of AldRs from mycobacteria
-
metabolism
-
by catalyzing the NAD+-dependent reversible interconversion of alanine and pyruvate, enzyme ALD plays a central role in the carbon and nitrogen metabolism in all microorganisms. This enzymatic process not only provides alanine as an energy source through the tricarboxylic acid cycle for most bacterial species but it is also the key pathway for de novo alanine synthesis for some microorganisms. The oxidative deamination reaction catalyzed by ALD is required for microorganisms to utilize alanine as a nitrogen source
-
metabolism
-
regulation mechanism of ald expression by the AldR transcription factor in response to alanine availability, model for the regulation of ald expression by AldR, overview
-
metabolism
-
regulation mechanism of ald expression by the AldR transcription factor in response to alanine availability, model for the regulation of ald expression by AldR, overview
-
metabolism
-
expression of the ald gene is strongly upregulated in Mycolicibacterium smegmatis grown in the presence of alanine. Alanine-dependent regulation of ald is mediated by the AldR transcriptional regulator that belongs to the Lrp/AsnC (leucine-responsive regulatory protein/asparagine synthase C) family
-
metabolism
-
regulation mechanism of ald expression by the AldR transcription factor in response to alanine availability, model for the regulation of ald expression by AldR, overview. AldR exerts its regulatory effect on ald expression by binding AldR binding sites (O1, O2, O3, and O4) bearing a consensus sequence of GA/T-N2-NWW/WWN-N2-T/AC (W = A or T; / = or) in both Mycolicibacterium smegmatis. Three-dimensional structure of AldR and phylogenetic analysis of AldRs from mycobacteria
-
metabolism
-
by catalyzing the NAD+-dependent reversible interconversion of alanine and pyruvate, enzyme ALD plays a central role in the carbon and nitrogen metabolism in all microorganisms. This enzymatic process not only provides alanine as an energy source through the tricarboxylic acid cycle for most bacterial species but it is also the key pathway for de novo alanine synthesis for some microorganisms. The oxidative deamination reaction catalyzed by ALD is required for microorganisms to utilize alanine as a nitrogen source
-
physiological function
-
the enzyme is involved in the alanine catabolism in the heterocysts, that is needed for normal diazotrophic growth
physiological function
-
enzyme Ald may have several functions, including ammonium incorporation and alanine breakdown. Ald plays an essential role in the utilization of alanine but not of glycine. Ald is not essential for the breakdown of glycine
physiological function
-
the enzyme plays an important role in the carbon and nitrogen metabolism of microorganisms, it iis a key factor in assimilation of L-Ala as energy source through TCA cycle
physiological function
abundance and activity profiles of alanine dehydrogenase concomitantly increase with the onset of enhanced alanine utilization during transition into stationary growth phase
physiological function
both mRNA levels and enzymatic activities of isocitrate lyase, and alanine dehydrogenase increases during entry into nonreplicating persistence. Expression of alanine dehydrogenase is also induced in vitro by persistence-inducing stresses such as nitric oxide, and the gene is expressed at high levels in vivo during the initial lung infection in mice. Enzyme activity is maintained during extended hypoxia even after transcription levels decrease. A knockout mutant shows no reduction in anaerobic survival in vitro, but results in a significant lag in the resumption of growth after reoxygenation. During reactivation the mutant has an altered NADH/NAD ratio
physiological function
AlaDH catalyzes the reversible conversion of L-alanine and pyruvate, which has an important role in the TCA energy cycle
physiological function
Ald is beneficial to Mycolicibacterium smegmatis in its adaptation and survival under respiration-inhibitory conditions by maintaining NADH/NAD+ homeostasis. Ald is required for optimal mycobacterial growth under severe respiration-inhibitory conditions
physiological function
enzyme Ald is implicated in resistance of Mycobacterium tuberculosis to the second-line drug D-cycloserine (DCS). DCS is known to inhibit two enzymes, alanine racemase and D-alanine-D-alanine ligase
physiological function
