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ENZYME

ENZYME entry: EC 2.8.1.12

PURL: https://purl.expasy.org/enzyme/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-aminoethanethioate + cyclic pyranopterin phosphate + H2O = molybdopterin + 2 [molybdopterin-synthase sulfur-carrier protein]-C-terminal Gly-Gly + 2 H(+)
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
BRENDA2.8.1.12
EC2PDB2.8.1.12
ExplorEnz2.8.1.12
KEGG Ligand Database for Enzyme Nomenclature2.8.1.12
IUBMB Enzyme Nomenclature2.8.1.12
MEDLINEFind literature relating to 2.8.1.12
MetaCyc2.8.1.12
Rhea expert-curated reactions2.8.1.12
UniProtKB/Swiss-Prot
Q171H3, MO2B1_AEDAEQ1DGL6, MO2B2_AEDAEP9WJR2, MOAE1_MYCTO
P9WJR3, MOAE1_MYCTUP9WJR0, MOAE2_MYCTOP9WJR1, MOAE2_MYCTU
O67928, MOAE_AQUAEO31705, MOAE_BACSUP65396, MOAE_BRUME
P65397, MOAE_BRUSUQ9AC50, MOAE_CAUVCQ53091, MOAE_CERS4
P30749, MOAE_ECOLIQ7VLN4, MOAE_HAEDUP45308, MOAE_HAEIN
Q9K8I7, MOAE_HALH5Q9ZL44, MOAE_HELPJP56422, MOAE_HELPY
Q8YWH5, MOAE_NOSS1Q9CN24, MOAE_PASMUQ9HX97, MOAE_PSEAE
Q9V2A7, MOAE_PYRABQ8XZR3, MOAE_RALN1Q984P0, MOAE_RHILO
Q92QX5, MOAE_RHIMEP65399, MOAE_SALTIP65398, MOAE_SALTY
Q5HDT6, MOAE_STAACP65400, MOAE_STAAMP65401, MOAE_STAAN
Q6GEG3, MOAE_STAARQ6G751, MOAE_STAASQ8NVA3, MOAE_STAAW
Q9ZIM9, MOAE_STACTQ5HLX8, MOAE_STAEQQ8CNE3, MOAE_STAES
Q56210, MOAE_SYNE7Q97CL5, MOAE_THEVOQ9KT77, MOAE_VIBCH
Q8ZGW2, MOAE_YERPEA6R104, MOC2B_AJECNQ7QAD7, MOC2B_ANOGA
O22827, MOC2B_ARATHA1CJM9, MOC2B_ASPCLB0XYQ4, MOC2B_ASPFC
Q4WWW9, MOC2B_ASPFUA2QF55, MOC2B_ASPNCQ2U4W2, MOC2B_ASPOR
A4FUY7, MOC2B_BOVINQ1DQS9, MOC2B_COCIMB0X1V5, MOC2B_CULQU
Q86HF4, MOC2B_DICDIB3M268, MOC2B_DROANB3P6R5, MOC2B_DROER
B4JHP4, MOC2B_DROGRQ9VBX2, MOC2B_DROMEB4KBH3, MOC2B_DROMO
B4GE20, MOC2B_DROPEQ297G3, MOC2B_DROPSB4IJG7, MOC2B_DROSE
B4QUC0, MOC2B_DROSIB4LVP8, MOC2B_DROVIB4NJW0, MOC2B_DROWI
B4PUD1, MOC2B_DROYAQ9Y8C1, MOC2B_EMENIO96007, MOC2B_HUMAN
Q9Z223, MOC2B_MOUSEA1D7X4, MOC2B_NEOFIQ7SEW2, MOC2B_NEUCR
A2X0R4, MOC2B_ORYSIQ6Z2X3, MOC2B_ORYSJQ0V713, MOC2B_PHANO
Q5RA61, MOC2B_PONABQ2KF83, MOC2B_PYRO7B2WBW4, MOC2B_PYRTR
Q6AY59, MOC2B_RATA7EVF4, MOC2B_SCLS1B5FXU9, 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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