Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary 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

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.8.4.1 (+)-(2S,3R)-N-[7-(methylthio)heptanoyl]-O-phospho-L-threonine CoB substrate thioester derivative, synthesis, spectral analysis and binding structure, overview Methanothermobacter marburgensis
2.8.4.1 (+)-(2S,3R)-N-[7-(trifluoromethylthio)heptanoyl]-O-phospho-L-threonine fluorescent CoB substrate thioester derivative, synthesis, spectral analysis and binding structure, overview Methanothermobacter marburgensis
2.8.4.1 coenzyme M a competitive inhibitor Methanothermobacter marburgensis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.8.4.1 2-(methylthio)ethanesulfonate + N-(7-mercaptoheptanoyl)threonine 3-O-phosphate Methanothermobacter marburgensis i.e. CoM and CoB CoM-S-S-CoB + methane
-
?

Organism

EC Number Organism UniProt Comment Textmining
2.8.4.1 Methanothermobacter marburgensis
-
strain DSM 2133, MCR isoenzyme I
-

Reaction

EC Number Reaction Comment Organism Reaction ID
2.8.4.1 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

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.8.4.1 2-(methylthio)ethanesulfonate + N-(7-mercaptoheptanoyl)threonine 3-O-phosphate i.e. CoM and CoB Methanothermobacter marburgensis CoM-S-S-CoB + methane
-
?
2.8.4.1 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
-
?
2.8.4.1 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 ?
-
?

Synonyms

EC Number Synonyms Comment Organism
2.8.4.1 MCR
-
Methanothermobacter marburgensis
2.8.4.1 methyl-coenzyme M reductase
-
Methanothermobacter marburgensis

Cofactor

EC Number Cofactor Comment Organism Structure
2.8.4.1 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