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Literature summary for 2.8.4.1 extracted from

  • Kunz, R.C.; Horng, Y.C.; Ragsdale, S.W.
    Spectroscopic and kinetic studies of the reaction of bromopropanesulfonate with methyl-coenzyme M reductase (2006), J. Biol. Chem., 281, 34663-34676.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
1-butanesulfonate
-
Methanothermobacter marburgensis
1-propanesulfonate
-
Methanothermobacter marburgensis
2-bromoethanesulfonate
-
Methanothermobacter marburgensis
3-bromopropanesulfonate irreversible, strong inhibitor and competitive substrate Methanothermobacter marburgensis
3-Bromopropionate
-
Methanothermobacter marburgensis
3-chloropropanesulfonyl chloride
-
Methanothermobacter marburgensis
3-mercapto-1-propanesulfonate
-
Methanothermobacter marburgensis
4-bromobutanesulfonate
-
Methanothermobacter marburgensis
4-bromobutyrate
-
Methanothermobacter marburgensis
4-Chlorobutyrate
-
Methanothermobacter marburgensis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information steady-state and rapid kinetics, MCRred1-catalyzed cleavage of the C-S bond of methyl-SCoM requires the other substrate, HSCoB, even under single turnover conditions Methanothermobacter marburgensis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
methyl-coenzyme M + N-(7-mercaptoheptanoyl)threonine 3-O-phosphate (coenzyme B) Methanothermobacter marburgensis i.e. methyl-SCoM methane + CoB-S-S-CoM a the mixed disulfide ?
additional information Methanothermobacter marburgensis MCR also appears to initiate anaerobic methane oxidation, the reverse methanogenesis ?
-
?

Organism

Organism UniProt Comment Textmining
Methanothermobacter marburgensis
-
i.e. Methanothermobacter thermoautotrophicum strain Marburg
-

Purification (Commentary)

Purification (Comment) Organism
purification of native MCRox1, and of native MCRred1, the latter by ammonium sulfate fractionation and ion exchange chromatography Methanothermobacter marburgensis

Reaction

Reaction Comment Organism Reaction ID
methyl-CoM + CoB = CoM-S-S-CoB + methane two possible catalytic mechanisms, overview Methanothermobacter marburgensis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
methyl-coenzyme M + N-(7-mercaptoheptanoyl)threonine 3-O-phosphate (coenzyme B) i.e. methyl-SCoM Methanothermobacter marburgensis methane + CoB-S-S-CoM a the mixed disulfide ?
additional information MCR also appears to initiate anaerobic methane oxidation, the reverse methanogenesis Methanothermobacter marburgensis ?
-
?
additional information conversion of MCRox1 toMCRred1 by Ti(III)citrate, bromopropanesulfonate is an alternative substrate of MCR in an ionic reaction that is coenzyme B-independent and leads to debromination of bromopropanesulfonate and formation of a distinct state with an EPR signal that is assigned to a Ni(III)-propylsulfonate species, propanesulfonate formation also occurs in steady-state reactions in the presence of Ti(III) citrate Methanothermobacter marburgensis ?
-
?

Synonyms

Synonyms Comment Organism
methyl-coenzyme M reductase
-
Methanothermobacter marburgensis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
20 25 assay at Methanothermobacter marburgensis

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
4 65
-
Methanothermobacter marburgensis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
additional information
-
pH 10.0 is optimal for activation of MCRox1 to MCRred1 with Ti(III) citrate Methanothermobacter marburgensis
7 7.6 assay at Methanothermobacter marburgensis

Cofactor

Cofactor Comment Organism Structure
coenzyme F430 the nickel-containing tetrapyrrole is essential for the reaction, and is bound to the active site Methanothermobacter marburgensis