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Information on EC 2.1.1.247 - [methyl-Co(III) methylamine-specific corrinoid protein]:coenzyme M methyltransferase and Organism(s) Methanosarcina barkeri and UniProt Accession O30640
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2.1.1.247 [methyl-Co(III) methylamine-specific corrinoid protein]:coenzyme M methyltransferaseIUBMB Comments
Contains zinc . The enzyme, which is involved in methanogenesis from mono-, di-, and trimethylamine, catalyses the transfer of a methyl group bound to the cobalt cofactor of several corrinoid proteins (mono-, di-, and trimethylamine-specific corrinoid proteins, cf. EC 2.1.1.248, methylamine---corrinoid protein Co-methyltransferase, EC 2.1.1.249, dimethylamine---corrinoid protein Co-methyltransferase, and EC 2.1.1.250, trimethylamine---corrinoid protein Co-methyltransferase) to CoM, forming the substrate for EC 2.8.4.1, coenzyme-B sulfoethylthiotransferase, the enzyme that catalyses the final step in methanogenesis.
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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 [methyl-Co(III) methylamine-specific corrinoid protein]
+
=
+
a [Co(I) methylamine-specific corrinoid protein]
Synonyms
methylcorrinoid:com methyltransferase, corrinoid:coenzyme m methyltransferase, methylcorrinoid:coenzyme m methyltransferase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
methylated [methylamine-specific corrinoid protein]:coenzymeM methyltransferase
-
MT2-A
mtbA
MT2-A
-
-
-
-
mtbA
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a [methyl-Co(III) methylamine-specific corrinoid protein] + CoM = methyl-CoM + a [Co(I) methylamine-specific corrinoid protein]
catalysis by MT2 proceeds by nucleophilic substitution, with attack of CoM on the methylcorrinoid Co3+-methyl group and expulsion of the demethylated corrinoid in the Co1+ form
PATHWAY SOURCE
PATHWAYS
-
-, -, -
SYSTEMATIC NAME
IUBMB Comments
methylated monomethylamine-specific corrinoid protein:coenzyme M methyltransferase
Contains zinc [2]. The enzyme, which is involved in methanogenesis from mono-, di-, and trimethylamine, catalyses the transfer of a methyl group bound to the cobalt cofactor of several corrinoid proteins (mono-, di-, and trimethylamine-specific corrinoid proteins, cf. EC 2.1.1.248, methylamine---corrinoid protein Co-methyltransferase, EC 2.1.1.249, dimethylamine---corrinoid protein Co-methyltransferase, and EC 2.1.1.250, trimethylamine---corrinoid protein Co-methyltransferase) to CoM, forming the substrate for EC 2.8.4.1, coenzyme-B sulfoethylthiotransferase, the enzyme that catalyses the final step in methanogenesis.
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
a [methyl-Co(III) dimethylamine-specific corrinoid protein] + coenzyme M
methyl-CoM + a [Co(I) dimethylamine-specific corrinoid protein]
-
-
-
?
a [methyl-Co(III) methylamine-specific corrinoid protein] + coenzyme M
methyl-CoM + a [Co(I) methylamine-specific corrinoid protein]
a [methyl-Co(III) trimethylamine-specific corrinoid protein] + coenzyme M
methyl-CoM + a [Co(I) trimethylamine-specific corrinoid protein]
-
-
-
?
[methyl-Co(III) dimethylamine-specific corrinoid protein] + coenzyme M
methyl-CoM + [Co(I) dimethylamine-specific corrinoid protein]
isozyme MT2-A, not MT2-M
-
-
r
[methyl-Co(III) monomethylamine-specific corrinoid protein] + coenzyme M
methyl-CoM + [Co(I) monomethylamine-specific corrinoid protein]
isozyme MT2-A, not MT2-M
-
-
r
[methyl-Co(III) trimethylamine-specific corrinoid protein] + 3-mercaptopropionate
methyl-3-mercaptopropionate + [Co(I) trimethylamine-specific corrinoid protein]
3-mercaptopropionate is a coenzyme M analogue
-
-
?
[methyl-Co(III) trimethylamine-specific corrinoid protein] + coenzyme M
methyl-CoM + [Co(I) trimethylamine-specific corrinoid protein]
a [methyl-Co(III) dimethylamine-specific corrinoid protein] + coenzyme M
methyl-CoM + a [Co(I) dimethylamine-specific corrinoid protein]
-
-
-
-
?
a [methyl-Co(III) monomethylamine-specific corrinoid protein] + coenzyme M
methyl-CoM + a [Co(I) monomethylamine-specific corrinoid protein]
-
-
-
-
?
a [methyl-Co(III) trimethylamine-specific corrinoid protein] + coenzyme M
methyl-CoM + a [Co(I) trimethylamine-specific corrinoid protein]
-
-
-
-
?