enzyme Ald is suggested to primarily play a biosynthetic role by catalyzing the reductive amination of pyruvate to alanine as judged by the very small Keq for the oxidative deamination reaction
physiological function
enzyme Ald seems to play a crucial role in the growth and survival of the organism under severe respiration-inhibitory conditions such as the inhibitory condition of both the bcc1-aa3 branch and bd quinol oxidase of the respiratory ETC
physiological function
gene ApalaDH encodes a bifunctional protein catalyzing the reversible reaction of pyruvate to L-alanine via its pyruvate reductive aminase (PvRA) activity, the reaction of L-alanine to pyruvate via its alanine oxidative dehydrogenase activity, and the non-reversible reaction of glyoxylate to glycine via its glyoxylate reductive aminase (GxRA) activity. The assimilatory/dissimilatory roles of enzyme ApAlaDH from the halotolerant cyanobacterium Aphanothece halophytica are not only specific for L-alanine and pyruvate, but also, upon salt stress, include glyoxylate to generate glycine. ApAlaDH is a bifunctional enzyme
physiological function
L-alanine dehydrogenase is a NADH-dependent enzyme that catalyzes the reversible reductive amination of pyruvate using ammonia as amine source
physiological function
-
the enzyme is involved in the alanine catabolism in the heterocysts, that is needed for normal diazotrophic growth
-
physiological function
-
L-alanine dehydrogenase is a NADH-dependent enzyme that catalyzes the reversible reductive amination of pyruvate using ammonia as amine source
-
physiological function
-
gene ApalaDH encodes a bifunctional protein catalyzing the reversible reaction of pyruvate to L-alanine via its pyruvate reductive aminase (PvRA) activity, the reaction of L-alanine to pyruvate via its alanine oxidative dehydrogenase activity, and the non-reversible reaction of glyoxylate to glycine via its glyoxylate reductive aminase (GxRA) activity. The assimilatory/dissimilatory roles of enzyme ApAlaDH from the halotolerant cyanobacterium Aphanothece halophytica are not only specific for L-alanine and pyruvate, but also, upon salt stress, include glyoxylate to generate glycine. ApAlaDH is a bifunctional enzyme
-
physiological function
-
Ald is beneficial to Mycolicibacterium smegmatis in its adaptation and survival under respiration-inhibitory conditions by maintaining NADH/NAD+ homeostasis. Ald is required for optimal mycobacterial growth under severe respiration-inhibitory conditions
-
physiological function
-
enzyme Ald seems to play a crucial role in the growth and survival of the organism under severe respiration-inhibitory conditions such as the inhibitory condition of both the bcc1-aa3 branch and bd quinol oxidase of the respiratory ETC
-
physiological function
-
enzyme Ald may have several functions, including ammonium incorporation and alanine breakdown. Ald plays an essential role in the utilization of alanine but not of glycine. Ald is not essential for the breakdown of glycine
-
physiological function
-
both mRNA levels and enzymatic activities of isocitrate lyase, and alanine dehydrogenase increases during entry into nonreplicating persistence. Expression of alanine dehydrogenase is also induced in vitro by persistence-inducing stresses such as nitric oxide, and the gene is expressed at high levels in vivo during the initial lung infection in mice. Enzyme activity is maintained during extended hypoxia even after transcription levels decrease. A knockout mutant shows no reduction in anaerobic survival in vitro, but results in a significant lag in the resumption of growth after reoxygenation. During reactivation the mutant has an altered NADH/NAD ratio
-
physiological function
-
enzyme Ald is implicated in resistance of Mycobacterium tuberculosis to the second-line drug D-cycloserine (DCS). DCS is known to inhibit two enzymes, alanine racemase and D-alanine-D-alanine ligase
-
physiological function
-
enzyme Ald is suggested to primarily play a biosynthetic role by catalyzing the reductive amination of pyruvate to alanine as judged by the very small Keq for the oxidative deamination reaction
-
physiological function
-
enzyme Ald is implicated in resistance of Mycobacterium tuberculosis to the second-line drug D-cycloserine (DCS). DCS is known to inhibit two enzymes, alanine racemase and D-alanine-D-alanine ligase
-
