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Information on EC 2.1.1.249 - dimethylamine-corrinoid protein Co-methyltransferase and Organism(s) Methanosarcina barkeri and UniProt Accession O30642
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2.1.1.249 dimethylamine-corrinoid protein Co-methyltransferaseIUBMB Comments
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 taxonomic range for the selected organisms is: Methanosarcina barkeri
The expected taxonomic range for this enzyme is: Archaea, Bacteria
The expected taxonomic range for this enzyme is: Archaea, Bacteria
Reaction Schemes
+
=
+
+
a [Co(I) dimethylamine-specific corrinoid protein]
=
a [methyl-Co(III) dimethylamine-specific corrinoid protein]
+
Synonyms
mtbb1, dma-mt, dma methyltransferase, mtbb2, mtbb3, dimethylamine/5-hydroxybenzimidazolylcobamide methyltransferase, dimethylamine:corrinoid methyltransferase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
dimethylamine/5-hydroxybenzimidazolylcobamide methyltransferase
-
-
DMA methyltransferase
MtbB
MtbB1
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
dimethylamine + a [Co(I) dimethylamine-specific corrinoid protein] = a [methyl-Co(III) dimethylamine-specific corrinoid protein] + methylamine
mechanism of the dimethylamine/coenzyme M methyltransfer, detailed overview
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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
53414-88-3
methylcobalamin-coenzyme M methyltransferase, EC 2.1.1.246 to EC 2.1.1.253
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
dimethylamine + a [Co(I) dimethylamine-specific corrinoid protein]
a [methyl-Co(III) dimethylamine-specific corrinoid protein] + methylamine
-
-
-
?
dimethylamine + a [Co(I) dimethylamine-specific corrinoid protein]
a [methyl-Co(III) dimethylamine-specific corrinoid protein] + methylamine
dimethylamine + a [Co(I) methylamine-specific corrinoid protein]
a [methyl-Co(III) dimethylamine-specific corrinoid protein] + methylamine
-
-
-
?
dimethylamine + a [Co(I) dimethylamine-specific corrinoid protein]
a [methyl-Co(III) dimethylamine-specific corrinoid protein] + methylamine
-
-
-
-
?
dimethylamine + a [Co(I) dimethylamine-specific corrinoid protein]
a [methyl-Co(III) dimethylamine-specific corrinoid protein] + methylamine
-
-
-
?
dimethylamine + a [Co(I) dimethylamine-specific corrinoid protein]
a [methyl-Co(III) dimethylamine-specific corrinoid protein] + methylamine
-
-
-
?
dimethylamine + a [Co(I) dimethylamine-specific corrinoid protein]
a [methyl-Co(III) dimethylamine-specific corrinoid protein] + methylamine
-
methylation of the corrinoid prosthetic group
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-
?
dimethylamine + a [Co(I) dimethylamine-specific corrinoid protein]
a [methyl-Co(III) dimethylamine-specific corrinoid protein] + methylamine
the DMA methyltransferase cognate corrinoid protein MtbC
-
-
?
dimethylamine + a [Co(I) dimethylamine-specific corrinoid protein]
a [methyl-Co(III) dimethylamine-specific corrinoid protein] + methylamine
-
the methylation is specifically reversed by methylamine
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-
?
dimethylamine + a [Co(I) dimethylamine-specific corrinoid protein]
a [methyl-Co(III) dimethylamine-specific corrinoid protein] + methylamine
the enzyme demethylates dimethylamine and specifically methylates the corrinoid prosthetic group of the corrinoid protein MtbC
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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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-
?
additional information
?
-
-
dimethylamine-dependent methylation of free cobalamin by MtbB1, kinetics, overview
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-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
dimethylamine + a [Co(I) dimethylamine-specific corrinoid protein]
a [methyl-Co(III) dimethylamine-specific corrinoid protein] + methylamine
-
-
-
?
dimethylamine + a [Co(I) dimethylamine-specific corrinoid protein]
a [methyl-Co(III) dimethylamine-specific corrinoid protein] + methylamine
dimethylamine + a [Co(I) methylamine-specific corrinoid protein]
a [methyl-Co(III) dimethylamine-specific corrinoid protein] + methylamine
-
-
-
?
additional information
?