[methyl-Co(III) trimethylamine-specific corrinoid protein] + coenzyme M
methyl-CoM + [Co(I) trimethylamine-specific corrinoid protein]
-
-
-
-
?
a [methyl-Co(III) methylamine-specific corrinoid protein] + coenzyme M
methyl-CoM + a [Co(I) methylamine-specific corrinoid protein]
-
-
-
?
a [methyl-Co(III) methylamine-specific corrinoid protein] + coenzyme M
methyl-CoM + a [Co(I) methylamine-specific corrinoid protein]
binding analysis of CoM at the metal center of isozyme MT2-A, overview
-
-
?
a [methyl-Co(III) methylamine-specific corrinoid protein] + coenzyme M
methyl-CoM + a [Co(I) methylamine-specific corrinoid protein]
trimethylamine methyl transfer required, neither dimethylamine nor monomethylamine serve as substrate
-
-
?
[methyl-Co(III) trimethylamine-specific corrinoid protein] + coenzyme M
methyl-CoM + [Co(I) trimethylamine-specific corrinoid protein]
heterolytic cleavage of the methylcobamide carbon-cobalt bond with cob(I)alamin as the major product of the reaction
-
-
r
[methyl-Co(III) trimethylamine-specific corrinoid protein] + coenzyme M
methyl-CoM + [Co(I) trimethylamine-specific corrinoid protein]
isozymes MT2-A and MT2-M, heterolytic cleavage of the methylcobamide carbon-cobalt bond with cob(I)alamin as the major product of the reaction
-
-
r
additional information
?
-
corrinoid proteins mediating CoM methylation from dimethylamine or monomethylamine have a specific requirement for MT2-A, reconstitution of trimethylamine-dependent coenzyme M methylation, overview. Trimethylamine methyl transfer can interact with either isozyme of MT2 but has the greatest affinity for the A isozyme. The predominant isozyme of MT2 from in TMA-grown cells is the favored participant in the TMA:CoM methyl transfer reaction
-
-
?
additional information
?
-
-
corrinoid proteins mediating CoM methylation from dimethylamine or monomethylamine have a specific requirement for MT2-A, reconstitution of trimethylamine-dependent coenzyme M methylation, overview. Trimethylamine methyl transfer can interact with either isozyme of MT2 but has the greatest affinity for the A isozyme. The predominant isozyme of MT2 from in TMA-grown cells is the favored participant in the TMA:CoM methyl transfer reaction
-
-
?
additional information
?
-
methylamine-dependent methylation of CoM mediated by trimethyamine- or monomethylamine-specific methyltransferases derived from cells grown on trimethylamine. Methylation of CoM by trimethylamine and methylation by monomethylamine are mediated by separate enzyme systems with at least one different component
-
-
?
additional information
?
-
conversions of monomethylamine and dimethylamine to CH3-SCoM are dependent upon MT2-A, and are not supported by MT2-M, both isozymes catalyze S-methylation of 2-thioethanesulfonate, i.e. coenzyme M, and exhibit similar apparent Km values for coenzyme M, isozymes substrate specificities, overview
-
-
?
additional information
?
-
the enzyme exhibits MT2 activity, the MT2 activity is measured by following the coenzyme-M-dependent demethylation of methylcobalamin. Trimethylammonium:coenzyme M methyltransferase activity detected by coenzyme M methylation
-
-
?
additional information
?
-
-
the enzyme exhibits MT2 activity, the MT2 activity is measured by following the coenzyme-M-dependent demethylation of methylcobalamin
-
-
?
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
a [methyl-Co(III) dimethylamine-specific corrinoid protein] + coenzyme M
methyl-CoM + a [Co(I) dimethylamine-specific corrinoid protein]
-
-
-
?
a [methyl-Co(III) methylamine-specific corrinoid protein] + coenzyme M
methyl-CoM + a [Co(I) methylamine-specific corrinoid protein]
-
-
-
?
a [methyl-Co(III) trimethylamine-specific corrinoid protein] + coenzyme M
methyl-CoM + a [Co(I) trimethylamine-specific corrinoid protein]
-
-
-
?
[methyl-Co(III) trimethylamine-specific corrinoid protein] + coenzyme M
methyl-CoM + [Co(I) trimethylamine-specific corrinoid protein]
heterolytic cleavage of the methylcobamide carbon-cobalt bond with cob(I)alamin as the major product of the reaction
-
-
r
a [methyl-Co(III) dimethylamine-specific corrinoid protein] + coenzyme M
methyl-CoM + a [Co(I) dimethylamine-specific corrinoid protein]
-
-
-
-
?
a [methyl-Co(III) monomethylamine-specific corrinoid protein] + coenzyme M
methyl-CoM + a [Co(I) monomethylamine-specific corrinoid protein]
-
-
-
-
?
a [methyl-Co(III) trimethylamine-specific corrinoid protein] + coenzyme M
methyl-CoM + a [Co(I) trimethylamine-specific corrinoid protein]
-
-
-
-
?
additional information
?