physiological function
-
enzyme Ald is suggested to primarily play a biosynthetic role by catalyzing the reductive amination of pyruvate to alanine as judged by the very small Keq for the oxidative deamination reaction
-
physiological function
-
Ald is beneficial to Mycolicibacterium smegmatis in its adaptation and survival under respiration-inhibitory conditions by maintaining NADH/NAD+ homeostasis. Ald is required for optimal mycobacterial growth under severe respiration-inhibitory conditions
-
physiological function
-
enzyme Ald seems to play a crucial role in the growth and survival of the organism under severe respiration-inhibitory conditions such as the inhibitory condition of both the bcc1-aa3 branch and bd quinol oxidase of the respiratory ETC
-
physiological function
-
abundance and activity profiles of alanine dehydrogenase concomitantly increase with the onset of enhanced alanine utilization during transition into stationary growth phase
-
additional information
-
alanine is transported from vegetative cells into heterocysts in the diazotrophic Anabaena filament
additional information
Alkalihalophilus pseudofirmus
five highly conserved amino acid residues Arg15, Lys73, Lys75, His96, and Asp269 are potential catalytic residues of L-alanine dehydrogenase from Bacillus pseudofirmus strain OF4. Enzyme structure homology modeling and structure-function analysis, comparison of the partial potential active site of OF4Ald and its mutants based on the structure of Mycobacterium tuberculosis MtAld (PDB ID 2VHY)., overview. Residue Lys73 is involved in substrate binding
additional information
-
alanine is transported from vegetative cells into heterocysts in the diazotrophic Anabaena filament
-
additional information
Alkalihalophilus pseudofirmus OF4
-
five highly conserved amino acid residues Arg15, Lys73, Lys75, His96, and Asp269 are potential catalytic residues of L-alanine dehydrogenase from Bacillus pseudofirmus strain OF4. Enzyme structure homology modeling and structure-function analysis, comparison of the partial potential active site of OF4Ald and its mutants based on the structure of Mycobacterium tuberculosis MtAld (PDB ID 2VHY)., overview. Residue Lys73 is involved in substrate binding
-
additional information
Alkalihalophilus pseudofirmus ATCC BAA-2126
-
five highly conserved amino acid residues Arg15, Lys73, Lys75, His96, and Asp269 are potential catalytic residues of L-alanine dehydrogenase from Bacillus pseudofirmus strain OF4. Enzyme structure homology modeling and structure-function analysis, comparison of the partial potential active site of OF4Ald and its mutants based on the structure of Mycobacterium tuberculosis MtAld (PDB ID 2VHY)., overview. Residue Lys73 is involved in substrate binding
-
additional information
Alkalihalophilus pseudofirmus JCM 17055
-
five highly conserved amino acid residues Arg15, Lys73, Lys75, His96, and Asp269 are potential catalytic residues of L-alanine dehydrogenase from Bacillus pseudofirmus strain OF4. Enzyme structure homology modeling and structure-function analysis, comparison of the partial potential active site of OF4Ald and its mutants based on the structure of Mycobacterium tuberculosis MtAld (PDB ID 2VHY)., overview. Residue Lys73 is involved in substrate binding
-
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D269A
Alkalihalophilus pseudofirmus
site-directed mutagenesis
H96A
Alkalihalophilus pseudofirmus
site-directed mutagenesis
K73A
Alkalihalophilus pseudofirmus
site-directed mutagenesis, the mutant shows 6fold improvement in kcat/Km towards L-alanine as compared to the wild-type enzyme, the mutant is slightly more temperture-sensitive compared to wild-type
K73E
Alkalihalophilus pseudofirmus
site-directed mutagenesis
K73F
Alkalihalophilus pseudofirmus
site-directed mutagenesis
K73Q
Alkalihalophilus pseudofirmus
site-directed mutagenesis
K73R
Alkalihalophilus pseudofirmus
site-directed mutagenesis
K73S
Alkalihalophilus pseudofirmus
site-directed mutagenesis
K73Y
Alkalihalophilus pseudofirmus
site-directed mutagenesis
K75A
Alkalihalophilus pseudofirmus
site-directed mutagenesis
R15A
Alkalihalophilus pseudofirmus
site-directed mutagenesis
H96A
Alkalihalophilus pseudofirmus ATCC BAA-2126
-
site-directed mutagenesis
-
K73A
Alkalihalophilus pseudofirmus ATCC BAA-2126
-
