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Literature summary extracted from

  • Kahnt, J.; Buchenau, B.; Mahlert, F.; Krueger, M.; Shima, S.; Thauer, R.K.
    Post-translational modifications in the active site region of methyl-coenzyme M reductase from methanogenic and methanotrophic archaea (2007), FEBS J., 274, 4913-4921.
    View publication on PubMed

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.8.4.1 300000
-
-
Methanosarcina barkeri
2.8.4.1 300000
-
-
Methanocaldococcus jannaschii
2.8.4.1 300000
-
-
Methanopyrus kandleri
2.8.4.1 300000
-
-
Methanococcus voltae
2.8.4.1 300000
-
-
Methanoculleus thermophilus
2.8.4.1 300000
-
-
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 CH3-S-CoM + HS-CoB Methanosarcina barkeri MCR catalyzes the methane-forming step in methanogenic archaea CoM-S-S-CoB + methane
-
?
2.8.4.1 CH3-S-CoM + HS-CoB Methanocaldococcus jannaschii MCR catalyzes the methane-forming step in methanogenic archaea CoM-S-S-CoB + methane
-
?
2.8.4.1 CH3-S-CoM + HS-CoB Methanococcus voltae MCR catalyzes the methane-forming step in methanogenic archaea CoM-S-S-CoB + methane
-
?
2.8.4.1 CH3-S-CoM + HS-CoB Methanoculleus thermophilus MCR catalyzes the methane-forming step in methanogenic archaea CoM-S-S-CoB + methane
-
?
2.8.4.1 CH3-S-CoM + HS-CoB Methanothermobacter marburgensis MCR catalyzes the methane-forming step in methanogenic archaea CoM-S-S-CoB + methane
-
?
2.8.4.1 CH3-S-CoM + HS-CoB Methanopyrus kandleri MCR catalyzes the methane-forming step in methanogenic archaea CoM-S-S-CoB + methane
-
?
2.8.4.1 methyl-coenzyme M + N-(7-mercaptoheptanoyl)threonine 3-O-phosphate (coenzyme B) Methanosarcina barkeri the enzyme catalyzes the methane forming step in methane biosynthesis by methanogenic archaea methane + CoM-S-S-CoB a the mixed disulfide ?
2.8.4.1 methyl-coenzyme M + N-(7-mercaptoheptanoyl)threonine 3-O-phosphate (coenzyme B) Methanocaldococcus jannaschii the enzyme catalyzes the methane forming step in methane biosynthesis by methanogenic archaea methane + CoM-S-S-CoB a the mixed disulfide ?
2.8.4.1 methyl-coenzyme M + N-(7-mercaptoheptanoyl)threonine 3-O-phosphate (coenzyme B) Methanopyrus kandleri the enzyme catalyzes the methane forming step in methane biosynthesis by methanogenic archaea methane + CoM-S-S-CoB a the mixed disulfide ?
2.8.4.1 methyl-coenzyme M + N-(7-mercaptoheptanoyl)threonine 3-O-phosphate (coenzyme B) Methanococcus voltae the enzyme catalyzes the methane forming step in methane biosynthesis by methanogenic archaea methane + CoM-S-S-CoB a the mixed disulfide ?
2.8.4.1 methyl-coenzyme M + N-(7-mercaptoheptanoyl)threonine 3-O-phosphate (coenzyme B) Methanoculleus thermophilus the enzyme catalyzes the methane forming step in methane biosynthesis by methanogenic archaea methane + CoM-S-S-CoB a the mixed disulfide ?
2.8.4.1 methyl-coenzyme M + N-(7-mercaptoheptanoyl)threonine 3-O-phosphate (coenzyme B) Methanothermobacter marburgensis the enzyme catalyzes the methane forming step in methane biosynthesis by methanogenic archaea methane + CoM-S-S-CoB a the mixed disulfide ?

