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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-
-
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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
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