Information on EC 2.1.1.246 - [methyl-Co(III) methanol-specific corrinoid protein]:coenzyme M methyltransferase

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The expected taxonomic range for this enzyme is: Methanosarcina

EC NUMBER
COMMENTARY hide
2.1.1.246
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RECOMMENDED NAME
GeneOntology No.
[methyl-Co(III) methanol-specific corrinoid protein]:coenzyme M methyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
a [methyl-Co(III) methanol-specific corrinoid protein] + coenzyme M = methyl-CoM + a [Co(I) methanol-specific corrinoid protein]
show the reaction diagram
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
methanogenesis from methanol
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Methane metabolism
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Microbial metabolism in diverse environments
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SYSTEMATIC NAME
IUBMB Comments
methylated methanol-specific corrinoid protein:coenzyme M methyltransferase
The enzyme, which is involved in methanogenesis from methanol, catalyses the transfer of a methyl group from a corrinoid protein (see EC 2.1.1.90, methanol---corrinoid protein Co-methyltransferase), where it is bound to the cobalt cofactor, to coenzyme M, forming the substrate for EC 2.8.4.1, coenzyme-B sulfoethylthiotransferase, the enzyme that catalyses the final step in methanogenesis. Free methylcob(I)alamin can substitute for the corrinoid protein in vitro [5].
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 mtaA
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Manually annotated by BRENDA team
DSM 804, gene mtaA
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Manually annotated by BRENDA team
gene variant mtaA-1, no expression or a low level of expression of mtaA-2
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Manually annotated by BRENDA team
gene variant mtaA-1, no expression or a low level of expression of mtaA-2
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
metabolism
physiological function
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) methanol-specific corrinoid protein] + 3-mercaptopropanoic acid
methyl-3-mercaptopropanoic acid + a [Co(I) methanol-specific corrinoid protein]
show the reaction diagram
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r
a [methyl-Co(III) methanol-specific corrinoid protein] + coenzyme M
methyl-CoM + a [Co(I) methanol-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) methanol-specific corrinoid protein] + coenzyme M
methyl-CoM + a [Co(I) methanol-specific corrinoid protein]
show the reaction diagram
additional information
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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Zn21 or Co21 are required for MtaA activity, Zn2+ can be replaced by Co2+ but not by Mg2+, the kinetics of activation by Co2+ being similarily slow. About 1 mol of transition metal is bound per mol of protein. The role of the transition metal in MtaA is to lower the microscopic pKa of the thiol group of coenzyme M by coordination to the zinc, and thus to increase its nucleophilicity for methyl group attack, pKZn2+ of MtaA is over 15
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
EDTA
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75% inhibition at 1 mM, complete inhibition at 2 mM, reversible by Zn2+ addition, competitive versus Zn2+, kinetics, overview
imidazole
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the demethylation of cob(I)inamide reaction is inhibited by imidazole. Imidazole does not inhibit methyltransfer from methylcob(III)alamin to coenzyme M at 10 mM
additional information
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1 mm nitrilotriacetic acid has almost no effect on the MtaA activity
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
methanol
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MtaB plus methanol positively affect the catalytic efficiency of MtaA. activation of MtaA by MtaB is methanol-dependent. Methylation of cob(I)inamide with methanol is dependent on imidazole but not on the demethylation of methylcob(III)inamide with coenzyme M. The demethylation reaction is even inhibited by imidazole
MtaB
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MtaB plus methanol positively affect the catalytic efficiency of MtaA. activation of MtaA by MtaB is methanol-dependent. Methylation of cob(I)inamide with methanol is dependent on imidazole but not on the demethylation of methylcob(III)inamide with coenzyme M. The demethylation reaction is even inhibited by imidazole
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Ti(III) citrate
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.01
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purified recombinant mutant C239A MtaA, pH 7.0, 37C
0.02
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purified recombinant mutant H237A MtaA, pH 7.0, 37C
0.154
MT2 activity in recombinant Escherichia coli cells transfected with gene cmtM, pH 7.2, 37C
0.2
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MtaA with substrate methylcob(III)-alamin, pH 7.0, 37C
0.3
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purified recombinant wild-type MtaA, pH 7.0, 37C
0.5377
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mtaC3B3A1 strain, cells grown on trimethylamine with tetracycline, pH 7.0, 37C
0.5657