Organism

EC Number Organism UniProt Comment Textmining
2.8.4.1 Methanocaldococcus jannaschii
-
gene mcrA
-
2.8.4.1 Methanocaldococcus jannaschii
-
isozyme MCR I
-
2.8.4.1 Methanococcus voltae
-
-
-
2.8.4.1 Methanoculleus thermophilus
-
isozymes MCR I, gene mcrA
-
2.8.4.1 Methanoculleus thermophilus
-
isozyme MCR I
-
2.8.4.1 Methanopyrus kandleri
-
gene mcrA
-
2.8.4.1 Methanopyrus kandleri Q49605
-
-
2.8.4.1 Methanosarcina barkeri
-
-
-
2.8.4.1 Methanosarcina barkeri
-
gene mcrA
-
2.8.4.1 Methanothermobacter marburgensis
-
isozymes MCR I and MCR II, gene mcrA
-
2.8.4.1 Methanothermobacter marburgensis
-
isozymes MCR I and MCR II
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
2.8.4.1 side-chain modification methylation of residues in the active site, e.g. at His257, 5fold methylation in isozyme MCR I, overview Methanocaldococcus jannaschii
2.8.4.1 side-chain modification methylation of residues in the active site, e.g. at His257, 5fold methylation in isozyme MCR I, overview Methanoculleus thermophilus
2.8.4.1 side-chain modification methylation of residues in the active site, e.g. at His257, 5fold methylation in isozyme MCR I, overview Methanothermobacter marburgensis
2.8.4.1 side-chain modification methylation of residues in the active site, e.g. at His257, overview Methanosarcina barkeri
2.8.4.1 side-chain modification methylation of residues in the active site, e.g. at His257, overview Methanococcus voltae
2.8.4.1 side-chain modification methylation of residues in the active site, e.g. at His257, overview Methanopyrus kandleri

