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IUBMB CommentsContains zinc . The enzyme, which is involved in methanogenesis from mono-, di-, and trimethylamine, catalyses the transfer of a methyl group bound to the cobalt cofactor of several corrinoid proteins (mono-, di-, and trimethylamine-specific corrinoid proteins, cf. EC 2.1.1.248, methylamine---corrinoid protein Co-methyltransferase, EC 2.1.1.249, dimethylamine---corrinoid protein Co-methyltransferase, and EC 2.1.1.250, trimethylamine---corrinoid protein Co-methyltransferase) to CoM, forming the substrate for EC 2.8.4.1, coenzyme-B sulfoethylthiotransferase, the enzyme that catalyses the final step in methanogenesis.
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a [methyl-Co(III) dimethylamine-specific corrinoid protein] + coenzyme M
methyl-CoM + a [Co(I) dimethylamine-specific corrinoid protein]
a [methyl-Co(III) methylamine-specific corrinoid protein] + coenzyme M
methyl-CoM + a [Co(I) methylamine-specific corrinoid protein]
a [methyl-Co(III) monomethylamine-specific corrinoid protein] + coenzyme M
methyl-CoM + a [Co(I) monomethylamine-specific corrinoid protein]
a [methyl-Co(III) trimethylamine-specific corrinoid protein] + coenzyme M
methyl-CoM + a [Co(I) trimethylamine-specific corrinoid protein]
HSCoM + methylcobalamin
CH3-SCoM + cob(I)alamin + H+
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-
-
r
[methyl-Co(III) dimethylamine-specific corrinoid protein] + coenzyme M
methyl-CoM + [Co(I) dimethylamine-specific corrinoid protein]
isozyme MT2-A, not MT2-M
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-
r
[methyl-Co(III) monomethylamine-specific corrinoid protein] + coenzyme M
methyl-CoM + [Co(I) monomethylamine-specific corrinoid protein]
isozyme MT2-A, not MT2-M
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-
r
[methyl-Co(III) trimethylamine-specific corrinoid protein] + 3-mercaptopropionate
methyl-3-mercaptopropionate + [Co(I) trimethylamine-specific corrinoid protein]
3-mercaptopropionate is a coenzyme M analogue
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-
?
[methyl-Co(III) trimethylamine-specific corrinoid protein] + coenzyme M
methyl-CoM + [Co(I) trimethylamine-specific corrinoid protein]
additional information
?
-
a [methyl-Co(III) dimethylamine-specific corrinoid protein] + coenzyme M
methyl-CoM + a [Co(I) dimethylamine-specific corrinoid protein]
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-
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-
?
a [methyl-Co(III) dimethylamine-specific corrinoid protein] + coenzyme M
methyl-CoM + a [Co(I) dimethylamine-specific corrinoid protein]
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-
-
-
?
a [methyl-Co(III) dimethylamine-specific corrinoid protein] + coenzyme M
methyl-CoM + a [Co(I) dimethylamine-specific corrinoid protein]
-
-
-
?
a [methyl-Co(III) dimethylamine-specific corrinoid protein] + coenzyme M
methyl-CoM + a [Co(I) dimethylamine-specific corrinoid protein]
-
-
-
-
?
a [methyl-Co(III) methylamine-specific corrinoid protein] + coenzyme M
methyl-CoM + a [Co(I) methylamine-specific corrinoid protein]
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-
-
-
?
a [methyl-Co(III) methylamine-specific corrinoid protein] + coenzyme M
methyl-CoM + a [Co(I) methylamine-specific corrinoid protein]
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-
-
?
a [methyl-Co(III) methylamine-specific corrinoid protein] + coenzyme M
methyl-CoM + a [Co(I) methylamine-specific corrinoid protein]
binding analysis of CoM at the metal center of isozyme MT2-A, overview
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-
?
a [methyl-Co(III) methylamine-specific corrinoid protein] + coenzyme M
methyl-CoM + a [Co(I) methylamine-specific corrinoid protein]
trimethylamine methyl transfer required, neither dimethylamine nor monomethylamine serve as substrate
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-
?
