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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
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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
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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
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isozyme MT2-A functions in methanogenesis from monomethylamine
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additional information
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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
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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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