Information on EC 2.1.1.253 - [methyl-Co(III) tetramethylammonium-specific corrinoid protein]:coenzyme M methyltransferase

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The expected taxonomic range for this enzyme is: Methanosarcina barkeri

EC NUMBER
COMMENTARY hide
2.1.1.253
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RECOMMENDED NAME
GeneOntology No.
[methyl-Co(III) tetramethylammonium-specific corrinoid protein]:coenzyme M methyltransferase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
a [methyl-Co(III) tetramethylammonium-specific corrinoid protein] + coenzyme M = methyl-CoM + a [Co(I) tetramethylammonium-specific corrinoid protein]
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
methanogenesis from tetramethylammonium
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SYSTEMATIC NAME
IUBMB Comments
methylated tetramethylammonium-specific corrinoid protein:coenzyme M methyltransferase
The enzyme, which is involved in methanogenesis from tetramethylammonium, catalyses the transfer of a methyl group from a corrinoid protein (see EC 2.1.1.252, tetramethylammonium---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.
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
gene mtqA
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Manually annotated by BRENDA team
gene mtqA
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ATP
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dependent on
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Ti(III) citrate
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dependent on
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40000
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x * 40000, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
native enzyme by ultracentrifugation, a first step of anion exchange chromatography, hydroxyapatite chromatography, a second step of anion exchange chromatography, adsorption and again a third step of anion exchange chromatography
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