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mtaC3B3A1 strain, cells grown on methanol with tetracycline, pH 7.0, 37C
1.21
MT2 activity in recombinant Escherichia coli cells transfected with gene cmtA, pH 7.2, 37C
2
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purified Zn2+-containing holoenzyme, pH 7.0, 37C
2.2
MT2 activity in cells grown on trimethylamine, pH 7.2, 37C
5.5
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purified recombinant enzyme, pH 7.2, 37C
7.5
MT2 activity in cells grown on methanol, pH 7.2, 37C
8
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MtaA with substrate methylcob(III)inamide, 50 mM methylcob(III)inamide as substrate show an activity of 8 U/mg, approximately 40fold higher than with 50 mM methylcob(III)-alamin, pH 7.0, 37C
additional information
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specific activities of diverse mtaCBA transcripts from cells with different growth conditions, overview
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
the isozymes MT2-A and MT2-M differ in their overall charge
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged apo MtaA from Escherichia coli strain M15 by nickel affinity and anionexchange chromatography
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recombinant His-tagged MtaA from Escherichia coli strain M15 by nickel affinity and anion exchange chromatography to homogeneity
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recombinant His6-tagged MtaA from Escherichia coli strain M15 to homogeneity by nickel affinity and anion exchange chromatography
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recombinant N-terminally His-tagged isozymes MtaA and MtbA from Escherichia coli strain M15 by nickel affinity chromatography
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recombinant N-terminally His6-tagged mtaA1 in Escherichia coli strain BL21(DE3) by affinity chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene mtaA, DNA and amino acid sequence determination and analysis, gene mtaA is monocislronically transcribed, transcription of the gene is positively controlled by the growth substrate rnethanol, overexpression of the His6-tagged enzyme in Escherichia coli strain M15
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gene mtaA, expression of His-tagged MtaA in Escherichia coli strain M15
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gene mtaA, sequence comparison, expression of His-tagged MtaA in Escherichia coli strain M15
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genes cmtA and cmtM, DNA and amino acid sequence determination and analysis, expressionin Escherichia coli strain XL-1 Blue
genes mtaA and mtaB, expression of N-terminally His-tagged isozymes MtaA and MtbA in Escherichia coli strain M15
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genes mtaA1 and mtaA2, overexpression of N-terminally His6-tagged mtaA1 in Escherichia coli strain BL21(DE3), strains carrying various combinations of mtaC, mtaB, and mtaA expressed from the strong, tetracycline-regulated PmcrB(tetO1) promoter exhibit similar growth characteristics on methanol, showing that all combinations of MtaC, MtaB, and MtaA can form functional MT1/MT2 complexes. Variations in activity correlate with differences in protein abundance, despite the fact that all the encoding genes are expressed from the same promoter, overview. The mtaCBA transcripts show different stabilities, which are strongly influenced by the growth substrate, quantitative expression and activity analysis, overview
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overexpression of His-tagged inactive MtaA apoprotein in Escherichia coli strain M15 grown in the presence of 2 mM EDTA
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
methanol induces the expression of mtaA-1
mtaA is induced by growth on methanol
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C239A
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site-directed mutagenesis, mutation of the residue involved in zinc coordination in MtaA results in reduced zinc content and reduced activity compared to the wild-type enzyme
H237A
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site-directed mutagenesis, mutation of the residue involved in zinc coordination in MtaA results in reduced zinc content and reduced activity compared to the wild-type enzyme
C239A
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site-directed mutagenesis, mutation of the residue involved in zinc coordination in MtaA results in reduced zinc content and reduced activity compared to the wild-type enzyme
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H237A
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site-directed mutagenesis, mutation of the residue involved in zinc coordination in MtaA results in reduced zinc content and reduced activity compared to the wild-type enzyme
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C239A
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site-directed mutagenesis, mutation of the residue involved in zinc coordination in MtaA results in reduced zinc content and reduced activity compared to the wild-type enzyme
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H237A
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site-directed mutagenesis, mutation of the residue involved in zinc coordination in MtaA results in reduced zinc content and reduced activity compared to the wild-type enzyme
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