Information on EC 2.1.1.249 - dimethylamine-corrinoid protein Co-methyltransferase

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The expected taxonomic range for this enzyme is: Methanosarcina

EC NUMBER
COMMENTARY hide
2.1.1.249
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RECOMMENDED NAME
GeneOntology No.
dimethylamine-corrinoid protein Co-methyltransferase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
dimethylamine + a [Co(I) dimethylamine-specific corrinoid protein] = a [methyl-Co(III) dimethylamine-specific corrinoid protein] + methylamine
show the reaction diagram
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Methane metabolism
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methanogenesis from dimethylamine
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Microbial metabolism in diverse environments
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SYSTEMATIC NAME
IUBMB Comments
dimethylamine:5-hydroxybenzimidazolylcobamide Co-methyltransferase
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.
CAS REGISTRY NUMBER
COMMENTARY hide
53414-88-3
methylcobalamin-coenzyme M methyltransferase, EC 2.1.1.246 to EC 2.1.1.253
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene mtbB
UniProt
Manually annotated by BRENDA team
DSM 3647, genes mtbB1 and mtbB2C2
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
physiological function
the enzyme is involved in the corrinoid-dependent demethylation of methylamines, which are used for coenzyme M methylation
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
dimethylamine + a [Co(I) dimethylamine-specific corrinoid protein]
a [methyl-Co(III) dimethylamine-specific corrinoid protein] + methylamine
show the reaction diagram
dimethylamine + a [Co(I) methylamine-specific corrinoid protein]
a [methyl-Co(III) dimethylamine-specific corrinoid protein] + methylamine
show the reaction diagram
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?
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
dimethylamine + a [Co(I) dimethylamine-specific corrinoid protein]
a [methyl-Co(III) dimethylamine-specific corrinoid protein] + methylamine
show the reaction diagram
dimethylamine + a [Co(I) methylamine-specific corrinoid protein]
a [methyl-Co(III) dimethylamine-specific corrinoid protein] + methylamine
show the reaction diagram
Q9P9N0
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?
additional information
?
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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
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Co(I) dimethylamine-specific corrinoid protein
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corrinoid prosthetic group
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corrinoid protein
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prosthetic group, with a corrinoid content of 0.9 mol B12/mol holoenzyme
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Zn2+
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0.43 mol of zinc/mol of polypeptide
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Monomethylamine
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ATP
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acts as a powerful allosteric effector on the methyltransferase reaction. ATP serves as the substrate for MAP, which, after being phosporylated by ATP, operates in the reductive activation of the corrinoid methyltransferase
methyltransferase activating protein
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MAP, dependent on. ATP serves as the substrate for MAP, which, after being phosporylated by ATP, operates in the reductive activation of the corrinoid methyltransferase
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RamA
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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
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additional information
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as isolated, DMA-MT is inactive, but it can enzymically be reactivated by methyltransferase activating protein, ATP, and hydrogenase
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4.5
Monomethylamine
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pH 7.0, 37C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1.74
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pH 7.4, 37C
1.89
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purified enzyme, pH 6.5, 23C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 46
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rapid decline of activity above 46C, inactive at 55C
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.7
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isoelectric focusing
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
100000
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gel filtration
230000
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
oligomer
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x * 51000, SDS-PAGE
additional information
mass spectrometric structure analysis, overview, primary structure of MtbB
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
native enzyme 35.2fold MtbB1 by two steps of anion exchange chromatography, and adsorption and hydrophobic interaction chromatography
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native enzyme 62.8fold by ammonium sulfate fractionation, hydrophobic interaction chromatography, ultrafiltration, and anion exchange chromatography
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native enzyme by three different steps of anion exchange chromatography, adsorption and hydrophobic interaction chromatography
native enzyme to homogeneity
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene mtbB, DNA and amino acid sequence determination and analysis, UAG is not the stop codon in the encoding gene, no UAG modification
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, 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
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
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