site-directed mutagenesis, the mutant shows 6fold improvement in kcat/Km towards L-alanine as compared to the wild-type enzyme, the mutant is slightly more temperture-sensitive compared to wild-type
-
K73Q
Alkalihalophilus pseudofirmus ATCC BAA-2126
-
site-directed mutagenesis
-
K75A
Alkalihalophilus pseudofirmus ATCC BAA-2126
-
site-directed mutagenesis
-
H96A
Alkalihalophilus pseudofirmus JCM 17055
-
site-directed mutagenesis
-
K73A
Alkalihalophilus pseudofirmus JCM 17055
-
site-directed mutagenesis, the mutant shows 6fold improvement in kcat/Km towards L-alanine as compared to the wild-type enzyme, the mutant is slightly more temperture-sensitive compared to wild-type
-
K73Q
Alkalihalophilus pseudofirmus JCM 17055
-
site-directed mutagenesis
-
K75A
Alkalihalophilus pseudofirmus JCM 17055
-
site-directed mutagenesis
-
H96A
Alkalihalophilus pseudofirmus OF4
-
site-directed mutagenesis
-
K73A
Alkalihalophilus pseudofirmus OF4
-
site-directed mutagenesis, the mutant shows 6fold improvement in kcat/Km towards L-alanine as compared to the wild-type enzyme, the mutant is slightly more temperture-sensitive compared to wild-type
-
K73Q
Alkalihalophilus pseudofirmus OF4
-
site-directed mutagenesis
-
K75A
Alkalihalophilus pseudofirmus OF4
-
site-directed mutagenesis
-
D196A
-
alterating cofactor specificity from NADH to NADPH, 10fold decrease in activity with NADH, 4fold increase in activity with NADPH
D196A/L197R
-
alterating cofactor specificity from NADH to NADPH, almost the same activity with NADPH as the wild-type enzyme for NADH
D196A/L197R/N198S/R201A
-
alterating cofactor specificity from NADH to NADPH, loss of activity with NADH, 5fold increase in activity with NADPH
D196A/L197R/R201A
-
alterating cofactor specificity from NADH to NADPH, loss of activity with NADH, 2fold increase in activity with NADPH
D270N/H96A
the protein can still convert its conformation from open state to closed state. The key interactions between NADH and Asn270 disappear with mutation, with loss of protein activity
F94S
mutation alters its substrate specificity pattern, enabling activity toward a range of larger amino acids
F94S/Y117L
mutant shows improved activity toward hydrophobic amino acids
D270N
-
upon mutation of residue D270 or H96A, the protein always changes its conformations from open state to closed state upon binding NADH. The nicotinamide ring and ribose of NADH is unstable due to the loss of interactions of NADH with Asp270, and the structural rearrangement of active site leads to an orientation change of Asn270 and Gln271, which makes the protein lose its activity
-
D270N/H96A
-
the protein can still convert its conformation from open state to closed state. The key interactions between NADH and Asn270 disappear with mutation, with loss of protein activity
-
F94S
-
mutation alters its substrate specificity pattern, enabling activity toward a range of larger amino acids
-
F94S/Y117L
-
mutant shows improved activity toward hydrophobic amino acids
-
H96A
-
upon mutation of residue D270 or H96A, the protein always changes its conformations from open state to closed state upon binding NADH. The nicotinamide ring and ribose of NADH is unstable due to the loss of interactions of NADH with Asp270, and the structural rearrangement of active site leads to an orientation change of Asn270 and Gln271, which makes the protein lose its activity
-
R199I
specific for NAD+ as the wild-type enzyme
D198R
-
acts also on NADP+
-
R199I
-
specific for NAD+ as the wild-type enzyme
-
D198A
-
mutant enzyme shows higher efficiency with NADP+ as coenzyme than with NAD+
D198G
-
mutant enzyme shows higher efficiency with NADP+ as coenzyme than with NAD+
D198L
-
mutant enzyme shows higher efficiency with NADP+ as coenzyme than with NAD+
D198V
-
mutant enzyme shows higher efficiency with NADP+ as coenzyme than with NAD+
D198A
-
mutant enzyme shows higher efficiency with NADP+ as coenzyme than with NAD+
-
D198G
-
mutant enzyme shows higher efficiency with NADP+ as coenzyme than with NAD+
-
D198L
-
mutant enzyme shows higher efficiency with NADP+ as coenzyme than with NAD+
-
D198V
-
mutant enzyme shows higher efficiency with NADP+ as coenzyme than with NAD+
-
D270N
-
inactive, the bifurcated hydrogen bond between Asp270 and the ribose of NAD is replaced by a single hydrogen bond
D270N
