The enzyme, which catalyses the transfer of a methyl group from dimethylamine to a dimethylamine-specific corrinoid protein (MtbC), is involved in methanogenesis from dimethylamine. The enzyme contains the unusual amino acid pyrrolysine . Methylation of the corrinoid protein requires the central cobalt to be in the Co(I) state. During methylation the cobalt is oxidized to the Co(III) state. The methylated corrinoid protein is substrate for EC 2.1.1.247, methylated methylamine-specific corrinoid protein:coenzyme M methyltransferase.
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The expected taxonomic range for this enzyme is: Archaea, Bacteria
The enzyme, which catalyses the transfer of a methyl group from dimethylamine to a dimethylamine-specific corrinoid protein (MtbC), is involved in methanogenesis from dimethylamine. The enzyme contains the unusual amino acid pyrrolysine [3]. Methylation of the corrinoid protein requires the central cobalt to be in the Co(I) state. During methylation the cobalt is oxidized to the Co(III) state. The methylated corrinoid protein is substrate for EC 2.1.1.247, methylated methylamine-specific corrinoid protein:coenzyme M methyltransferase.
MtbB1 demethylates dimethylamine and specifically methylates the corrinoid prosthetic group of MtbC, which is subsequently demethylated by MtbA to methylate coenzyme M during methanogenesis from dimethylamine. A MtbB1to corrinoid protein MtbC ratio of 1 is optimal for coenzyme M methylation with dimethylamine. MtbB1 methylated either corrinoid bound to MtbC or free cob(I)alamin with dimethylamine, indicating MtbB1 carries an active site for dimethylamine demethylation and corrinoid methylation
MtbB1 demethylates dimethylamine and specifically methylates the corrinoid prosthetic group of MtbC, which is subsequently demethylated by MtbA to methylate coenzyme M during methanogenesis from dimethylamine. A MtbB1to corrinoid protein MtbC ratio of 1 is optimal for coenzyme M methylation with dimethylamine. MtbB1 methylated either corrinoid bound to MtbC or free cob(I)alamin with dimethylamine, indicating MtbB1 carries an active site for dimethylamine demethylation and corrinoid methylation
analysis of the metal content of MtbB1 by plasma emission spectroscopy revealed no detectable cobalt with a lower limit of detection for cobalt of 0.04 mol of cobalt/mol of polypeptide
acts as a powerful allosteric effector on the methyltransferase reaction. ATP serves as the substrate for MAP, which, after being phosphorylated by ATP, operates in the reductive activation of the corrinoid methyltransferase
MAP, dependent on. ATP serves as the substrate for MAP, which, after being phosphorylated by ATP, operates in the reductive activation of the corrinoid methyltransferase
a 60-kDa monomeric iron sulfur protein, is a protein required for reductive activation of corrinoid-dependent methylamine methyltransferase reactions in methanogenic archaea, it is required for in vitro ATP-dependent reductive activation of dimethylamine:CoM methyl transfer mediating the ATP-dependent reductive activation of Co(II) corrinoid to the Co(I) state for the trimethylamine corrinoid protein, MtbC, overview
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
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
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
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
three different methyltransferases initiate methanogenesis from trimethylamine, dimethylamine, or monomethylamine by methylating different cognate corrinoid proteins that are subsequently used to methylate coenzyme M
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
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
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
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
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
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
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
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
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
gene mtbB2, DNA and amino acid sequence determination and analysis, homology sequence comparison, co-transcription with of gene mttB encoding the TMA methyltransferase. The genes, organized on the chromosome in the order mtbC, mttB, mttC, mttP, and mtbB1, form a single transcriptional unit. The genes encoding the three types of methyltransferases that initiate methanogenesis from methylamine contain in-frame amber codons that are suppressed during expression of the characterized methyltransferases
gene mtbB3, DNA and amino acid sequence determination and analysis, homology sequence comparison, co-transcription with of gene mttB encoding the TMA methyltransferase. The genes, organized on the chromosome in the order mtbC, mttB, mttC, mttP, and mtbB1, form a single transcriptional unit. The genes encoding the three types of methyltransferases that initiate methanogenesis from methylamine contain in-frame amber codons that are suppressed during expression of the characterized methyltransferases
genes mtbB1 and mtbB2C2, operon encoding DMA methylamine methyltransferase, quantitative RT-PCR expression analysis, comparison with other methylamine methyltransferases, overview. Transcriptional regulation of genes encoding methylamine methyltransferases in cells growing on trimethylamine or methanol in the presence of ammonium, overview
genes mtbB1, mtbB2, and mtbB3, DNA and amino acid sequence determination and analysis, homology sequence comparison, co-transcription with of gene mttB encoding the TMA methyltransferase. The genes, organized on the chromosome in the order mtbC, mttB, mttC, mttP, and mtbB1, form a single transcriptional unit. The genes encoding the three types of methyltransferases that initiate methanogenesis from methylamine contain in-frame amber codons that are suppressed during expression of the characterized methyltransferases
The trimethylamine methyltransferase gene and multiple dimethylamine methyltransferase genes of Methanosarcina barkeri contain in-frame and read-through amber codons
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