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ENZYME

ENZYME entry: EC 1.2.1.84

Accepted Name
alcohol-forming fatty acyl-CoA reductase
Reaction catalysed
a long-chain fatty acyl-CoA + 2 H(+) + 2 NADPH <=> a long-chain primary fatty alcohol + CoA + 2 NADP(+)
Comment(s)
  • The enzyme has been characterized from the plant Simmondsia chinensis (jojoba).
  • The alcohol is formed by a four-electron reduction of fatty acyl-CoA.
  • Although the reaction proceeds through an aldehyde intermediate, a free aldehyde is not released.
  • The recombinant enzyme was shown to accept saturated and mono- unsaturated fatty acyl-CoAs of 16 to 22 carbons.
Cross-references
BRENDA 1.2.1.84
EC2PDB 1.2.1.84
ExplorEnz 1.2.1.84
PRIAM enzyme-specific profiles 1.2.1.84
KEGG Ligand Database for Enzyme Nomenclature 1.2.1.84
IUBMB Enzyme Nomenclature 1.2.1.84
IntEnz 1.2.1.84
MEDLINE Find literature relating to 1.2.1.84
MetaCyc 1.2.1.84
Rhea expert-curated reactions 1.2.1.84
UniProtKB/Swiss-Prot
Q39152, FACR1_ARATH Q5ZM72, FACR1_CHICK A1ZAI5, FACR1_DROME
Q8WVX9, FACR1_HUMAN Q922J9, FACR1_MOUSE Q5R834, FACR1_PONAB
Q66H50, FACR1_RAT Q7ZXF5, FACR1_XENLA Q08891, FACR2_ARATH
Q0P5J1, FACR2_BOVIN A1ZAI3, FACR2_DROME Q96K12, FACR2_HUMAN
Q7TNT2, FACR2_MOUSE Q93ZB9, FACR3_ARATH Q960W6, FACR3_DROME
Q9LXN3, FACR4_ARATH Q0WRB0, FACR5_ARATH B9TSP7, FACR6_ARATH
Q1PEI6, FACR8_ARATH Q9XGY7, FAR_SIMCH Q8MS59, WAT_DROME

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All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.2.1.-
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