a [methyl-Co(III) monomethylamine-specific corrinoid protein] + coenzyme M
methyl-CoM + a [Co(I) monomethylamine-specific corrinoid protein]
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-
-
-
?
a [methyl-Co(III) monomethylamine-specific corrinoid protein] + coenzyme M
methyl-CoM + a [Co(I) monomethylamine-specific corrinoid protein]
-
-
-
-
?
a [methyl-Co(III) trimethylamine-specific corrinoid protein] + coenzyme M
methyl-CoM + a [Co(I) trimethylamine-specific corrinoid protein]
-
-
-
-
?
a [methyl-Co(III) trimethylamine-specific corrinoid protein] + coenzyme M
methyl-CoM + a [Co(I) trimethylamine-specific corrinoid protein]
-
-
-
-
?
a [methyl-Co(III) trimethylamine-specific corrinoid protein] + coenzyme M
methyl-CoM + a [Co(I) trimethylamine-specific corrinoid protein]
-
-
-
?
a [methyl-Co(III) trimethylamine-specific corrinoid protein] + coenzyme M
methyl-CoM + a [Co(I) trimethylamine-specific corrinoid protein]
-
-
-
-
?
[methyl-Co(III) trimethylamine-specific corrinoid protein] + coenzyme M
methyl-CoM + [Co(I) trimethylamine-specific corrinoid protein]
-
-
-
-
?
[methyl-Co(III) trimethylamine-specific corrinoid protein] + coenzyme M
methyl-CoM + [Co(I) trimethylamine-specific corrinoid protein]
heterolytic cleavage of the methylcobamide carbon-cobalt bond with cob(I)alamin as the major product of the reaction
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-
r
[methyl-Co(III) trimethylamine-specific corrinoid protein] + coenzyme M
methyl-CoM + [Co(I) trimethylamine-specific corrinoid protein]
isozymes MT2-A and MT2-M, heterolytic cleavage of the methylcobamide carbon-cobalt bond with cob(I)alamin as the major product of the reaction
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-
r
[methyl-Co(III) trimethylamine-specific corrinoid protein] + coenzyme M
methyl-CoM + [Co(I) trimethylamine-specific corrinoid protein]
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-
-
-
?
additional information
?
-
corrinoid proteins mediating CoM methylation from dimethylamine or monomethylamine have a specific requirement for MT2-A, reconstitution of trimethylamine-dependent coenzyme M methylation, overview. Trimethylamine methyl transfer can interact with either isozyme of MT2 but has the greatest affinity for the A isozyme. The predominant isozyme of MT2 from in TMA-grown cells is the favored participant in the TMA:CoM methyl transfer reaction
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?
additional information
?
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corrinoid proteins mediating CoM methylation from dimethylamine or monomethylamine have a specific requirement for MT2-A, reconstitution of trimethylamine-dependent coenzyme M methylation, overview. Trimethylamine methyl transfer can interact with either isozyme of MT2 but has the greatest affinity for the A isozyme. The predominant isozyme of MT2 from in TMA-grown cells is the favored participant in the TMA:CoM methyl transfer reaction
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?
additional information
?
-
methylamine-dependent methylation of CoM mediated by trimethyamine- or monomethylamine-specific methyltransferases derived from cells grown on trimethylamine. Methylation of CoM by trimethylamine and methylation by monomethylamine are mediated by separate enzyme systems with at least one different component
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?
additional information
?
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conversions of monomethylamine and dimethylamine to CH3-SCoM are dependent upon MT2-A, and are not supported by MT2-M, both isozymes catalyze S-methylation of 2-thioethanesulfonate, i.e. coenzyme M, and exhibit similar apparent Km values for coenzyme M, isozymes substrate specificities, overview
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?
additional information
?
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the enzyme exhibits MT2 activity, the MT2 activity is measured by following the coenzyme-M-dependent demethylation of methylcobalamin
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?
additional information
?
