The enzyme, which catalyses the transfer of a methyl group from trimethylamine to a trimethylamine-specific corrinoid protein (MttC), is involved in methanogenesis from trimethylamine. 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.
The enzyme, which catalyses the transfer of a methyl group from trimethylamine to a trimethylamine-specific corrinoid protein (MttC), is involved in methanogenesis from trimethylamine. The enzyme contains the unusual amino acid pyrrolysine [2]. 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.
ability of the recombinant DSY3156 protein to methylate cob(I)alamin with various substrates. Quaternary amines such as carnitine and choline do not serve as substrates, nor do tertiary amines such as dimethylglycine or trimethylamine. Instead, DSY3156 protein carries out a robust methylation of cob(I)alamin in the presence of glycine betaine
ability of the recombinant DSY3156 protein to methylate cob(I)alamin with various substrates. Quaternary amines such as carnitine and choline do not serve as substrates, nor do tertiary amines such as dimethylglycine or trimethylamine. Instead, DSY3156 protein carries out a robust methylation of cob(I)alamin in the presence of glycine betaine
ability of the recombinant DSY3156 protein to methylate cob(I)alamin with various substrates. Quaternary amines such as carnitine and choline do not serve as substrates, nor do tertiary amines such as dimethylglycine or trimethylamine. Instead, DSY3156 protein carries out a robust methylation of cob(I)alamin in the presence of glycine betaine
ability of the recombinant DSY3156 protein to methylate cob(I)alamin with various substrates. Quaternary amines such as carnitine and choline do not serve as substrates, nor do tertiary amines such as dimethylglycine or trimethylamine. Instead, DSY3156 protein carries out a robust methylation of cob(I)alamin in the presence of glycine betaine
ability of the recombinant DSY3156 protein to methylate cob(I)alamin with various substrates. Quaternary amines such as carnitine and choline do not serve as substrates, nor do tertiary amines such as dimethylglycine or trimethylamine. Instead, DSY3156 protein carries out a robust methylation of cob(I)alamin in the presence of glycine betaine
ability of the recombinant DSY3156 protein to methylate cob(I)alamin with various substrates. Quaternary amines such as carnitine and choline do not serve as substrates, nor do tertiary amines such as dimethylglycine or trimethylamine. Instead, DSY3156 protein carries out a robust methylation of cob(I)alamin in the presence of glycine betaine
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 trimethylamine:CoM methyl transfer mediating the ATP-dependent reductive activation of Co(II) corrinoid to the Co(I) state for the trimethylamine corrinoid protein, MttC, overview
the enzyme belongs to the COG5598 MttB superfamily. Based on the draft B1d genome, MV8460 is the sole Pyl-lacking MttB found in B1d, which is 65% identical and has 83% sequence similarity to Desulfitobacterium hafniense Y51 DhMtgB. Four predicted active site residues may interact with GB as they are conserved between DhMtgB and MV8460: Y94, N199, R309, and H345
the enzyme belongs to the COG5598 MttB superfamily. Based on the draft B1d genome, MV8460 is the sole Pyl-lacking MttB found in B1d, which is 65% identical and has 83% sequence similarity to Desulfitobacterium hafniense Y51 DhMtgB. Four predicted active site residues may interact with GB as they are conserved between DhMtgB and MV8460: Y94, N199, R309, and H345
the enzyme belongs to the COG5598 MttB superfamily. Based on the draft B1d genome, MV8460 is the sole Pyl-lacking MttB found in B1d, which is 65% identical and has 83% sequence similarity to Desulfitobacterium hafniense Y51 DhMtgB. Four predicted active site residues may interact with GB as they are conserved between DhMtgB and MV8460: Y94, N199, R309, and H345
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 2.1.1.248 and EC 2.1.1.249, overview
three different methyltransferases initiate methanogenesis from trimethylamine, dimethylamine, or monomethylamine by methylating different cognate corrinoid proteins that are subsequently used to methylate coenzyme M
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 TMA methyltransferase is not regulated in response to the nitrogen source. Regulation of soluble methyltransferases in response to different nitrogen and carbon sources, overview
the enzyme is involved in the the glycine betaine-dependent methylotrophic methanogenesis pathway. Environmentally abundant quaternary amines (QAs) are a primary source for methanogenesis. The methanogenic archaeon Methanolobus vulcani B1d metabolizes glycine betaine (GB) through a corrinoid-dependent GB:coenzyme M (CoM) methyl transfer pathway
