Information on EC 2.1.1.251 - methylated-thiol-coenzyme M methyltransferase

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The expected taxonomic range for this enzyme is: Methanosarcina barkeri

EC NUMBER
COMMENTARY hide
2.1.1.251
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RECOMMENDED NAME
GeneOntology No.
methylated-thiol-coenzyme M methyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
a [methyl-Co(III) methylated-thiol-specific corrinoid protein] + coenzyme M = methyl-CoM + a [Co(I) methylated-thiol-specific corrinoid protein]
show the reaction diagram
methanethiol + a [Co(I) methylated--thiol-specific corrinoid protein] = a [methyl-Co(III) methylated-thiol-specific corrinoid protein] + hydrogen sulfide
show the reaction diagram
1a
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methanethiol + a [Co(I) methylated-thiol-specific corrinoid protein] = a [methyl-Co(III) methylated-thiol-specific corrinoid protein] + hydrogen sulfide
show the reaction diagram
methanethiol + coenzyme M = methyl-CoM + hydrogen sulfide
show the reaction diagram
overall reaction
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
methanogenesis from dimethylsulfide
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methanogenesis from methanethiol
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methanogenesis from methylthiopropanoate
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NIL
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Sulfur metabolism
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SYSTEMATIC NAME
IUBMB Comments
methylated-thiol:coenzyme M methyltransferase
The enzyme, which is involved in methanogenesis from methylated thiols, such as methane thiol, dimethyl sulfide, and 3-S-methylmercaptopropionate, catalyses two successive steps - the transfer of a methyl group from the substrate to the cobalt cofactor of a methylated-thiol-specific corrinoid protein (MtsB), and the subsequent transfer of the methyl group from the corrinoid protein to coenzyme M. With most other methanogenesis substrates this process is carried out by two different enzymes (for example, EC 2.1.1.90, methanol---corrinoid protein Co-methyltransferase, and EC 2.1.1.246, methylated methanol-specific corrinoid protein:coenzyme M methyltransferase). The cobalt is oxidized during methylation from the Co(I) state to the Co(III) state, and is reduced back to the Co(I) form during demethylation.
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
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
the sequence of MtsA is homologous to the A and M isozymes of methylcobamide:coenzyme M methyltransferases (methyltransferase II), indicating that the alpha polypeptide is a member of the methyltransferase II family of coenzyme M methylases
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
3-methylmercapto-1-propanol + coenzyme M
methyl-CoM + 3-mercapto-1-propanol
show the reaction diagram
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-
?
a [methyl-Co(III) methylated-thiol-specific corrinoid protein] + coenzyme M
methyl-CoM + a [Co(I) methylated-thiol-specific corrinoid protein]
show the reaction diagram
dimethylsulfide + coenzyme M
methyl-CoM + methanethiol
show the reaction diagram
methanethiol + a [Co(I) methylated-thiol-specific corrinoid protein]
a [methyl-Co(III) methylated-thiol-specific corrinoid protein] + hydrogen sulfide
show the reaction diagram
methanethiol + coenzyme M
methyl-CoM + hydrogen sulfide
show the reaction diagram
methylmercaptopropionate + coenzyme M
methyl-CoM + mercaptopropionate
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) methylated-thiol-specific corrinoid protein] + coenzyme M
methyl-CoM + a [Co(I) methylated-thiol-specific corrinoid protein]
show the reaction diagram
Q48924
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-
-
?
dimethylsulfide + coenzyme M
methyl-CoM + methanethiol
show the reaction diagram
methanethiol + a [Co(I) methylated-thiol-specific corrinoid protein]
a [methyl-Co(III) methylated-thiol-specific corrinoid protein] + hydrogen sulfide
show the reaction diagram
Q48924
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-
-
?
methanethiol + coenzyme M
methyl-CoM + hydrogen sulfide
show the reaction diagram
methylmercaptopropionate + coenzyme M
methyl-CoM + mercaptopropionate
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
corrinoid
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the enzyme obligately requires the bound methylated corrinoid cofactor for activity. Corrinoid-dependent methyltransferases cycle between methylated corrinoid in the Co(III) redox state and the highly nucleophilic, reducing, and oxygen-sensitive Co(I) state. In the Co(II) form, these methyltransferase is inactive
additional information
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no corrinoid cofactor bound to the enzyme
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co3+
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the enzyme obligately requires the bound methylated corrinoid cofactor for activity. Corrinoid-dependent methyltransferases cycle between methylated corrinoid in the Co(III) redox state and the highly nucleophilic, reducing, and oxygen-sensitive Co(I) state. In the Co(II) form, these methyltransferase is inactive
Cobalt
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the enzyme obligately requires the bound methylated corrinoid cofactor for activity. Corrinoid-dependent methyltransferases cycle between methylated corrinoid in the Co(III) redox state and the highly nucleophilic, reducing, and oxygen-sensitive Co(I) state. In the Co(II) form, these methyltransferase is inactive
Zn2+
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one zinc atom per polypeptide
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Dimethylsulfide
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inhibits methylcobalamin:coenzyme methyl transfer by MtsA. Inhibition by dimethylsulfide is mixed with respect to methylcobalamin, but competitive with coenzyme M
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Ti(III) citrate
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not essential activation
additional information
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5.5
a [Co(I) methylated-thiol-specific corrinoid protein]
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recombinant enzyme, pH 7.0, 37°C
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10.8
coenzyme M
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recombinant enzyme, pH 7.0, 37°C
33
Dimethylsulfide
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recombinant enzyme, pH 7.0, 37°C
10
methylmercaptopropionate
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pH 7.0, 37°C
additional information
additional information
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kinetic analysis, overview
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.078
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purified recombinant enzyme, substrate is dimethylsulfide, pH 7.0, 37°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
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Cob(I)alamin methylation assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
41000
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2 * 41000, recombinant enzyme, SDS-PAGE
77000
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recombinant enzyme, gel filtration
480000
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
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2 * 41000, recombinant enzyme, SDS-PAGE
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant MtsA solubilized from inclusion bodies after expression in Escherichia coli strain BL21(DE3)
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene mtsA, DNA and amino acid sequence determination and analysis, expression in Escherichia coli strain DH5alpha. The gene encoding the alpha subunit of the CoM methylase, mtsA, is 5' to the gene encoding the beta subunit, mtsB, regulated cotranscription of mtsA and mtsB
gene mtsA, functional expression in Escherichia coli strain BL21(DE3)pLysS, MtsA is expressed largely in an insoluble form
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Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme from inclusion bodies harvested from cells solubilized using 6 M guanidine hydrochloride, 50 mM DTT, and 20 mM 2-mercaptoethanol. The solubilized protein is diluted 60fold with protein refolding at room temperature for 24 h in refolding buffer consisting of 500 mM Tris, pH 8.0, 1 M KCl, 10 mM DTT, 10 mM 2-mercaptoethanol, and 100 mM ZnCl2. Refolding buffers containing 500 mM guanidine hydrochloride, 33 mM CHAPS, 0.5% Triton X-100, 5 mM SDS, or 20% glycerol do not produce active methyltransferase, nor do refolding at 4°C in the optimal refolding buffer
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