2.1.1.249: dimethylamine-corrinoid protein Co-methyltransferase
This is an abbreviated version!
For detailed information about dimethylamine-corrinoid protein Co-methyltransferase, go to the full flat file.
Reaction
Synonyms
dimethyl-12-HBI methyltransferase, dimethylamine methyltransferase, dimethylamine/5-hydroxybenzimidazolylcobamide methyltransferase, dimethylamine: corrinoid methyltransferase, dimethylamine:CoM methyltransferase, dimethylamine:corrinoid methyltransferase, DMA methyltransferase, DMA-MT, DMA:CoM methyltransferase, DMA:corrinoid methyltransferase, MtbB, MtbB1, MtbB2, MtbB3, MtcB
ECTree
2.1.1.249 dimethylamine-corrinoid protein Co-methyltransferaseAdvanced search results
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General Information on EC 2.1.1.249 - dimethylamine-corrinoid protein Co-methyltransferase
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GENERAL INFORMATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
metabolism
physiological function
the enzyme is involved in the corrinoid-dependent demethylation of methylamines, which are used for coenzyme M methylation
additional information
metabolism
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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 2.1.1.248, overview
metabolism
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highly purified dimethylamine: corrinoid methyltransferase MtbB1, corrinoid protein MtbC, and methylcorrinoid:coenzyme M methyltransferase MtbA, EC 2.1.1.247, are sufficient to catalyze in vitro CoM methylation by DMA
metabolism
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the methyl group bound to the corrinoid prosthetic group of DMA-MT is subsequently transferred to coenzyme M in a reaction mediated by methylcobalamin/coenzyme M methyltransferase isoenzyme II, EC 2.1.1.247, which binds with high affinity to DMA-MT
metabolism
three different methyltransferases initiate methanogenesis from trimethylamine, dimethylamine, or monomethylamine by methylating different cognate corrinoid proteins that are subsequently used to methylate coenzyme M
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. Transcription of the operon encoding DMA methyltransferase is not regulated in response to the nitrogen source. 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. Transcription of the operon encoding DMA methyltransferase is not regulated in response to the nitrogen source. Regulation of soluble methyltransferases in response to different nitrogen and carbon sources, overview
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metabolism
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the methyl group bound to the corrinoid prosthetic group of DMA-MT is subsequently transferred to coenzyme M in a reaction mediated by methylcobalamin/coenzyme M methyltransferase isoenzyme II, EC 2.1.1.247, which binds with high affinity to DMA-MT
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additional information
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as-isolated DMA-MT is inactive. The enzyme can be reactivated to yield the methylated B12-HBI prosthetic group by a system that comprises a methyl donor, a reductant, ATP and one (or more) component(s) present in the partially purified methyltransferase activating protein, MAP, fraction
additional information
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as-isolated DMA-MT is inactive. The enzyme can be reactivated to yield the methylated B12-HBI prosthetic group by a system that comprises a methyl donor, a reductant, ATP and one (or more) component(s) present in the partially purified methyltransferase activating protein, MAP, fraction
additional information
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MtbB1 is a 230-kDa protein composed of 51-kDa subunits that do not possess a corrinoid prosthetic group
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
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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additional information
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as-isolated DMA-MT is inactive. The enzyme can be reactivated to yield the methylated B12-HBI prosthetic group by a system that comprises a methyl donor, a reductant, ATP and one (or more) component(s) present in the partially purified methyltransferase activating protein, MAP, fraction
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additional information
Methanosarcina barkeri Fusaro / DSM 804
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as-isolated DMA-MT is inactive. The enzyme can be reactivated to yield the methylated B12-HBI prosthetic group by a system that comprises a methyl donor, a reductant, ATP and one (or more) component(s) present in the partially purified methyltransferase activating protein, MAP, fraction
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