-
corrinoid proteins mediating CoM methylation from dimethylamine or monomethylamine have a specific requirement for MT2-A, reconstitution of trimethylamine-dependent coenzyme M methylation, overview. Trimethylamine methyl transfer can interact with either isozyme of MT2 but has the greatest affinity for the A isozyme. The predominant isozyme of MT2 from in TMA-grown cells is the favored participant in the TMA:CoM methyl transfer reaction
-
-
?
additional information
?
-
-
corrinoid proteins mediating CoM methylation from dimethylamine or monomethylamine have a specific requirement for MT2-A, reconstitution of trimethylamine-dependent coenzyme M methylation, overview. Trimethylamine methyl transfer can interact with either isozyme of MT2 but has the greatest affinity for the A isozyme. The predominant isozyme of MT2 from in TMA-grown cells is the favored participant in the TMA:CoM methyl transfer reaction
-
-
?
additional information
?
-
methylamine-dependent methylation of CoM mediated by trimethyamine- or monomethylamine-specific methyltransferases derived from cells grown on trimethylamine. Methylation of CoM by trimethylamine and methylation by monomethylamine are mediated by separate enzyme systems with at least one different component
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
no enzyme-bound organic or inorganic cofactors
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Co2+
reconstitution of apo-enzyme with Co2+ yields an enzyme with 16fold higher specific activity, cysteine thiolate coordination in approximate tetrahedral geometry indicated by strong d-d transition absorbance centered at 622 nm, overview
Zn2+
Zn2+
both isozymes are zinc-containing metalloproteins, zinc involvement in catalysis of coenzyme M methylation
Zn2+
required for activity by both isozymes MT2-A and MT2-M, tightly bound by the enzyme, 0.63 mol of Zn/mol of MT2-A, can be substituted by Co2+, which results in 16fold higher activity. Zn2+-MT2-A reveals 2S + 2N/O coordination with evidence for involvement of histidine. Interaction with the substrate CoM (2-mercaptoethanesulfonic acid) results in replacement of the second N/O group with S, indicating direct coordination of the CoM thiolate. Additional formation of an additional metal-thiolate bond, overview. Model formation in which metalthiolate formation occurs separately from H+ release from the enzyme-substrate complex at pH 6.2-7.7
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
stimulation of the TMA:CoM methyl transfer reaction in cell extracts
-
additional information
-
stimulation of the TMA:CoM methyl transfer reaction in cell extracts
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000014
[methyl-Co(III) trimethylamine-specific corrinoid protein]
isozymes MT2-A and MT-2-M, pH 7.2, 23°C
-
additional information
additional information
steady-state kinetics
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.258
MMA:CoM methyl transfer from TMA-grown cells, pH and temperature not specified in the publication
0.452
TMA:CoM methyl transfer from TMA-grown cells, pH and temperature not specified in the publication
0.2
-
trimethylamine:coenzyme M methyltransferase activity, pH 7.0, 37°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
isozymes MT2-A and MT2-M encoded by genes cmtA and cmtM
UniProt
sample of microbial consortium involved in biogas production collected from the fermenter tank of an agricultural two-stage biogas plant anaerobic digester in Miedzyrzec Podlaski, Poland, gene mtbA
UniProt
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
additional information
numerous extracts of cells grown on methanol do not possess detectable levels of TMA:CoM methyl group transfer activity
additional information
-
cell extracts of strain NaT1 grown on trimethylamine rather than on tetramethylammonium are devoid of tetramethylammonium:coenzyme M methyltransferase activity
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
Methanosarcinales are mainly responsible for the utilization of methylamines. mtbA-Specific primers LMTBA/RMTBA-detected sequences from analyzed samples mostly belong to the Methanosarcinales, with two dominating species: Methanosarcina barkeri and Methanomethylovorans hollandica
metabolism
malfunction
-
immunosorptive depletion of MT2 isozymes from cell-free extracts, extracts of methanol-grown cells depleted of MT2-M lose entirely the ability to carry out conversion of methanol to 2-(methylthio)ethanesulfonate, i.e. methyl-CoM. Methanol:CoM methyl transfer activity is completely restored by addition of purified MT2-M, but no activity is recovered by addition of MT2-A. In contrast, the activity of trimethylamine-grown cell extracts to convert monomethylamine and dimethylamine to methyl-CoM is lost almost entirely by immunosorptive removal of MT2-A. Addition of purified MT2-A but not MT2-M, to the MT2-A-depleted extract fully reconstitutes methyl-CoM formation from both mono- and dimethylamine
