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Literature summary for 2.8.4.1 extracted from

  • Ebner, S.; Jaun, B.; Goenrich, M.; Thauer, R.K.; Harmer, J.
    Binding of coenzyme B induces a major conformational change in the active site of methyl-coenzyme M reductase (2010), J. Am. Chem. Soc., 132, 567-575.
    View publication on PubMed
Search for more literature for 2.8.4.1

Inhibitors

Inhibitors Comment Organism Structure
(+)-(2S,3R)-N-[7-(methylthio)heptanoyl]-O-phospho-L-threonine CoB substrate thioester derivative, synthesis, spectral analysis and binding structure, overview Methanothermobacter marburgensis
(+)-(2S,3R)-N-[7-(trifluoromethylthio)heptanoyl]-O-phospho-L-threonine fluorescent CoB substrate thioester derivative, synthesis, spectral analysis and binding structure, overview Methanothermobacter marburgensis
coenzyme M a competitive inhibitor Methanothermobacter marburgensis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2-(methylthio)ethanesulfonate + N-(7-mercaptoheptanoyl)threonine 3-O-phosphate Methanothermobacter marburgensis i.e. CoM and CoB CoM-S-S-CoB + methane
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 ?

Organism

Organism UniProt Comment Textmining
Methanothermobacter marburgensis
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 strain DSM 2133, MCR isoenzyme I
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Reaction

Reaction Comment Organism Reaction ID
methyl-CoM + CoB = CoM-S-S-CoB + methane catalytic mechanism, the first step of the mechanism is proposed to involve a nucleophilic attack of the NiI active state, MCRred1, on Me-SCoM to form a NiIII-methyl intermediate, spectroscopic analysis and structures, overview Methanothermobacter marburgensis
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-(methylthio)ethanesulfonate + N-(7-mercaptoheptanoyl)threonine 3-O-phosphate i.e. CoM and CoB Methanothermobacter marburgensis CoM-S-S-CoB + methane
-
 ?
2-(methylthio)ethanesulfonate + N-(7-mercaptoheptanoyl)threonine 3-O-phosphate i.e. CoM and CoB, the enzyme exists in the the inactive Ni(II) MCRox1-silent form and the active Ni(I) MCRred1 form with transition from MCRred1 to MCRred2 forms, the protein is able to undergo a conformational change upon binding of the second substrate. Analysis of the catalytic mechanism of the reduction at the nickel center using inhibitory fluorescent trifluoromethyl thio esters of the substrate CoB for spectroscopic analysis of the structure of the enzyme-cofactor complex, derivatives synthesis, overview Methanothermobacter marburgensis CoM-S-S-CoB + methane
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 ?
additional information MCR is the key enzyme in methane formation by methanogenic Archaea. It converts the thioether methyl-coenzyme M and the thiol coenzyme B into methane and the heterodisulfide of coenzyme M and coenzyme B Methanothermobacter marburgensis ?
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 ?

Synonyms

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

Cofactor

Cofactor Comment Organism Structure
F-430 a nickel hydrocorphin coenzyme F430, the Ni(I) MCRred1 form and the inactive Ni(II) MCRox1-silent form, no formation of an MCRis dependent methyl-Ni(F430) species, analysis of the catalytic mechanism of the reduction at the nickel center using inhibitory fluorescent trifluoromethyl thio esters of the substrate CoB for spectroscopic analysis of the structure of the enzyme-cofactor complex, derivatives synthesis, overview Methanothermobacter marburgensis