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Literature summary for 2.8.4.1 extracted from

  • Wongnate, T.; Ragsdale, S.W.
    The reaction mechanism of methyl-coenzyme M reductase: how an enzyme enforces strict binding order (2015), J. Biol. Chem., 290, 9322-9334.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.8.4.1

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.169
-
 CoB at pH 7.6 and 25°C Methanothermobacter marburgensis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
270000
-
 gel filtration Methanothermobacter marburgensis

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Methanothermobacter marburgensis
-
 formerly Methanothermobacter thermoautotrophicum strain Marburg
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
methyl-CoM + CoB
-
 Methanothermobacter marburgensis CoM-S-S-CoB + methane
-
 ?

Subunits

Subunits Comment Organism
dimer of heterotrimers
-
 Methanothermobacter marburgensis

Synonyms

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

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
18
-
 CoB at pH 7.6 and 25°C Methanothermobacter marburgensis

Cofactor

Cofactor Comment Organism Structure
coenzyme F430
-
 Methanothermobacter marburgensis

General Information

General Information Comment Organism
metabolism the enzyme catalyzes the final step in methanogenesis Methanothermobacter marburgensis