upon mutation of residue D270 or H96A, the protein always changes its conformations from open state to closed state upon binding NADH. The nicotinamide ring and ribose of NADH is unstable due to the loss of interactions of NADH with Asp270, and the structural rearrangement of active site leads to an orientation change of Asn270 and Gln271, which makes the protein lose its activity
H96A
-
inactive
H96A
upon mutation of residue D270 or H96A, the protein always changes its conformations from open state to closed state upon binding NADH. The nicotinamide ring and ribose of NADH is unstable due to the loss of interactions of NADH with Asp270, and the structural rearrangement of active site leads to an orientation change of Asn270 and Gln271, which makes the protein lose its activity
additional information
Alkalihalophilus pseudofirmus
mutations at four conserved residue Arg15, Lys75, His-6 and Asp269 (except residue Lys73) result in a complete loss in enzymatic activity, which signifies that these predicted active sites are indispensable for OF4Ald activity
additional information
Alkalihalophilus pseudofirmus ATCC BAA-2126
-
mutations at four conserved residue Arg15, Lys75, His-6 and Asp269 (except residue Lys73) result in a complete loss in enzymatic activity, which signifies that these predicted active sites are indispensable for OF4Ald activity
-
additional information
Alkalihalophilus pseudofirmus JCM 17055
-
mutations at four conserved residue Arg15, Lys75, His-6 and Asp269 (except residue Lys73) result in a complete loss in enzymatic activity, which signifies that these predicted active sites are indispensable for OF4Ald activity
-
additional information
Alkalihalophilus pseudofirmus OF4
-
mutations at four conserved residue Arg15, Lys75, His-6 and Asp269 (except residue Lys73) result in a complete loss in enzymatic activity, which signifies that these predicted active sites are indispensable for OF4Ald activity
-
additional information
-
inactivation of gene ald results in a lack of alanine dehydrogenase activity, a substantially decreased nitrogenase activity, and a 50% reduction in the rate of diazotrophic growth. While production of alanine is not affected in the ald mutant, alanine catabolism is hampered. Construction of several mutant strains, e,g, the insertion mutant strain CSR24, phenotypes, overview
additional information
-
inactivation of gene ald results in a lack of alanine dehydrogenase activity, a substantially decreased nitrogenase activity, and a 50% reduction in the rate of diazotrophic growth. While production of alanine is not affected in the ald mutant, alanine catabolism is hampered. Construction of several mutant strains, e,g, the insertion mutant strain CSR24, phenotypes, overview
-
additional information
biocatalytic deracemization of aliphatic amino acids into D-enantiomers by running cascade reactions: (1) stereoinversion of L-alanine to a D-form by L-alanine dehydrogenase and omega-transaminase and (2) regeneration of NAD+ by NADH oxidase. Under the cascade reaction conditions containing 100 mM isopropylamine and 1 mM NAD+, complete deracemization of 100 mM DL-alanine is achieved after 24 h with 95% reaction yield of D-alanine (over 99% enantiomeric excess, 52% isolation yield). AlaDH produces pyruvate from L-alanine with NAD+, NOX oxidizes NADH to NAD+, and reductive amination of the resulting pyruvate back to the amino acid in an enantiomerically opposite form by D-selective omega-transaminase (omega-TA) using isopropylamine as an amino donor cosubstrate. Method evaluation, overview
additional information
the purified enzyme is immobilized on porous agarose microbeads activated with glyoxyl groups (aliphatic aldehydes). 85% of the offered enzyme is immobilized on these microbeads and the enzyme recovers 45% of its initial reduction amination activity upon the multivalent and irreversible attachment. The immobilized enzyme shows 13fold increased thermostability compared to the soluble enzyme. The optimally immobilized enzyme is also stabilized against acidic pH. The enzyme works as heterogeneous biocatalyst for the synthesis of L-[13N]alanine using pyruvate and [13N]NH4OH obtaining a radiochemical yield of over 95% in 20 minutes. This immobilized enzyme is reused for up to 5 cycles keeping the maximum yield. Immobilization method optimization, overview
additional information
-
