Information on EC 1.8.1.B5 - protein-disulfide reductase (CoM-dependent)

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The expected taxonomic range for this enzyme is: Methanosarcina acetivorans

EC NUMBER
COMMENTARY hide
1.8.1.B5
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
protein-disulfide reductase (CoM-dependent)
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
protein-disulfide + reduced coenzyme M = protein-dithiol + oxidized coenzyme M
show the reaction diagram
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-
-
-
SYSTEMATIC NAME
IUBMB Comments
protein-dithiol:coenzyme M oxidoreductase
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
insulin disulfide + reduced coenzyme M
insulin dithiol + oxidized coenzyme M
show the reaction diagram
insulin disulfide + reduced glutathione
insulin dithiol + oxidized glutathione
show the reaction diagram
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
coenzyme M
coenzyme M-SH and glutathione bind to the active site
glutathione
coenzyme M-SH and glutathione bind to the active site
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Cd2+
a cadmium ion is found within the active site of each monomer, crystallization data
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.2
reduced coenzyme M
pH 6.8, temperature not specified in the publication
8.9
reduced glutathione
pH 6.8, temperature not specified in the publication
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
11500
1 * 11500, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
structure exhibits a classic thioredoxin-glutaredoxin fold comprising three alpha-helices surrounding four antiparallel beta-sheets. A pocket on the surface contains a CVWC motif, identifying the active site with architecture similar to glutaredoxins. Active site modeling of conezyme M shows the sulfate moiety hydrogen-bonded to the backbone amide and carbonyl oxygen of residue Phe 76