Literature summary for 2.8.4.1 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.

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
300000	-	-	Methanosarcina barkeri
300000	-	-	Methanocaldococcus jannaschii
300000	-	-	Methanopyrus kandleri
300000	-	-	Methanococcus voltae
300000	-	-	Methanoculleus thermophilus
300000	-	-	Methanothermobacter marburgensis

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.
CH3-S-CoM + HS-CoB	Methanosarcina barkeri	MCR catalyzes the methane-forming step in methanogenic archaea	CoM-S-S-CoB + methane	-	?
CH3-S-CoM + HS-CoB	Methanocaldococcus jannaschii	MCR catalyzes the methane-forming step in methanogenic archaea	CoM-S-S-CoB + methane	-	?
CH3-S-CoM + HS-CoB	Methanococcus voltae	MCR catalyzes the methane-forming step in methanogenic archaea	CoM-S-S-CoB + methane	-	?
CH3-S-CoM + HS-CoB	Methanoculleus thermophilus	MCR catalyzes the methane-forming step in methanogenic archaea	CoM-S-S-CoB + methane	-	?
CH3-S-CoM + HS-CoB	Methanothermobacter marburgensis	MCR catalyzes the methane-forming step in methanogenic archaea	CoM-S-S-CoB + methane	-	?
CH3-S-CoM + HS-CoB	Methanopyrus kandleri	MCR catalyzes the methane-forming step in methanogenic archaea	CoM-S-S-CoB + methane	-	?
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	?
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	?
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	?
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	?
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	?
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

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

Posttranslational Modification

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

Reaction

Reaction	Comment	Organism	Reaction ID
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	a
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	a
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	a
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	a
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	a
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	a

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.
CH3-S-CoM + HS-CoB	MCR catalyzes the methane-forming step in methanogenic archaea	Methanosarcina barkeri	CoM-S-S-CoB + methane	-	?
CH3-S-CoM + HS-CoB	MCR catalyzes the methane-forming step in methanogenic archaea	Methanocaldococcus jannaschii	CoM-S-S-CoB + methane	-	?
CH3-S-CoM + HS-CoB	MCR catalyzes the methane-forming step in methanogenic archaea	Methanococcus voltae	CoM-S-S-CoB + methane	-	?
CH3-S-CoM + HS-CoB	MCR catalyzes the methane-forming step in methanogenic archaea	Methanoculleus thermophilus	CoM-S-S-CoB + methane	-	?
CH3-S-CoM + HS-CoB	MCR catalyzes the methane-forming step in methanogenic archaea	Methanothermobacter marburgensis	CoM-S-S-CoB + methane	-	?
CH3-S-CoM + HS-CoB	MCR catalyzes the methane-forming step in methanogenic archaea	Methanopyrus kandleri	CoM-S-S-CoB + methane	-	?
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	-	?
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	-	?
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	-	?
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	-	?
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	-	?
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	-	?
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	?
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	?
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	?
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	?
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	?
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	?
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	?
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	?
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	?
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	?
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	?
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

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

Synonyms

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

Cofactor

Cofactor	Comment	Organism
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
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
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
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
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
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
F-430	with Ni(I) oxidation state	Methanosarcina barkeri
F-430	with Ni(I) oxidation state	Methanocaldococcus jannaschii
F-430	with Ni(I) oxidation state	Methanococcus voltae
F-430	with Ni(I) oxidation state	Methanoculleus thermophilus
F-430	with Ni(I) oxidation state	Methanothermobacter marburgensis
F-430	with Ni(I) oxidation state	Methanopyrus kandleri