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the enzyme exhibits MT2 activity, the MT2 activity is measured by following the coenzyme-M-dependent demethylation of methylcobalamin. Trimethylammonium:coenzyme M methyltransferase activity detected by coenzyme M methylation
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?
additional information
?
-
methylamine-dependent methylation of CoM mediated by trimethyamine- or monomethylamine-specific methyltransferases derived from cells grown on trimethylamine. Methylation of CoM by trimethylamine and methylation by monomethylamine are mediated by separate enzyme systems with at least one different component
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?
additional information
?
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the enzyme exhibits MT2 activity, the MT2 activity is measured by following the coenzyme-M-dependent demethylation of methylcobalamin
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?
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a [methyl-Co(III) dimethylamine-specific corrinoid protein] + coenzyme M
methyl-CoM + a [Co(I) dimethylamine-specific corrinoid protein]
a [methyl-Co(III) methylamine-specific corrinoid protein] + coenzyme M
methyl-CoM + a [Co(I) methylamine-specific corrinoid protein]
a [methyl-Co(III) monomethylamine-specific corrinoid protein] + coenzyme M
methyl-CoM + a [Co(I) monomethylamine-specific corrinoid protein]
a [methyl-Co(III) trimethylamine-specific corrinoid protein] + coenzyme M
methyl-CoM + a [Co(I) trimethylamine-specific corrinoid protein]
HSCoM + methylcobalamin
CH3-SCoM + cob(I)alamin + H+
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-
-
r
[methyl-Co(III) trimethylamine-specific corrinoid protein] + coenzyme M
methyl-CoM + [Co(I) trimethylamine-specific corrinoid protein]
heterolytic cleavage of the methylcobamide carbon-cobalt bond with cob(I)alamin as the major product of the reaction
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-
r
additional information
?
-
a [methyl-Co(III) dimethylamine-specific corrinoid protein] + coenzyme M
methyl-CoM + a [Co(I) dimethylamine-specific corrinoid protein]
-
-
-
-
?
a [methyl-Co(III) dimethylamine-specific corrinoid protein] + coenzyme M
methyl-CoM + a [Co(I) dimethylamine-specific corrinoid protein]
-
-
-
-
?
a [methyl-Co(III) dimethylamine-specific corrinoid protein] + coenzyme M
methyl-CoM + a [Co(I) dimethylamine-specific corrinoid protein]
-
-
-
?
a [methyl-Co(III) dimethylamine-specific corrinoid protein] + coenzyme M
methyl-CoM + a [Co(I) dimethylamine-specific corrinoid protein]
-
-
-
-
?
a [methyl-Co(III) methylamine-specific corrinoid protein] + coenzyme M
methyl-CoM + a [Co(I) methylamine-specific corrinoid protein]
-
-
-
-
?
a [methyl-Co(III) methylamine-specific corrinoid protein] + coenzyme M
methyl-CoM + a [Co(I) methylamine-specific corrinoid protein]
-
-
-
?
a [methyl-Co(III) monomethylamine-specific corrinoid protein] + coenzyme M
methyl-CoM + a [Co(I) monomethylamine-specific corrinoid protein]
-
-
-
-
?
a [methyl-Co(III) monomethylamine-specific corrinoid protein] + coenzyme M
methyl-CoM + a [Co(I) monomethylamine-specific corrinoid protein]
-
-
-
-
?
a [methyl-Co(III) trimethylamine-specific corrinoid protein] + coenzyme M
methyl-CoM + a [Co(I) trimethylamine-specific corrinoid protein]
-
-
-
-
?
a [methyl-Co(III) trimethylamine-specific corrinoid protein] + coenzyme M
methyl-CoM + a [Co(I) trimethylamine-specific corrinoid protein]
-
-
-
-
?
a [methyl-Co(III) trimethylamine-specific corrinoid protein] + coenzyme M
methyl-CoM + a [Co(I) trimethylamine-specific corrinoid protein]
-
-
-
?
a [methyl-Co(III) trimethylamine-specific corrinoid protein] + coenzyme M
methyl-CoM + a [Co(I) trimethylamine-specific corrinoid protein]
-
-
-
-
?
additional information
?
