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

for references in articles please use BRENDA:EC2.1.1.253
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The expected taxonomic range for this enzyme is: Methanosarcina barkeri

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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 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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CAS REGISTRY NUMBER
COMMENTARY hide
53414-88-3
methylcobalamin-coenzyme M methyltransferase, EC 2.1.1.246 to EC 2.1.1.253
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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
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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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
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Ti(III) citrate
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dependent on
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40000
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x * 40000, SDS-PAGE
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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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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LINKS TO OTHER DATABASES (specific for EC-Number 2.1.1.253)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
InterPro (database of protein families, domains and functional sites)