Reaction

EC Number Reaction Comment Organism Reaction ID
2.8.4.1 methyl-CoM + CoB = CoM-S-S-CoB + methane in the active site region of both isozymes, five modified amino acids occur determined by mass spectrometry: thioglycine alpha445, forming a thioxo peptide/thioamide bond with tyrosine alpha446, S-methylcysteine alpha452, 2-(S)-methylglutamine alpha400, 1-N-methylhistidine alpha257 and 5-(S)-methylarginine alpha271 Methanothermobacter marburgensis
2.8.4.1 methyl-CoM + CoB = CoM-S-S-CoB + methane in the active site region of both isozymes, modified amino acids occur determined by mass spectrometry: thioglycine alpha445, forming a thioxo peptide/thioamide bond with tyrosine alpha446, 2-(S)-methylglutamine alpha400, 1-N-methylhistidine alpha257 and 5-(S)-methylarginine alpha271 Methanocaldococcus jannaschii
2.8.4.1 methyl-CoM + CoB = CoM-S-S-CoB + methane in the active site region of both isozymes, modified amino acids occur determined by mass spectrometry: thioglycine alpha445, forming a thioxo peptide/thioamide bond with tyrosine alpha446, 2-(S)-methylglutamine alpha400, 1-N-methylhistidine alpha257 and 5-(S)-methylarginine alpha271 Methanopyrus kandleri
2.8.4.1 methyl-CoM + CoB = CoM-S-S-CoB + methane in the active site region of both isozymes, modified amino acids occur determined by mass spectrometry: thioglycine alpha445, forming a thioxo peptide/thioamide bond with tyrosine alpha446, S-methylcysteine alpha452, 1-N-methylhistidine alpha257 and 5-(S)-methylarginine alpha271 Methanosarcina barkeri
2.8.4.1 methyl-CoM + CoB = CoM-S-S-CoB + methane in the active site region of both isozymes, modified amino acids occur determined by mass spectrometry: thioglycine alpha445, forming a thioxo peptide/thioamide bond with tyrosine alpha446, S-methylcysteine alpha452, 2-(S)-methylglutamine alpha400, and 1-N-methylhistidine alpha257 Methanococcus voltae
2.8.4.1 methyl-CoM + CoB = CoM-S-S-CoB + methane in the active site region of both isozymes, modified amino acids occur determined by mass spectrometry: thioglycine alpha445, forming a thioxo peptide/thioamide bond with tyrosine alpha446, S-methylcysteine alpha452, 2-(S)-methylglutamine alpha400, and 5-(S)-methylarginine alpha271 Methanoculleus thermophilus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.8.4.1 CH3-S-CoM + HS-CoB MCR catalyzes the methane-forming step in methanogenic archaea Methanosarcina barkeri CoM-S-S-CoB + methane
-
?
2.8.4.1 CH3-S-CoM + HS-CoB MCR catalyzes the methane-forming step in methanogenic archaea Methanocaldococcus jannaschii CoM-S-S-CoB + methane
-
?
2.8.4.1 CH3-S-CoM + HS-CoB MCR catalyzes the methane-forming step in methanogenic archaea Methanococcus voltae CoM-S-S-CoB + methane
-
?
2.8.4.1 CH3-S-CoM + HS-CoB MCR catalyzes the methane-forming step in methanogenic archaea Methanoculleus thermophilus CoM-S-S-CoB + methane
-
?
2.8.4.1 CH3-S-CoM + HS-CoB MCR catalyzes the methane-forming step in methanogenic archaea Methanothermobacter marburgensis CoM-S-S-CoB + methane
-
?
2.8.4.1 CH3-S-CoM + HS-CoB MCR catalyzes the methane-forming step in methanogenic archaea Methanopyrus kandleri CoM-S-S-CoB + methane
-
?
2.8.4.1 CH3-S-CoM + HS-CoB MCR contains a thioxo peptide bond and methylated amino acids in the active site region, the number of methylated amino acids varies between species, overview Methanosarcina barkeri CoM-S-S-CoB + methane
-
?
2.8.4.1 CH3-S-CoM + HS-CoB MCR contains a thioxo peptide bond and methylated amino acids in the active site region, the number of methylated amino acids varies between species, overview Methanocaldococcus jannaschii CoM-S-S-CoB + methane
-
?
2.8.4.1 CH3-S-CoM + HS-CoB MCR contains a thioxo peptide bond and methylated amino acids in the active site region, the number of methylated amino acids varies between species, overview Methanococcus voltae CoM-S-S-CoB + methane
-
?
2.8.4.1 CH3-S-CoM + HS-CoB MCR contains a thioxo peptide bond and methylated amino acids in the active site region, the number of methylated amino acids varies between species, overview Methanoculleus thermophilus CoM-S-S-CoB + methane
-
?
2.8.4.1 CH3-S-CoM + HS-CoB MCR contains a thioxo peptide bond and methylated amino acids in the active site region, the number of methylated amino acids varies between species, overview Methanothermobacter marburgensis CoM-S-S-CoB + methane
-
?
2.8.4.1 CH3-S-CoM + HS-CoB MCR contains a thioxo peptide bond and methylated amino acids in the active site region, the number of methylated amino acids varies between species, overview Methanopyrus kandleri CoM-S-S-CoB + methane
-
?
2.8.4.1 methyl-coenzyme M + N-(7-mercaptoheptanoyl)threonine 3-O-phosphate (coenzyme B) i.e. methyl-SCoM Methanosarcina barkeri methane + CoM-S-S-CoB a the mixed disulfide ?
2.8.4.1 methyl-coenzyme M + N-(7-mercaptoheptanoyl)threonine 3-O-phosphate (coenzyme B) i.e. methyl-SCoM Methanocaldococcus jannaschii methane + CoM-S-S-CoB a the mixed disulfide ?
2.8.4.1 methyl-coenzyme M + N-(7-mercaptoheptanoyl)threonine 3-O-phosphate (coenzyme B) i.e. methyl-SCoM Methanopyrus kandleri methane + CoM-S-S-CoB a the mixed disulfide ?
2.8.4.1 methyl-coenzyme M + N-(7-mercaptoheptanoyl)threonine 3-O-phosphate (coenzyme B) i.e. methyl-SCoM Methanococcus voltae methane + CoM-S-S-CoB a the mixed disulfide ?
2.8.4.1 methyl-coenzyme M + N-(7-mercaptoheptanoyl)threonine 3-O-phosphate (coenzyme B) i.e. methyl-SCoM Methanoculleus thermophilus methane + CoM-S-S-CoB a the mixed disulfide ?
2.8.4.1 methyl-coenzyme M + N-(7-mercaptoheptanoyl)threonine 3-O-phosphate (coenzyme B) i.e. methyl-SCoM Methanothermobacter marburgensis methane + CoM-S-S-CoB a the mixed disulfide ?
2.8.4.1 methyl-coenzyme M + N-(7-mercaptoheptanoyl)threonine 3-O-phosphate (coenzyme B) the enzyme catalyzes the methane forming step in methane biosynthesis by methanogenic archaea Methanosarcina barkeri methane + CoM-S-S-CoB a the mixed disulfide ?
2.8.4.1 methyl-coenzyme M + N-(7-mercaptoheptanoyl)threonine 3-O-phosphate (coenzyme B) the enzyme catalyzes the methane forming step in methane biosynthesis by methanogenic archaea Methanocaldococcus jannaschii methane + CoM-S-S-CoB a the mixed disulfide ?
2.8.4.1 methyl-coenzyme M + N-(7-mercaptoheptanoyl)threonine 3-O-phosphate (coenzyme B) the enzyme catalyzes the methane forming step in methane biosynthesis by methanogenic archaea Methanopyrus kandleri methane + CoM-S-S-CoB a the mixed disulfide ?
2.8.4.1 methyl-coenzyme M + N-(7-mercaptoheptanoyl)threonine 3-O-phosphate (coenzyme B) the enzyme catalyzes the methane forming step in methane biosynthesis by methanogenic archaea Methanococcus voltae methane + CoM-S-S-CoB a the mixed disulfide ?
2.8.4.1 methyl-coenzyme M + N-(7-mercaptoheptanoyl)threonine 3-O-phosphate (coenzyme B) the enzyme catalyzes the methane forming step in methane biosynthesis by methanogenic archaea Methanoculleus thermophilus methane + CoM-S-S-CoB a the mixed disulfide ?
2.8.4.1 methyl-coenzyme M + N-(7-mercaptoheptanoyl)threonine 3-O-phosphate (coenzyme B) the enzyme catalyzes the methane forming step in methane biosynthesis by methanogenic archaea Methanothermobacter marburgensis methane + CoM-S-S-CoB a the mixed disulfide ?

