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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
BRENDA2.8.1.12
EC2PDB2.8.1.12
ExplorEnz2.8.1.12
PRIAM enzyme-specific profiles2.8.1.12
KEGG Ligand Database for Enzyme Nomenclature2.8.1.12
IUBMB Enzyme Nomenclature2.8.1.12
IntEnz2.8.1.12
MEDLINEFind literature relating to 2.8.1.12
MetaCyc2.8.1.12
Rhea expert-curated reactions2.8.1.12
UniProtKB/Swiss-Prot
Q171H3, MO2B1_AEDAE;  Q1DGL6, MO2B2_AEDAE;  P9WJR2, MOAE1_MYCTO;  
P9WJR3, MOAE1_MYCTU;  P9WJR0, MOAE2_MYCTO;  P9WJR1, MOAE2_MYCTU;  
Q9K8I7, MOAE_ALKHC;  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;  Q9ZL44, MOAE_HELPJ;  P56422, MOAE_HELPY;  
Q8YWH5, MOAE_NOSS1;  Q9CN24, MOAE_PASMU;  Q9HX97, MOAE_PSEAE;  
Q9V2A7, MOAE_PYRAB;  Q8XZR3, MOAE_RALSO;  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;  
Q2KF83, MOC2B_MAGO7;  Q9Z223, MOC2B_MOUSE;  A1D7X4, MOC2B_NEOFI;  
Q7SEW2, MOC2B_NEUCR;  A2X0R4, MOC2B_ORYSI;  Q6Z2X3, MOC2B_ORYSJ;  
Q0V713, MOC2B_PHANO;  Q5RA61, MOC2B_PONAB;  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.-.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 2.-.-.-