-
-
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
-
-
?
dimethylamine + a [Co(I) dimethylamine-specific corrinoid protein]
a [methyl-Co(III) dimethylamine-specific corrinoid protein] + methylamine
-
-
-
-
?
dimethylamine + a [Co(I) dimethylamine-specific corrinoid protein]
a [methyl-Co(III) dimethylamine-specific corrinoid protein] + methylamine
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
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
LITERATURE
additional information
additional information
-
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
additional information
-
Co(I) dimethylamine-specific corrinoid protein, prosthetic group
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Monomethylamine
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MMA, acts as competitive inhibitor of the reaction. The methylation is specifically reversed by MMA
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ATP
-
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
methyltransferase activating protein
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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
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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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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
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
physiological function
the enzyme is involved in the corrinoid-dependent demethylation of methylamines, which are used for coenzyme M methylation
metabolism
additional information
metabolism
-
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
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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
-
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
additional information
-
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
-
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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
230000
50000
51000
51000
homotetramer or possibly homopentamer, 4 or 5 * 51000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
mass spectrometric structure analysis, overview, primary structure of MtbB
?
homotetramer or possibly homopentamer, 4 or 5 * 51000, SDS-PAGE
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
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Bose, A.; Pritchett, M.A.; Rother, M.; Metcalf, W.W.
Differential regulation of the three methanol methyltransferase isozymes in Methanosarcina acetivorans C2A
J. Bacteriol.
188
7274-7283
2006
Methanosarcina barkeri
Krzycki, J.
Function of genetically encoded pyrrolysine in corrinoid-dependent methylamine methyltransferases
Curr. Opin. Chem. Biol.
8
484-491
2004
Methanosarcina barkeri (O30642)
Wassenaar, R.; Keltjens, J.; Van Der Drift, C.; Vogels, G.
Purification and characterization of dimethylamine: 5-hydroxybenzimidazolyl-cobamide methyltransferase from Methanosarcina barkeri Fusaro
Eur. J. Biochem.
253
692-697
1998
Methanosarcina barkeri, Methanosarcina barkeri Fusaro / DSM 804
Wassenaar, R.; Keltjens, J.; Van Der Drift, C.
Activation and reaction kinetics of the dimethylamine/coenzyme M methyltransfer in Methanosarcina barkeri strain Fusaro
Eur. J. Biochem.
258
597-602
1998
Methanosarcina barkeri, Methanosarcina barkeri DSM 804
Paul, L.; Ferguson Jr., D.; Krzycki, J.
The trimethylamine methyltransferase gene and multiple dimethylamine methyltransferase genes of Methanosarcina barkeri contain in-frame and read-through amber codons
J. Bacteriol.
182
2520-2529
2000
Methanosarcina barkeri (O93661), Methanosarcina barkeri (Q9P9M9), Methanosarcina barkeri (Q9P9N0), Methanosarcina barkeri
Soares, J.; Zhang, L.; Pitsch, R.; Kleinholz, N.; Jones, R.; Wolff, J.; Amster, J.; Green-Church, K.; Krzyck, J.
The residue mass of L-pyrrolysine in three distinct methylamine methyltransferases
J. Biol. Chem.
280
36962-36969
2005
Methanosarcina barkeri (Q9P9N0), Methanosarcina barkeri MS / DSM 800 (Q9P9N0)
Ferguson, T.; Soares, J.; Lienard, T.; Gottschalk, G.; Krzycki, J.
RamA, a protein required for reductive activation of corrinoid-dependent methylamine methyltransferase reactions in methanogenic archaea
J. Biol. Chem.
284
2285-2295
2009
Methanosarcina barkeri
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
J. Biol. Chem.
275
29053-29060
2000
Methanosarcina barkeri (O93661), Methanosarcina barkeri
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