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Literature summary for 2.8.4.1 extracted from

  • Dey, M.; Li, X.; Kunz, R.C.; Ragsdale, S.W.
    Detection of organometallic and radical intermediates in the catalytic mechanism of methyl-coenzyme M reductase using the natural substrate methyl-coenzyme M and a coenzyme B substrate analogue (2010), Biochemistry, 49, 10902-10911.
    View publication on PubMed
Search for more literature for 2.8.4.1

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.03
-
 CH3-S-CoM with SH-CoB6 as cosubstrate, pH not specified in the publication, at 25°C Methanothermobacter marburgensis
0.08
-
 SH-CoB6 pH not specified in the publication, at 25°C Methanothermobacter marburgensis
0.28
-
 CH3-S-CoM with SH-CoB5 as cosubstrate, pH not specified in the publication, at 25°C Methanothermobacter marburgensis
0.34
-
 SH-CoB5 pH not specified in the publication, at 25°C Methanothermobacter marburgensis

Metals/Ions

Metals/Ions Comment Organism Structure
Nickel the active site of the enzyme contains an essential redox-active nickel tetrapyrrole cofactor, coenzyme F430, which is active in the Ni(I) state Methanothermobacter marburgensis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
CH3-S-CoM + SH-CoB Methanothermobacter marburgensis
-
 CoM-S-S-CoB + methane
-
 ?
CH3-S-CoM + SH-CoB Methanothermobacter marburgensis OCM82
-
 CoM-S-S-CoB + methane
-
 ?

Organism

Organism UniProt Comment Textmining
Methanothermobacter marburgensis
-
-
-
Methanothermobacter marburgensis OCM82
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
CH3-S-CoM + SH-CoB
-
 Methanothermobacter marburgensis CoM-S-S-CoB + methane
-
 ?
CH3-S-CoM + SH-CoB
-
 Methanothermobacter marburgensis OCM82 CoM-S-S-CoB + methane
-
 ?
CH3-S-CoM + SH-CoB5
-
 Methanothermobacter marburgensis CoM-S-S-CoB5 + methane
-
 ?
CH3-S-CoM + SH-CoB5
-
 Methanothermobacter marburgensis OCM82 CoM-S-S-CoB5 + methane
-
 ?
CH3-S-CoM + SH-CoB6 methanogenesis occurs 1000fold more slowly than with SH-CoB Methanothermobacter marburgensis CoM-S-S-CoB6 + methane
-
 ?
CH3-S-CoM + SH-CoB6 methanogenesis occurs 1000fold more slowly than with SH-CoB Methanothermobacter marburgensis OCM82 CoM-S-S-CoB6 + methane
-
 ?
additional information no activity with SH-CoB8 or SH-CoB9 Methanothermobacter marburgensis ?
-
 ?
additional information no activity with SH-CoB8 or SH-CoB9 Methanothermobacter marburgensis OCM82 ?
-
 ?

Synonyms

Synonyms Comment Organism
MCR
-
 Methanothermobacter marburgensis
methyl-coenzyme M reductase
-
 Methanothermobacter marburgensis

Cofactor

Cofactor Comment Organism Structure
F-430 the active site of the enzyme contains an essential redox-active nickel tetrapyrrole cofactor, coenzyme F430, which is active in the Ni(I) state Methanothermobacter marburgensis