biocatalytic deracemization of aliphatic amino acids into D-enantiomers by running cascade reactions: (1) stereoinversion of L-alanine to a D-form by L-alanine dehydrogenase and omega-transaminase and (2) regeneration of NAD+ by NADH oxidase. Under the cascade reaction conditions containing 100 mM isopropylamine and 1 mM NAD+, complete deracemization of 100 mM DL-alanine is achieved after 24 h with 95% reaction yield of D-alanine (over 99% enantiomeric excess, 52% isolation yield). AlaDH produces pyruvate from L-alanine with NAD+, NOX oxidizes NADH to NAD+, and reductive amination of the resulting pyruvate back to the amino acid in an enantiomerically opposite form by D-selective omega-transaminase (omega-TA) using isopropylamine as an amino donor cosubstrate. Method evaluation, overview
-
additional information
-
the purified enzyme is immobilized on porous agarose microbeads activated with glyoxyl groups (aliphatic aldehydes). 85% of the offered enzyme is immobilized on these microbeads and the enzyme recovers 45% of its initial reduction amination activity upon the multivalent and irreversible attachment. The immobilized enzyme shows 13fold increased thermostability compared to the soluble enzyme. The optimally immobilized enzyme is also stabilized against acidic pH. The enzyme works as heterogeneous biocatalyst for the synthesis of L-[13N]alanine using pyruvate and [13N]NH4OH obtaining a radiochemical yield of over 95% in 20 minutes. This immobilized enzyme is reused for up to 5 cycles keeping the maximum yield. Immobilization method optimization, overview
-
additional information
-
coimmobilization of malic enzyme and alanine dehydrogenase on organic-inorganic hybrid gel fibers of cellulose acetate and zirconium alkoxide by air-gap wet spinning, and the production of L-alanine from malic acid using the fibers with coenzyme regeneration, overview
additional information
-
generation of ald knockout strain RVW7 from wild-type strain H37Rv
additional information
-
generation of ald knockout strain RVW7 from wild-type strain H37Rv
-
additional information
generation of a DELTAaldR mutant strain
additional information
-
generation of a DELTAaldR mutant strain
additional information
-
generation of a DELTAaldR mutant strain
-
additional information
-
generation of a DELTAaldR mutant strain
-
additional information
an enzymatic assay system to eliminate or measure D-Ala, which is reported to affect the taste of seafoods or sake, is constructed using alanine racemase (L-AlaR from Synechocystis sp. PCC6803) and L-alanine dehydrogenase (L-AlaDH from Phormidium lapideum). D-Ala is converted to L-Ala by alanine racemase and then deaminated by L-alanine dehydrogenase with the reduction of NAD+ to NADH, which is determined with water-soluble tetrazolium. NADH nonenzymatically reduces WST-1 to form water soluble formazan. Using the assay system, the D-Ala contents of 7 crustaceans are determined. Method evaluation, overview
additional information
construction of an amperometric biosensor using AlaDH of Streptomyces anulatus amidst the working electrode (3 mm diameter) present at the center of the screen printed electrode. The mixture contains AlaDH (80 mg/ml of freeze dried enzyme), NADH (200 mg/ml), pyruvate (80 mg/ml) and the binder 1% poly HEMA (poly-hydroxyethylmethacrylate) in 50 mM Tris-HCl buffer, pH 8.5. The mixture is allowed to dry at 4°C. The weight of the sensor strip after immobilizing the mixture is 0.56 g sensor strips are incubated at different temperatures (10-70°C) for 5 min before placing the samples (10 mM ammonium chloride dissolved in buffers of different pH) on the strip during the measurement of output current. The output current is measured by cyclic voltammetry by using a potentiostat
additional information
-
construction of an amperometric biosensor using AlaDH of Streptomyces anulatus amidst the working electrode (3 mm diameter) present at the center of the screen printed electrode. The mixture contains AlaDH (80 mg/ml of freeze dried enzyme), NADH (200 mg/ml), pyruvate (80 mg/ml) and the binder 1% poly HEMA (poly-hydroxyethylmethacrylate) in 50 mM Tris-HCl buffer, pH 8.5. The mixture is allowed to dry at 4°C. The weight of the sensor strip after immobilizing the mixture is 0.56 g sensor strips are incubated at different temperatures (10-70°C) for 5 min before placing the samples (10 mM ammonium chloride dissolved in buffers of different pH) on the strip during the measurement of output current. The output current is measured by cyclic voltammetry by using a potentiostat
-