the enzyme is involved in the the glycine betaine-dependent methylotrophic methanogenesis pathway. Environmentally abundant quaternary amines (QAs) are a primary source for methanogenesis. The methanogenic archaeon Methanolobus vulcani B1d metabolizes glycine betaine (GB) through a corrinoid-dependent GB:coenzyme M (CoM) methyl transfer pathway
the enzyme is involved in the the glycine betaine-dependent methylotrophic methanogenesis pathway. Environmentally abundant quaternary amines (QAs) are a primary source for methanogenesis. The methanogenic archaeon Methanolobus vulcani B1d metabolizes glycine betaine (GB) through a corrinoid-dependent GB:coenzyme M (CoM) methyl transfer pathway
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 TMA methyltransferase is not regulated in response to the nitrogen source. Regulation of soluble methyltransferases in response to different nitrogen and carbon sources, overview
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
the determined N-terminus of MttB, encoded by mttB, shows a UAG codon, which is represented in both strands of the DNA, follows at codon position 334. Cessation of translation at the UAG codon results in a 34-kDa product rather than the abundant 53-kDa polypeptide purified from TMA-grown cells
the determined N-terminus of MttB, encoded by mttB, shows a UAG codon, which is represented in both strands of the DNA, follows at codon position 334. Cessation of translation at the UAG codon results in a 34-kDa product rather than the abundant 53-kDa polypeptide purified from TMA-grown cells
the determined N-terminus of MttB, encoded by mttB, shows a UAG codon, which is represented in both strands of the DNA, follows at codon position 334. Cessation of translation at the UAG codon results in a 34-kDa product rather than the abundant 53-kDa polypeptide purified from TMA-grown cells
the determined N-terminus of MttB, encoded by mttB, shows a UAG codon, which is represented in both strands of the DNA, follows at codon position 334. Cessation of translation at the UAG codon results in a 34-kDa product rather than the abundant 53-kDa polypeptide purified from TMA-grown cells
gene mttB, co-transcription with gene mtbB1 encoding the DMA methyltransferase. The genes, organized on the chromosome in the order mtbC, mttB, mttC, mttP, and mtbB1, form a single transcriptional unit. The genes of all methyltransferases each contain a single in-frame amber codon
gene mttB1C1, operon encoding TMA methylamine methyltransferase, quantitative RT-PCR expression analysis, comparison with other methylamine methyltransferases, overview. Transcriptional regulation of genes encoding methylamine methyltransferases (MT) in cells growing on TMA or methanol in the presence of ammonium, overview
gene mttB2C2, operon encoding TMA methylamine methyltransferase, quantitative RT-PCR expression analysis, comparison with other methylamine methyltransferases, overview. Transcriptional regulation of genes encoding methylamine methyltransferases (MT) in cells growing on TMA or methanol in the presence of ammonium, overview
gene mttB, co-transcription with gene mtbB1 encoding the DMA methyltransferase. The genes, organized on the chromosome in the order mtbC, mttB, mttC, mttP, and mtbB1, form a single transcriptional unit. The genes of all methyltransferases each contain a single in-frame amber codon
gene mttB, co-transcription with gene mtbB1 encoding the DMA methyltransferase. The genes, organized on the chromosome in the order mtbC, mttB, mttC, mttP, and mtbB1, form a single transcriptional unit. The genes of all methyltransferases each contain a single in-frame amber codon
transcription of the mtmB1C1 operon is not affected by the nitrogen source but appears to be increased when trimethylamine is the sole carbon and energy source. Transcription of the homologous mtmB1C1 operon occurs at a constant level independently of the nitrogen source
under nitrogen limitation, a 543fold up-regulation of the mtmB2C2 operon, encoding MMA methyltransferase 2, is obtained when methanol is used as carbon source
transcription of the mtmB1C1 operon is not affected by the nitrogen source but appears to be increased when trimethylamine is the sole carbon and energy source. Transcription of the homologous mtmB1C1 operon occurs at a constant level independently of the nitrogen source
transcription of the mtmB1C1 operon is not affected by the nitrogen source but appears to be increased when trimethylamine is the sole carbon and energy source. Transcription of the homologous mtmB1C1 operon occurs at a constant level independently of the nitrogen source
under nitrogen limitation, a 543fold up-regulation of the mtmB2C2 operon, encoding MMA methyltransferase 2, is obtained when methanol is used as carbon source
under nitrogen limitation, a 543fold up-regulation of the mtmB2C2 operon, encoding MMA methyltransferase 2, is obtained when methanol is used as carbon source
The trimethylamine methyltransferase gene and multiple dimethylamine methyltransferase genes of Methanosarcina barkeri contain in-frame and read-through amber codons