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ENZYME

ENZYME entry: EC 2.8.1.12

Accepted Name
molybdopterin synthase
Alternative Name(s)
MPT synthase
Reaction catalysed
2 [molybdopterin-synthase sulfur-carrier protein]-C-terminal Gly-NH-CH2-C(O)SH + cyclic pyranopterin phosphate + H2O <=> 2 [molybdopterin-synthase sulfur-carrier protein]-C-terminal Gly-Gly + 4 H(+) + molybdopterin
Comment(s)
  • Catalyzes the synthesis of molybdopterin from cyclic pyranopterin phosphate.
  • Two sulfur atoms are transferred to cyclic pyranopterin phosphate in order to form the characteristic ene-dithiol group found in the molybdenum cofactor.
  • Molybdopterin synthase consists of two large subunits forming a central dimer and two small subunits (molybdopterin-synthase sulfur- carrier proteins) that are thiocarboxylated at the C-terminus by EC 2.8.1.11, molybdopterin synthase sulfurtransferase.
  • The reaction occurs in prokaryotes and eukaryotes.
Cross-references
BRENDA 2.8.1.12
EC2PDB 2.8.1.12
ExplorEnz 2.8.1.12
PRIAM enzyme-specific profiles 2.8.1.12
KEGG Ligand Database for Enzyme Nomenclature 2.8.1.12
IUBMB Enzyme Nomenclature 2.8.1.12
IntEnz 2.8.1.12
MEDLINE Find literature relating to 2.8.1.12
MetaCyc 2.8.1.12
Rhea expert-curated reactions 2.8.1.12
UniProtKB/Swiss-Prot
Q171H3, MO2B1_AEDAE Q1DGL6, MO2B2_AEDAE P9WJR2, MOAE1_MYCTO
P9WJR3, MOAE1_MYCTU P9WJR0, MOAE2_MYCTO P9WJR1, MOAE2_MYCTU
O67928, MOAE_AQUAE O31705, MOAE_BACSU P65396, MOAE_BRUME
P65397, MOAE_BRUSU Q9AC50, MOAE_CAUVC Q53091, MOAE_CERS4
P30749, MOAE_ECOLI Q7VLN4, MOAE_HAEDU P45308, MOAE_HAEIN
Q9K8I7, MOAE_HALH5 Q9ZL44, MOAE_HELPJ P56422, MOAE_HELPY
Q8YWH5, MOAE_NOSS1 Q9CN24, MOAE_PASMU Q9HX97, MOAE_PSEAE
Q9V2A7, MOAE_PYRAB Q8XZR3, MOAE_RALN1 Q984P0, MOAE_RHILO
Q92QX5, MOAE_RHIME P65399, MOAE_SALTI P65398, MOAE_SALTY
Q5HDT6, MOAE_STAAC P65400, MOAE_STAAM P65401, MOAE_STAAN
Q6GEG3, MOAE_STAAR Q6G751, MOAE_STAAS Q8NVA3, MOAE_STAAW
Q9ZIM9, MOAE_STACT Q5HLX8, MOAE_STAEQ Q8CNE3, MOAE_STAES
Q56210, MOAE_SYNE7 Q97CL5, MOAE_THEVO Q9KT77, MOAE_VIBCH
Q8ZGW2, MOAE_YERPE A6R104, MOC2B_AJECN Q7QAD7, MOC2B_ANOGA
O22827, MOC2B_ARATH A1CJM9, MOC2B_ASPCL B0XYQ4, MOC2B_ASPFC
Q4WWW9, MOC2B_ASPFU A2QF55, MOC2B_ASPNC Q2U4W2, MOC2B_ASPOR
A4FUY7, MOC2B_BOVIN Q1DQS9, MOC2B_COCIM B0X1V5, MOC2B_CULQU
Q86HF4, MOC2B_DICDI B3M268, MOC2B_DROAN B3P6R5, MOC2B_DROER
B4JHP4, MOC2B_DROGR Q9VBX2, MOC2B_DROME B4KBH3, MOC2B_DROMO
B4GE20, MOC2B_DROPE Q297G3, MOC2B_DROPS B4IJG7, MOC2B_DROSE
B4QUC0, MOC2B_DROSI B4LVP8, MOC2B_DROVI B4NJW0, MOC2B_DROWI
B4PUD1, MOC2B_DROYA Q9Y8C1, MOC2B_EMENI O96007, MOC2B_HUMAN
Q9Z223, MOC2B_MOUSE A1D7X4, MOC2B_NEOFI Q7SEW2, MOC2B_NEUCR
A2X0R4, MOC2B_ORYSI Q6Z2X3, MOC2B_ORYSJ Q0V713, MOC2B_PHANO
Q5RA61, MOC2B_PONAB Q2KF83, MOC2B_PYRO7 B2WBW4, MOC2B_PYRTR
Q6AY59, MOC2B_RAT A7EVF4, MOC2B_SCLS1 B5FXU9, MOC2B_TAEGU

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All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 2.8.1.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 2.8.-.-
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