-
corrinoid proteins mediating CoM methylation from dimethylamine or monomethylamine have a specific requirement for MT2-A, reconstitution of trimethylamine-dependent coenzyme M methylation, overview. Trimethylamine methyl transfer can interact with either isozyme of MT2 but has the greatest affinity for the A isozyme. The predominant isozyme of MT2 from in TMA-grown cells is the favored participant in the TMA:CoM methyl transfer reaction
-
-
?
additional information
?
-
-
corrinoid proteins mediating CoM methylation from dimethylamine or monomethylamine have a specific requirement for MT2-A, reconstitution of trimethylamine-dependent coenzyme M methylation, overview. Trimethylamine methyl transfer can interact with either isozyme of MT2 but has the greatest affinity for the A isozyme. The predominant isozyme of MT2 from in TMA-grown cells is the favored participant in the TMA:CoM methyl transfer reaction
-
-
?
additional information
?
-
methylamine-dependent methylation of CoM mediated by trimethyamine- or monomethylamine-specific methyltransferases derived from cells grown on trimethylamine. Methylation of CoM by trimethylamine and methylation by monomethylamine are mediated by separate enzyme systems with at least one different component
-
-
?
additional information
?
-
methylamine-dependent methylation of CoM mediated by trimethyamine- or monomethylamine-specific methyltransferases derived from cells grown on trimethylamine. Methylation of CoM by trimethylamine and methylation by monomethylamine are mediated by separate enzyme systems with at least one different component
-
-
?
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malfunction
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immunosorptive depletion of MT2 isozymes from cell-free extracts, extracts of methanol-grown cells depleted of MT2-M lose entirely the ability to carry out conversion of methanol to 2-(methylthio)ethanesulfonate, i.e. methyl-CoM. Methanol:CoM methyl transfer activity is completely restored by addition of purified MT2-M, but no activity is recovered by addition of MT2-A. In contrast, the activity of trimethylamine-grown cell extracts to convert monomethylamine and dimethylamine to methyl-CoM is lost almost entirely by immunosorptive removal of MT2-A. Addition of purified MT2-A but not MT2-M, to the MT2-A-depleted extract fully reconstitutes methyl-CoM formation from both mono- and dimethylamine
evolution
Methanosarcinales are mainly responsible for the utilization of methylamines. mtbA-Specific primers LMTBA/RMTBA-detected sequences from analyzed samples mostly belong to the Methanosarcinales, with two dominating species: Methanosarcina barkeri and Methanomethylovorans hollandica
evolution
-
Methanosarcinales are mainly responsible for the utilization of methylamines. mtbA-Specific primers LMTBA/RMTBA-detected sequences from analyzed samples mostly belong to the Methanosarcinales, with two dominating species: Methanosarcina barkeri and Methanomethylovorans hollandica
metabolism
involvement of MT2-A in monomethylamine metabolism
metabolism
isozyme MT2-A functions in methanogenesis from monomethylamine
metabolism
-
MT2-A plays a specific role in metabolism of methylated amine substrates, whereas, MT2-M functions in methane formation from trimethylamine and methanol, while neither of the two MT2 isozymes is involved in methane formation from acetate
metabolism
the enzyme is involved in the conversion of methylated amines into methyl-CoM, part of the superpathway of methanogenesis, overview
metabolism
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the enzyme is involved in the conversion of methylated amines into methyl-CoM, part of the superpathway of methanogenesis, overview
metabolism
-
isozyme MT2-A functions in methanogenesis from monomethylamine
-
additional information
-
cell extracts of strain NaT1 catalyze the formation of methyl-coenzyme M from coenzyme M and tetramethylammonium, EC 2.1.1.253, or trimethylamine, EC 2.1.1.250, but not from coenzyme M and dimethylamine, EC 2.1.1.249, monomethylamine, EC 2.1.1.248, or methanol, EC 2.1.1.246
additional information
the enzyme shows an active site geometry in which coenzyme M is bound both by S-coordination to zinc, and electrostatic interaction of the sulfonate with a cationic group on the enzyme
additional information
-
cell extracts of strain NaT1 catalyze the formation of methyl-coenzyme M from coenzyme M and tetramethylammonium, EC 2.1.1.253, or trimethylamine, EC 2.1.1.250, but not from coenzyme M and dimethylamine, EC 2.1.1.249, monomethylamine, EC 2.1.1.248, or methanol, EC 2.1.1.246
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Asakawa, S.; Sauer, K.; Liesack, W.; Thauer, R.
