Information on EC 2.1.1.247 - [methyl-Co(III) methylamine-specific corrinoid protein]:coenzyme M methyltransferase

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The expected taxonomic range for this enzyme is: Methanosarcina

EC NUMBER
COMMENTARY hide
2.1.1.247
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RECOMMENDED NAME
GeneOntology No.
[methyl-Co(III) methylamine-specific corrinoid protein]:coenzyme M methyltransferase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
a [methyl-Co(III) methylamine-specific corrinoid protein] + coenzyme M = methyl-CoM + a [Co(I) methylamine-specific corrinoid protein]
show the reaction diagram
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Methane metabolism
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methanogenesis from dimethylamine
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methanogenesis from methylamine
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methanogenesis from trimethylamine
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Microbial metabolism in diverse environments
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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 coenzyme M, 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 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
Fusaro, gene mtbA
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Manually annotated by BRENDA team
isozyme MT2-A
UniProt
Manually annotated by BRENDA team
gene mtbA
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Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
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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
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
a [methyl-Co(III) dimethylamine-specific corrinoid protein] + coenzyme M
methyl-CoM + a [Co(I) dimethylamine-specific corrinoid protein]
show the reaction diagram
a [methyl-Co(III) methylamine-specific corrinoid protein] + coenzyme M
methyl-CoM + a [Co(I) methylamine-specific corrinoid protein]
show the reaction diagram
a [methyl-Co(III) monomethylamine-specific corrinoid protein] + coenzyme M
methyl-CoM + a [Co(I) monomethylamine-specific corrinoid protein]
show the reaction diagram
a [methyl-Co(III) trimethylamine-specific corrinoid protein] + coenzyme M
methyl-CoM + a [Co(I) trimethylamine-specific corrinoid protein]
show the reaction diagram
HSCoM + methylcobalamin
CH3-SCoM + cob(I)alamin + H+
show the reaction diagram
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r
[methyl-Co(III) dimethylamine-specific corrinoid protein] + coenzyme M
methyl-CoM + [Co(I) dimethylamine-specific corrinoid protein]
show the reaction diagram
isozyme MT2-A, not MT2-M
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r
[methyl-Co(III) monomethylamine-specific corrinoid protein] + coenzyme M
methyl-CoM + [Co(I) monomethylamine-specific corrinoid protein]
show the reaction diagram
isozyme MT2-A, not MT2-M
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r
[methyl-Co(III) trimethylamine-specific corrinoid protein] + 3-mercaptopropionate
methyl-3-mercaptopropionate + [Co(I) trimethylamine-specific corrinoid protein]
show the reaction diagram
3-mercaptopropionate is a coenzyme M analogue
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-
?
[methyl-Co(III) trimethylamine-specific corrinoid protein] + coenzyme M
methyl-CoM + [Co(I) trimethylamine-specific corrinoid protein]
show the reaction diagram
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
a [methyl-Co(III) dimethylamine-specific corrinoid protein] + coenzyme M
methyl-CoM + a [Co(I) dimethylamine-specific corrinoid protein]
show the reaction diagram
a [methyl-Co(III) monomethylamine-specific corrinoid protein] + coenzyme M
methyl-CoM + a [Co(I) monomethylamine-specific corrinoid protein]
show the reaction diagram
a [methyl-Co(III) trimethylamine-specific corrinoid protein] + coenzyme M
methyl-CoM + a [Co(I) trimethylamine-specific corrinoid protein]
show the reaction diagram
HSCoM + methylcobalamin
CH3-SCoM + cob(I)alamin + H+
show the reaction diagram
O30640
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r
[methyl-Co(III) trimethylamine-specific corrinoid protein] + coenzyme M
methyl-CoM + [Co(I) trimethylamine-specific corrinoid protein]
show the reaction diagram
O30640
heterolytic cleavage of the methylcobamide carbon-cobalt bond with cob(I)alamin as the major product of the reaction
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r
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
no enzyme-bound organic or inorganic cofactors
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
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
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
methyl viologen
strictly dependent on
Ti(III) citrate
strictly dependent on
additional information
stimulation of the TMA:CoM methyl transfer reaction in cell extracts
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
9 - 10
3-Mercaptopropionate
0.02 - 0.035
coenzyme M
0.000014
[methyl-Co(III) trimethylamine-specific corrinoid protein]
isozymes MT2-A and MT-2-M, pH 7.2, 23C
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additional information
additional information
steady-state kinetics
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.07
1,10-phenanthroline
Methanosarcina barkeri
O30640
pH 7.2, 23C
0.005
EDTA
Methanosarcina barkeri
O30640
pH 7.2, 23C
0.05
EGTA
Methanosarcina barkeri
O30640
pH 7.2, 23C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.2
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trimethylamine:coenzyme M methyltransferase activity, pH 7.0, 37C
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
1.7
isozyme MT2-A, pH 7.0, 37C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 8
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assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
PDB
SCOP
CATH
ORGANISM
UNIPROT
Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88)
Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
52900
gel filtration and native PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 36000-37000, recombinant isozymes MT2-A and MT2-M, SDS-PAGE
monomer
1 * 52000, SDS-PAGE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystals of His6-tagged MtaA are obtained at room temperature by the hanging-drop vapour-diffusion method. Hexagonal-shaped crystals of the selenomethionine derivative are obtained by the sitting-drop vapour-diffusion method. The crystal structures of MtaA in a substrate-free but Zn2+-bound state and in complex with Zn2+ and coenzyme M (HS-CoM) are reported at resolutions of 1.8 and 2.1 A
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, gene mtbA is monocislronically transcribed
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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
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
mtbA is induced by growth on trimethylamine