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ENZYME entry: EC 2.8.1.12

Accepted Name
Molybdopterin synthase.
Alternative Name(s)
MPT synthase.
Reaction catalysed
Cyclic pyranopterin phosphate + 2 [molybdopterin-synthase sulfur-carrier protein]-Gly-NH-CH(2)-C(O)SH + H(2)O <=> molybdopterin + 2 [molybdopterin-synthase sulfur-carrier protein]
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
UniProtKB/Swiss-Prot
Q171H3, MO2B1_AEDAE;  Q1DGL6, MO2B2_AEDAE;  P9WJR2, MOAE1_MYCTO;  
P9WJR3, MOAE1_MYCTU;  O67928, MOAE_AQUAE;  Q9K8I7, MOAE_BACHD;  
O31705, MOAE_BACSU;  P65396, MOAE_BRUME;  P65397, MOAE_BRUSU;  
Q9AC50, MOAE_CAUCR;  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;  Q53091, MOAE_RHOS4;  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 UniProtKB/Swiss-Prot entries referenced in this entry, with possibility to download in different formats, align etc.
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.-.-.-