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Literature summary for 2.8.4.1 extracted from

  • Kunz, R.C.; Dey, M.; Ragsdale, S.W.
    Characterization of the thioether product formed from the thiolytic cleavage of the alkyl-nickel bond in methyl-coenzyme M reductase (2008), Biochemistry, 47, 2661-2667.
    View publication on PubMed
Search for more literature for 2.8.4.1

Inhibitors

Inhibitors Comment Organism Structure
bromopropanesulfonate BPS, a potent inhibitor and reversible redox inactivator that reacts with MCRred1 to form an EPR-active state called MCRPS, which is an alkyl-nickel species. Treatment of MCRPS with free thiol containing compounds leads to reconvertion to the active MCRred1 state Methanothermobacter marburgensis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information stopped flow kinetics, overview Methanothermobacter marburgensis
0.016
-
 HS-CoB8 pH 10.0, 25°C Methanothermobacter marburgensis
0.46
-
 HS-CoB9 pH 10.0, 25°C Methanothermobacter marburgensis
3.5
-
 CH3-S-CoM pH 10.0, 25°C Methanothermobacter marburgensis
62
-
 CH3-S-CoM3 pH 10.0, 25°C Methanothermobacter marburgensis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
CH3-S-CoM + HS-CoB Methanothermobacter marburgensis MCR catalyzes the first proposed step in anaerobic methane oxidation and terminal step in methanogenesis by using N-7-mercaptoheptanolyl-threonine phosphate, i.e. CoB-SH. as the two-electron donor to reduce 2-(methylthiol)-ethane sulfonate, i.e. methyl-SCoM, to methane, and producing the heterodisulfide, CoBS-SCoM CoM-S-S-CoB + methane
-
 ?

Organism

Organism UniProt Comment Textmining
Methanothermobacter marburgensis
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
CH3-S-CoM + HS-CoB MCR catalyzes the first proposed step in anaerobic methane oxidation and terminal step in methanogenesis by using N-7-mercaptoheptanolyl-threonine phosphate, i.e. CoB-SH. as the two-electron donor to reduce 2-(methylthiol)-ethane sulfonate, i.e. methyl-SCoM, to methane, and producing the heterodisulfide, CoBS-SCoM Methanothermobacter marburgensis CoM-S-S-CoB + methane
-
 ?
CH3-S-CoM + HS-CoB8 a two-electron transfer reaction Methanothermobacter marburgensis CoM-S-S-CoB8 + methane
-
 ?
CH3-S-CoM + HS-CoB9
-
 Methanothermobacter marburgensis CoM-S-S-CoB9 + methane
-
 ?
CH3-S-CoM3 + HS-CoB8
-
 Methanothermobacter marburgensis CoM3-S-S-CoB8 + methane
-
 ?
additional information MCR substrate specificity and reactivation activity of different thiols, e.g. 2-mercaptoethanol, DTT, Na2S, and cysteine, kinetics, overview Methanothermobacter marburgensis ?
-
 ?

Synonyms

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

Temperature Optimum [°C]

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

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
10
-
 assay at Methanothermobacter marburgensis

Cofactor

Cofactor Comment Organism Structure
F-430 the active site of MCR includes a noncovalently bound Ni tetrapyrrolic coenzyme F430, which is in the Ni(I) state in the active enzyme, MCRred1 Methanothermobacter marburgensis