metabolism
-
MT2-A plays a specific role in metabolism of methylated amine substrates, whereas, MT2-M functions in methane formation from trimethylamine and methanol, while neither of the two MT2 isozymes is involved in methane formation from acetate
additional information
metabolism
isozyme MT2-A functions in methanogenesis from monomethylamine
metabolism
the enzyme is involved in the conversion of methylated amines into methyl-CoM, part of the superpathway of methanogenesis, overview
additional information
the enzyme shows an active site geometry in which coenzyme M is bound both by S-coordination to zinc, and electrostatic interaction of the sulfonate with a cationic group on the enzyme
additional information
-
cell extracts of strain NaT1 catalyze the formation of methyl-coenzyme M from coenzyme M and tetramethylammonium, EC 2.1.1.253, or trimethylamine, EC 2.1.1.250, but not from coenzyme M and dimethylamine, EC 2.1.1.249, monomethylamine, EC 2.1.1.248, or methanol, EC 2.1.1.246
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
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
x * 36000-37000, recombinant isozymes MT2-A and MT2-M, SDS-PAGE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native enzyme by two different steps of anion exchange chromatography, gel filtration, and another step of anion exchange chromatography, co-purification with the 26-kDa the trimethylamine-specific corrinoid protein
recombinant His6-tagged isozyme MT2-A from Escherichia coli strain M15 by anion exchange and hydrophobic interaction chromatography, and ultrafiltration to approximately 98% purity
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene mtbA, DNA and amino acid sequence determination and analysis, development and optimization of specific detection primers, phylogenetic analysis and tree
gene mtbA, isozyme MT2-A, DNA and amino acid sequence determination and analysis, expression as His6-tagged enzyme in Escherichia coli strain M15
genes cmtA and cmtM, DNA and amino acid sequence determination and analysis, expression of the isozymes in Escherichia coli
gene mtbA, DNA and amino acid sequence determination and analysis, gene mtbA is monocislronically transcribed
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Asakawa, S.; Sauer, K.; Liesack, W.; Thauer, R.
Tetramethylammonium:coenzyme M methyltransferase system from Methanococcoides sp.
Arch. Microbiol.
170
220-226
1998
Methanosarcina barkeri, Methanosarcina barkeri NaT1
Gencic, S.; LeClerc, G.; Gorlatova, N.; Peariso, K.; Penner-Hahn, J.; Grahame, D.
Zinc-thiolate intermediate in catalysis of methyl group transfer in Methanosarcina barkeri
Biochemistry
40
13068-13078
2001
Methanosarcina barkeri (O30640)
Harms, U.; Thauer, R.
Methylcobalamin:coenzyme M methyltransferase isoenzymes MtaA and MtbA from Methanosarcina barkeri: Cloning, sequencing and differential transcription of the encoding genes, and functional overexpression of the mtaA gene in Escherichia coli
Eur. J. Biochem.
235
653-659
1996
Methanosarcina barkeri, Methanosarcina barkeri DSM 804
Burke, S.; Krzycki, J.
Involvement of the A isozyme of methyltransferase II and the 29-kilodalton corrinoid protein in methanogenesis from monomethylamine
J. Bacteriol.
177
4410-4416
1995
Methanosarcina barkeri (O30640), Methanosarcina barkeri MS / DSM 800 (O30640)
Ferguson Jr., D.; Krzycki, J.
Reconstitution of trimethylamine-dependent coenzyme M methylation with the trimethylamine corrinoid protein and the isozymes of methyltransferase II from Methanosarcina barkeri
J. Bacteriol.
179
846-852
1997
Methanosarcina barkeri (O30640), Methanosarcina barkeri
LeClerc, G.M.; Grahame, D.A.
Methylcobamide:coenzyme M methyltransferase isozymes from Methanosarcina barkeri. Physicochemical characterization, cloning, sequence analysis, and heterologous gene expression
J. Biol. Chem.
271
18725-18731
1996
Methanosarcina barkeri (O30640)
Ferguson Jr., D.; Krzycki, J.; Grahame, D.
Specific roles of methylcobamide:coenzyme M methyltransferase isozymes in metabolism of methanol and methylamines in Methanosarcina barkeri
J. Biol. Chem.
271
5189-5194
1996
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 (O30640), Methanosarcina barkeri
Dziewit, L.; Pyzik, A.; Romaniuk, K.; Sobczak, A.; Szczesny, P.; Lipinski, L.; Bartosik, D.; Drewniak, L.
Novel molecular markers for the detection of methanogens and phylogenetic analyses of methanogenic communities
Front. Microbiol.
6
694
2015
Methanomethylovorans hollandica, Methanosarcina barkeri (O30640)
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