KEGG   ENZYME: 2.8.4.1Help
Entry
EC 2.8.4.1                  Enzyme                                 

Name
coenzyme-B sulfoethylthiotransferase;
methyl-CoM reductase;
methyl coenzyme M reductase
Class
Transferases;
Transferring sulfur-containing groups;
Transferring alkylthio groups
BRITE hierarchy
Sysname
methyl-CoM:CoB S-(2-sulfoethyl)thiotransferase
Reaction(IUBMB)
methyl-CoM + CoB = CoM-S-S-CoB + methane [RN:R04541]
Reaction(KEGG)
Substrate
methyl-CoM [CPD:C03920];
CoB
Product
CoM-S-S-CoB [CPD:C04832];
methane [CPD:C01438]
Comment
This enzyme catalyses 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 F430. 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.
History
EC 2.8.4.1 created 2001, modified 2011
Pathway
Methane metabolism
Metabolic pathways
Microbial metabolism in diverse environments
Orthology
K00399  
methyl-coenzyme M reductase alpha subunit
K00401  
methyl-coenzyme M reductase beta subunit
K00402  
methyl-coenzyme M reductase gamma subunit
Genes
MJA: 
MFE: 
MVU: 
MFS: 
MIF: 
MIG: 
MMP: 
MMP1555(mcrB) MMP1558(mcrG) MMP1559(mcrA)
MMQ: 
MMX: 
MMZ: 
MMD: 
MAE: 
MVN: 
MVO: 
MOK: 
MAC: 
MBA: 
MMA: 
MMAZ: 
MBU: 
MMH: 
MEV: 
MZH: 
MPY: 
MHZ: 
MTP: 
MCJ: 
MCON_0759(mcrA) MCON_0760(mcrG) MCON_0762(mcrB)
MHI: 
MHU: 
MLA: 
MEM: 
MBG: 
BN140_1521(mcrA) BN140_1522(mcrG1) BN140_1524(mcrB1) BN140_1734(mcrB3) BN140_1737(mcrG3) BN140_1738(mrtA)
MPI: 
MBN: 
MFO: 
MPL: 
MPD: 
MCP_0512(mcrB) MCP_0515(mcrG) MCP_0516(mcrA)
MEZ: 
Mtc_0904(mcrB) Mtc_0907(mcrG) Mtc_0908(mcrA)
RCI: 
RCIX2059(mcrB) RCIX2062(mcrG) RCIX2063(mcrA)
MER: 
MTH: 
MMG: 
MST: 
Msp_0318(mrtB) Msp_0320(mrtG) Msp_0321(mrtA)
MSI: 
MRU: 
mru_1924(mcrA) mru_1925(mcrG) mru_1928(mcrB)
MEB: 
Abm4_1526(mcrA) Abm4_1527(mcrG) Abm4_1530(mcrB)
MEL: 
MEW: 
METH: 
MBMB1_1682(mcrA) MBMB1_1683(mcrG) MBMB1_1686(mcrB) MBMB1_1822(mrtB) MBMB1_1824(mrtG) MBMB1_1825(mrtA)
MFV: 
MKA: 
MK0651(McrB) MK0654(McrG) MK0655(McrA)
MAX: 
TAR: 
 » show all
Taxonomy
Reference
1  [PMID:3122735]
  Authors
Bobik TA, Olson KD, Noll KM, Wolfe RS.
  Title
Evidence that the heterodisulfide of coenzyme M and 7-mercaptoheptanoylthreonine phosphate is a product of the methylreductase reaction in Methanobacterium.
  Journal
Biochem. Biophys. Res. Commun. 149 (1987) 455-60.
  Organism
Methanobacterium thermoautotrophicum
Reference
2
  Authors
Ellermann, J., Hedderich, R., Boecher, R. and Thauer, R.K.
  Title
The final step in methane formation: investigations with highly purified methyl coenzyme M reductase component C from Methanobacterium thermoautotrophicum (strain Marburg).
  Journal
Eur. J. Biochem. 184 (1988) 63-68.
Reference
3  [PMID:9367957]
  Authors
Ermler U, Grabarse W, Shima S, Goubeaud M, Thauer RK.
  Title
Crystal structure of methyl-coenzyme M reductase: the key enzyme of biological methane formation.
  Journal
Science. 278 (1997) 1457-62.
  Organism
Methanobacterium thermoautotrophicum
Reference
4  [PMID:11072815]
  Authors
Signor L, Knuppe C, Hug R, Schweizer B, Pfaltz A, Jaun B.
  Title
Methane formation by reaction of a methyl thioether with a photo-excited nickel thiolate--a process mimicking methanogenesis in archaea.
  Journal
Chemistry. 6 (2000) 3508-16.
  Organism
methanogenic archaea
Reference
5  [PMID:20520712]
  Authors
Scheller S, Goenrich M, Boecher R, Thauer RK, Jaun B
  Title
The key nickel enzyme of methanogenesis catalyses the anaerobic oxidation of methane.
  Journal
Nature. 465 (2010) 606-8.
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
UM-BBD (Biocatalysis/Biodegradation Database): 
BRENDA, the Enzyme Database: 

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