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ENZYME entry: EC

Accepted Name
Coenzyme-B sulfoethylthiotransferase.
Alternative Name(s)
Methyl coenzyme M reductase.
Methyl-CoM reductase.
Reaction catalysed
Methyl-CoM + CoB <=> CoM-S-S-CoB + methane
Coenzyme F430.
  • This enzyme catalyzes the final step in methanogenesis, the biological production of methane.
  • This important anaerobic process is carried out only by methanogenic archaea.
  • The enzyme can also function in reverse, for anaerobic oxidation of methane.
  • The enzyme requires the hydroporphinoid nickel complex coenzyme F(430).
  • Highly specific for coenzyme B with a heptanoyl chain; ethyl CoM and difluoromethyl CoM are poor substrates.
  • The sulfide sulfur can be replaced by selenium but not by oxygen.
PRIAM enzyme-specific profiles2.8.4.1
KEGG Ligand Database for Enzyme Nomenclature2.8.4.1
IUBMB Enzyme Nomenclature2.8.4.1
MEDLINEFind literature relating to
P07962, MCRA_METBF;  P12971, MCRA_METFE;  Q58256, MCRA_METJA;  
Q49605, MCRA_METKA;  P22948, MCRA_METTE;  O27232, MCRA_METTH;  
P11558, MCRA_METTM;  P07961, MCRA_METVA;  P11559, MCRA_METVO;  
P07955, MCRB_METBF;  P12972, MCRB_METFE;  Q58252, MCRB_METJA;  
P22949, MCRB_METTE;  O27236, MCRB_METTH;  P11560, MCRB_METTM;  
P07956, MCRB_METVA;  P11561, MCRB_METVO;  P07964, MCRG_METBF;  
P12973, MCRG_METFE;  Q58255, MCRG_METJA;  P22950, MCRG_METTE;  
O27233, MCRG_METTH;  P11562, MCRG_METTM;  P07963, MCRG_METVA;  
P11563, MCRG_METVO;  Q49174, MCRX_METFV;  Q60391, MCRX_METJA;  
P21110, MCRX_METTH;  P58815, MCRX_METTM;  Q49171, MCRY_METFV;  
Q60390, MCRY_METJA;  P21111, MCRY_METTH;  Q49173, MCRZ_METFV;  
Q60387, MCRZ_METJA;  P21112, MCRZ_METTH;  P58816, MCRZ_METTM;  

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All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 2.8.4.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 2.8.-.-
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