additional information
construction an ald gene deletion strain (SCDELTAALD) by double crossover in-frame deletion of the ald gene (SCO1773) in wild-type strain SCWT by PCR targeting. An ald complementation strain SC-ALD is generated by using a site-specific integrating vector pMS81 that inserts into PhiBT1 attB site of SCDELTAALD. An effect of the ald gene deletion on the pigmentation during sporulation on solid agar medium in observed. Mutant SCDELTAALD spores have a paler appearance compared to the standard brownish gray pigmentation for the wild-type SCWT spores. This reduced pigmentation is complemented, and the standard brownish gray pigmentation reappeares during SC-ALD sporulation
additional information
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construction an ald gene deletion strain (SCDELTAALD) by double crossover in-frame deletion of the ald gene (SCO1773) in wild-type strain SCWT by PCR targeting. An ald complementation strain SC-ALD is generated by using a site-specific integrating vector pMS81 that inserts into PhiBT1 attB site of SCDELTAALD. An effect of the ald gene deletion on the pigmentation during sporulation on solid agar medium in observed. Mutant SCDELTAALD spores have a paler appearance compared to the standard brownish gray pigmentation for the wild-type SCWT spores. This reduced pigmentation is complemented, and the standard brownish gray pigmentation reappeares during SC-ALD sporulation
additional information
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construction an ald gene deletion strain (SCDELTAALD) by double crossover in-frame deletion of the ald gene (SCO1773) in wild-type strain SCWT by PCR targeting. An ald complementation strain SC-ALD is generated by using a site-specific integrating vector pMS81 that inserts into PhiBT1 attB site of SCDELTAALD. An effect of the ald gene deletion on the pigmentation during sporulation on solid agar medium in observed. Mutant SCDELTAALD spores have a paler appearance compared to the standard brownish gray pigmentation for the wild-type SCWT spores. This reduced pigmentation is complemented, and the standard brownish gray pigmentation reappeares during SC-ALD sporulation
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additional information
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construction an ald gene deletion strain (SCDELTAALD) by double crossover in-frame deletion of the ald gene (SCO1773) in wild-type strain SCWT by PCR targeting. An ald complementation strain SC-ALD is generated by using a site-specific integrating vector pMS81 that inserts into PhiBT1 attB site of SCDELTAALD. An effect of the ald gene deletion on the pigmentation during sporulation on solid agar medium in observed. Mutant SCDELTAALD spores have a paler appearance compared to the standard brownish gray pigmentation for the wild-type SCWT spores. This reduced pigmentation is complemented, and the standard brownish gray pigmentation reappeares during SC-ALD sporulation
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additional information
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construction an ald gene deletion strain (SCDELTAALD) by double crossover in-frame deletion of the ald gene (SCO1773) in wild-type strain SCWT by PCR targeting. An ald complementation strain SC-ALD is generated by using a site-specific integrating vector pMS81 that inserts into PhiBT1 attB site of SCDELTAALD. An effect of the ald gene deletion on the pigmentation during sporulation on solid agar medium in observed. Mutant SCDELTAALD spores have a paler appearance compared to the standard brownish gray pigmentation for the wild-type SCWT spores. This reduced pigmentation is complemented, and the standard brownish gray pigmentation reappeares during SC-ALD sporulation
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additional information
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mutant Aldomega, deficient in transcription induction of a number of genes during nitrogen starvation, transcripts of several specific nitrogen-responsive genes accumulate at lower levels in the mutant than in the wild-type strain, accumulates alanine upon nitrogen starvation, does not decrease the accumulation of transcripts during sulfur starvation, attenuated phycobilisome degradation during nitrogen starvation
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