EC Number |
General Information |
Reference |
---|
2.1.1.247 | 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 |
736150 |
2.1.1.247 | malfunction |
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 |
717754 |
2.1.1.247 | metabolism |
involvement of MT2-A in monomethylamine metabolism |
717718 |
2.1.1.247 | metabolism |
isozyme MT2-A functions in methanogenesis from monomethylamine |
-, 717713 |
2.1.1.247 | 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 |
717754 |
2.1.1.247 | metabolism |
the enzyme is involved in the conversion of methylated amines into methyl-CoM, part of the superpathway of methanogenesis, overview |
736150 |
2.1.1.247 | more |
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 |
-, 717162 |
2.1.1.247 | more |
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 |
717753 |