Tetramethylammonium:coenzyme M methyltransferase system from Methanococcoides sp.
Arch. Microbiol.
170
220-226
1998
Methanosarcina barkeri, Methanosarcina barkeri NaT1
brenda
Gencic, S.; LeClerc, G.; Gorlatova, N.; Peariso, K.; Penner-Hahn, J.; Grahame, D.
Zinc-thiolate intermediate in catalysis of methyl group transfer in Methanosarcina barkeri
Biochemistry
40
13068-13078
2001
Methanosarcina barkeri (O30640)
brenda
Harms, U.; Thauer, R.
Methylcobalamin:coenzyme M methyltransferase isoenzymes MtaA and MtbA from Methanosarcina barkeri: Cloning, sequencing and differential transcription of the encoding genes, and functional overexpression of the mtaA gene in Escherichia coli
Eur. J. Biochem.
235
653-659
1996
Methanosarcina barkeri, Methanosarcina barkeri DSM 804
brenda
Burke, S.; Krzycki, J.
Involvement of the A isozyme of methyltransferase II and the 29-kilodalton corrinoid protein in methanogenesis from monomethylamine
J. Bacteriol.
177
4410-4416
1995
Methanosarcina barkeri (O30640), Methanosarcina barkeri MS / DSM 800 (O30640)
brenda
Ferguson Jr., D.; Krzycki, J.
Reconstitution of trimethylamine-dependent coenzyme M methylation with the trimethylamine corrinoid protein and the isozymes of methyltransferase II from Methanosarcina barkeri
J. Bacteriol.
179
846-852
1997
Methanosarcina barkeri (O30640), Methanosarcina barkeri
brenda
LeClerc, G.M.; Grahame, D.A.
Methylcobamide:coenzyme M methyltransferase isozymes from Methanosarcina barkeri. Physicochemical characterization, cloning, sequence analysis, and heterologous gene expression
J. Biol. Chem.
271
18725-18731
1996
Methanosarcina barkeri (O30640)
brenda
Ferguson Jr., D.; Krzycki, J.; Grahame, D.
Specific roles of methylcobamide:coenzyme M methyltransferase isozymes in metabolism of methanol and methylamines in Methanosarcina barkeri
J. Biol. Chem.
271
5189-5194
1996
Methanosarcina barkeri
brenda
Hoeppner, A.; Thomas F, Rueppel, A.; Hensel, R.; Blankenfeldt W, Bayer P, Faust A.
Structure of the corrinoid:coenzyme M methyltransferase MtaA from Methanosarcina mazei
Acta Crystallogr. Sect. D
68
1549-1557
2012
Methanosarcina mazei (Q8PXZ6), Methanosarcina mazei, Methanosarcina mazei DSM 3647 (Q8PXZ6)
brenda
Ferguson, D.J.; Gorlatova, N.; Grahame, D.A.; Krzycki, J.A.
Reconstitution of dimethylamine:coenzyme M methyl transfer with a discrete corrinoid protein and two methyltransferases purified from Methanosarcina barkeri
J. Biol. Chem.
275
29053-29060
2000
Methanosarcina barkeri (O30640), Methanosarcina barkeri
brenda
Dziewit, L.; Pyzik, A.; Romaniuk, K.; Sobczak, A.; Szczesny, P.; Lipinski, L.; Bartosik, D.; Drewniak, L.
Novel molecular markers for the detection of methanogens and phylogenetic analyses of methanogenic communities
Front. Microbiol.
6
694
2015
Methanomethylovorans hollandica, Methanosarcina barkeri (O30640)
brenda