Subunits

EC Number Subunits Comment Organism
2.8.4.1 hexamer alpha2beta2gamma2 Methanosarcina barkeri
2.8.4.1 hexamer alpha2beta2gamma2 Methanocaldococcus jannaschii
2.8.4.1 hexamer alpha2beta2gamma2 Methanopyrus kandleri
2.8.4.1 hexamer alpha2beta2gamma2 Methanococcus voltae
2.8.4.1 hexamer alpha2beta2gamma2 Methanoculleus thermophilus
2.8.4.1 hexamer alpha2beta2gamma2 Methanothermobacter marburgensis

Synonyms

EC Number Synonyms Comment Organism
2.8.4.1 MCR
-
Methanosarcina barkeri
2.8.4.1 MCR
-
Methanocaldococcus jannaschii
2.8.4.1 MCR
-
Methanopyrus kandleri
2.8.4.1 MCR
-
Methanococcus voltae
2.8.4.1 MCR
-
Methanoculleus thermophilus
2.8.4.1 MCR
-
Methanothermobacter marburgensis
2.8.4.1 methyl-coenzyme M reductase
-
Methanosarcina barkeri
2.8.4.1 methyl-coenzyme M reductase
-
Methanocaldococcus jannaschii
2.8.4.1 methyl-coenzyme M reductase
-
Methanopyrus kandleri
2.8.4.1 methyl-coenzyme M reductase
-
Methanococcus voltae
2.8.4.1 methyl-coenzyme M reductase
-
Methanoculleus thermophilus
2.8.4.1 methyl-coenzyme M reductase
-
Methanothermobacter marburgensis

Cofactor

EC Number Cofactor Comment Organism Structure
2.8.4.1 coenzyme F430 2 mol of the nickel tetrapyrrole coenzyme F430, tightly bound, per enzyme hexamer, nickel is in the Ni(I) state in the active enzyme Methanosarcina barkeri
2.8.4.1 coenzyme F430 2 mol of the nickel tetrapyrrole coenzyme F430, tightly bound, per enzyme hexamer, nickel is in the Ni(I) state in the active enzyme Methanocaldococcus jannaschii
2.8.4.1 coenzyme F430 2 mol of the nickel tetrapyrrole coenzyme F430, tightly bound, per enzyme hexamer, nickel is in the Ni(I) state in the active enzyme Methanopyrus kandleri
2.8.4.1 coenzyme F430 2 mol of the nickel tetrapyrrole coenzyme F430, tightly bound, per enzyme hexamer, nickel is in the Ni(I) state in the active enzyme Methanococcus voltae
2.8.4.1 coenzyme F430 2 mol of the nickel tetrapyrrole coenzyme F430, tightly bound, per enzyme hexamer, nickel is in the Ni(I) state in the active enzyme Methanoculleus thermophilus
2.8.4.1 coenzyme F430 2 mol of the nickel tetrapyrrole coenzyme F430, tightly bound, per enzyme hexamer, nickel is in the Ni(I) state in the active enzyme Methanothermobacter marburgensis
2.8.4.1 F-430 with Ni(I) oxidation state Methanosarcina barkeri
2.8.4.1 F-430 with Ni(I) oxidation state Methanocaldococcus jannaschii
2.8.4.1 F-430 with Ni(I) oxidation state Methanococcus voltae
2.8.4.1 F-430 with Ni(I) oxidation state Methanoculleus thermophilus
2.8.4.1 F-430 with Ni(I) oxidation state Methanothermobacter marburgensis
2.8.4.1 F-430 with Ni(I) oxidation state Methanopyrus kandleri