2.1.1.248: methylamine-corrinoid protein Co-methyltransferase
This is an abbreviated version!
For detailed information about methylamine-corrinoid protein Co-methyltransferase, go to the full flat file.
Word Map on EC 2.1.1.248
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2.1.1.248
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methanosarcina
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barkeri
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methyltransferases
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pyrrolysine
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amber
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methanogenesis
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methanogen
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in-frame
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trnapyl
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dimethylamine
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acetivorans
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pyrrolysyl-trna
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aminoacylated
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lysyl-trna
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dimethylarsinic
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synthetases
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arsenite
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monomethylarsonate
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lysrs1
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selenocysteine
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pylts
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synthetase-like
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methylarsonic
- 2.1.1.248
- methanosarcina
- barkeri
- methyltransferases
- pyrrolysine
-
amber
-
methanogenesis
-
methanogen
-
in-frame
- trnapyl
- dimethylamine
- acetivorans
-
pyrrolysyl-trna
-
aminoacylated
- lysyl-trna
-
dimethylarsinic
- synthetases
- arsenite
- monomethylarsonate
- lysrs1
- selenocysteine
-
pylts
-
synthetase-like
-
methylarsonic
Reaction
Synonyms
corrinoid-dependent methylamine methyltransferase, MMA methyltransferase, MMA:CoM methyltransferase, MMA:MMCP methyltransferase, MMAMT, monomethylamine methyltransferase, monomethylamine:coenzyme M methyl transferase, monomethylamine:MMCP methyltransferase, MtmB, mtmB1, mtmB2
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General Information
General Information on EC 2.1.1.248 - methylamine-corrinoid protein Co-methyltransferase
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metabolism
physiological function
additional information
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archaeal methane formation from methylamines is initiated by distinct methyltransferases with specificity for monomethylamine, dimethylamine, or trimethylamine. Each methylamine methyltransferase methylates a cognate corrinoid protein, which is subsequently demethylated by a second methyltransferase to form methyl-coenzyme M, the direct methane precursor
metabolism
biochemistry of methane formation by Methanosarcina species from monomethylamine, dimethylamine, and trimethylamine: methanogenesis from these substrates is initiated by three methyltransferases that specifically methylate their cognate corrinoid proteins with one of these methylamines, cf. EC 2.1.1.250 and EC 2.1.1.249, overview
metabolism
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when growing on trimethylamine, nitrogen fixation does not occur in the cells, indicating that ammonium released during trimethylamine degradation is sufficient to serve as a nitrogen source and represses nif gene induction, transcriptional regulation of soluble methyltransferases, which catalyze the initial step of methylamine consumption by methanogenesis, in response to different carbon and nitrogen sources, overview. Regulation of soluble methyltransferases in response to different nitrogen and carbon sources, overview
metabolism
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when growing on trimethylamine, nitrogen fixation does not occur in the cells, indicating that ammonium released during trimethylamine degradation is sufficient to serve as a nitrogen source and represses nif gene induction, transcriptional regulation of soluble methyltransferases, which catalyze the initial step of methylamine consumption by methanogenesis, in response to different carbon and nitrogen sources, overview. Regulation of soluble methyltransferases in response to different nitrogen and carbon sources, overview
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the enzyme is involved in the corrinoid-dependent demethylation of methylamines, which are used for coenzyme M methylation, homology modeling of MtmC, the methylamine-specific corrinoid protein. Pyrrolysine in MtmB mediates methylation of MtmC
physiological function
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the MMAMT polypeptide is rate-limiting for methyl transfer until at a 2fold molar excess over monomethylamine corrinoid protein, MMCP. MMAMT and MMCP form a complex. MMCP is the major corrinoid protein for methanogenesis from monomethylamine
single in-frame amber UAG codons are found in the genes encoding MtmB, MtbB, or MttB, the methyltransferases initiating methane formation from monomethylamine, dimethylamine, or trimethylamine, respectively, in certain Archaea. The amber codon codes for pyrrolysine, the 22nd genetically encoded amino acid found in nature
additional information
single in-frame amber UAG codons are found in the genes encoding MtmB, MtbB, or MttB, the methyltransferases initiating methane formation from monomethylamine, dimethylamine, or trimethylamine, respectively, in certain Archaea. The amber codon codes for pyrrolysine, the 22nd genetically encoded amino acid found in nature
additional information
the enzyme contains pyrrolysine at the UAG posotion, crystal structure of MtmB reveals lysine, but with epsilonN in amide linkage with (4R,5R)-4 substituted-pyrroline-5-carboxylate
additional information
Methanosarcina barkeri MS / DSM 800
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single in-frame amber UAG codons are found in the genes encoding MtmB, MtbB, or MttB, the methyltransferases initiating methane formation from monomethylamine, dimethylamine, or trimethylamine, respectively, in certain Archaea. The amber codon codes for pyrrolysine, the 22nd genetically encoded amino acid found in nature
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