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Literature summary extracted from

  • Ermler, U.; Grabarse, W.; Shima, S.; Goubeaud, M.; Thauer, R.K.
    Crystal structure of methyl-coenzyme M reductase: the key enzyme of biological methane formation (1997), Science, 278, 1457-1462.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
2.8.4.1 Ti(III) citrate activation of the oxidized state of enzyme Methanothermobacter thermautotrophicus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.8.4.1 Ni(2+)
-
Methanothermobacter thermautotrophicus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.8.4.1 300000
-
-
Methanothermobacter thermautotrophicus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.8.4.1 methyl coenzyme M + coenzyme B Methanothermobacter thermautotrophicus strictly anaerobic conditions methane + CoM-S-S-CoB
-
?
2.8.4.1 methyl coenzyme M + coenzyme B Methanothermobacter thermautotrophicus key enzyme in methane formation by methanogenic Archaea methane + CoM-S-S-CoB
-
?

Organism

EC Number Organism UniProt Comment Textmining
2.8.4.1 Methanothermobacter thermautotrophicus
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
2.8.4.1 methyl-CoM + CoB = CoM-S-S-CoB + methane proposed reaction mechanism uses a radical intermediate and a nickel organic compound. Suggested solutions for enzyme state, structure, reaction cycle and binding mechanism for the enzyme are given Methanothermobacter thermautotrophicus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.8.4.1 methyl coenzyme M + coenzyme B strictly anaerobic conditions Methanothermobacter thermautotrophicus methane + CoM-S-S-CoB
-
?
2.8.4.1 methyl coenzyme M + coenzyme B key enzyme in methane formation by methanogenic Archaea Methanothermobacter thermautotrophicus methane + CoM-S-S-CoB
-
?

Subunits

EC Number Subunits Comment Organism
2.8.4.1 hexamer alpha2,beta2,gamma2 Methanothermobacter thermautotrophicus

Cofactor

EC Number Cofactor Comment Organism Structure
2.8.4.1 F-430
-
Methanothermobacter thermautotrophicus
2.8.4.1 additional information 2 molecules of the nickel porphinoid coenzyme F-430 are embedded between the subunits, forming 2 structurally identical active sites Methanothermobacter thermautotrophicus