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 |
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 | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
2.8.4.1 | Methanothermobacter marburgensis | - |
strain DSM 2133, MCR isoenzyme I | - |
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 |
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 | ? | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
2.8.4.1 | MCR | - |
Methanothermobacter marburgensis |
2.8.4.1 | methyl-coenzyme M reductase | - |
Methanothermobacter marburgensis |
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 |