Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.8.4.1 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
Search for more literature for 2.8.4.1

Activating Compound

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

Metals/Ions

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

Molecular Weight [Da]

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

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Methanothermobacter thermautotrophicus
-
-
-

Reaction

Reaction Comment Organism Reaction ID
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
a

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
hexamer alpha2,beta2,gamma2 Methanothermobacter thermautotrophicus

Cofactor

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