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Enzyme Nomenclature
Information on EC 1.8.1.B4 - [protein disulfide oxidoreductase]-disulfide oxidoreductase
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The expected taxonomic range for this enzyme is: Sulfolobus solfataricus
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EC NUMBER 
COMMENTARY 
1.8.1.B4
preliminary BRENDA-supplied EC number
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RECOMMENDED NAME
GeneOntology No.
[protein disulfide oxidoreductase]-disulfide oxidoreductase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
[protein disulfide oxidoreductase]-dithiol + NADP+ = [protein disulfide oxidoreductase]-disulfide + NADPH + H+
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-
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SYSTEMATIC NAME
IUBMB Comments
[protein disulfide oxidoreductase]:NADP+ oxidoreductase
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
[C173S/C178S mutant of protein-disulfide-oxidoreductase]-disulfide + NADPH + H+
[C173S/C178S mutant of protein-disulfide-oxidoreductase]-dithiol + NADP+
[C173S/C178S mutant of protein-disulfide-oxidoreductase]-disulfide + NADPH + H+
[C173S/C178S mutant ofprotein-disulfide-oxidoreductase]-dithiol + NADP+
[C41S/C44S mutant of protein-disulfide-oxidoreductase]-disulfide + NADPH + H+
[C41S/C44S mutant of protein disulfide oxidoreductase]-dithiol + NADP+
[C41S/C44S mutant of protein-disulfide-oxidoreductase]-disulfide + NADPH + H+
[C41S/C44S mutant ofprotein disulfide oxidoreductase]-dithiol + NADP+
[protein disulfide oxidoreductase]-disulfide + NADPH + H+
[protein disulfide oxidoreductase]-dithiol + NADP+
[C173S/C178S mutant of protein-disulfide-oxidoreductase]-disulfide + NADPH + H+
[C173S/C178S mutant of protein-disulfide-oxidoreductase]-dithiol + NADP+
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the enzyme is able to reduce mutant protein-disulfide-oxidoreductase C41S/C44S and mutant protein-disulfide-oxidoreductase C173S/C178S with an affinity comparable with the wild-type protein-disulfide-oxidoreductase
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-
?
[C173S/C178S mutant of protein-disulfide-oxidoreductase]-disulfide + NADPH + H+
[C173S/C178S mutant of protein-disulfide-oxidoreductase]-dithiol + NADP+
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the enzyme is able to reduce mutant protein-disulfide-oxidoreductase C41S/C44S and mutant protein-disulfide-oxidoreductase C173S/C178S with an affinity comparable with the wild-type protein-disulfide-oxidoreductase
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-
?
[C173S/C178S mutant of protein-disulfide-oxidoreductase]-disulfide + NADPH + H+
[C173S/C178S mutant ofprotein-disulfide-oxidoreductase]-dithiol + NADP+
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the enzyme is able to reduce mutant protein-disulfide-oxidoreductase C41S/C44S and mutant protein-disulfide-oxidoreductase C173S/C178S with an affinity comparable with the wild-type protein-disulfide-oxidoreductase
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-
?
[C173S/C178S mutant of protein-disulfide-oxidoreductase]-disulfide + NADPH + H+
[C173S/C178S mutant ofprotein-disulfide-oxidoreductase]-dithiol + NADP+
-
the enzyme is able to reduce mutant protein-disulfide-oxidoreductase C41S/C44S and mutant protein-disulfide-oxidoreductase C173S/C178S with an affinity comparable with the wild-type protein-disulfide-oxidoreductase
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-
?
[C41S/C44S mutant of protein-disulfide-oxidoreductase]-disulfide + NADPH + H+
[C41S/C44S mutant of protein disulfide oxidoreductase]-dithiol + NADP+
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the enzyme is able to reduce mutant protein-disulfide-oxidoreductase C41S/C44S and mutant protein-disulfide-oxidoreductase C173S/C178S with an affinity comparable with the wild-type protein-disulfide-oxidoreductase
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-
?
[C41S/C44S mutant of protein-disulfide-oxidoreductase]-disulfide + NADPH + H+
[C41S/C44S mutant of protein disulfide oxidoreductase]-dithiol + NADP+
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the enzyme is able to reduce mutant protein-disulfide-oxidoreductase C41S/C44S and mutant protein-disulfide-oxidoreductase C173S/C178S with an affinity comparable with the wild-type protein-disulfide-oxidoreductase
-
-
?
[C41S/C44S mutant of protein-disulfide-oxidoreductase]-disulfide + NADPH + H+
[C41S/C44S mutant ofprotein disulfide oxidoreductase]-dithiol + NADP+
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the enzyme is able to reduce mutant protein-disulfide-oxidoreductase C41S/C44S and mutant protein-disulfide-oxidoreductase C173S/C178S with an affinity comparable with the wild-type protein-disulfide-oxidoreductase
-
-
?
[C41S/C44S mutant of protein-disulfide-oxidoreductase]-disulfide + NADPH + H+
[C41S/C44S mutant ofprotein disulfide oxidoreductase]-dithiol + NADP+
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the enzyme is able to reduce mutant protein-disulfide-oxidoreductase C41S/C44S and mutant protein-disulfide-oxidoreductase C173S/C178S with an affinity comparable with the wild-type protein-disulfide-oxidoreductase
-
-
?
[protein disulfide oxidoreductase]-disulfide + NADPH + H+
[protein disulfide oxidoreductase]-dithiol + NADP+
the highest activity is observed with protein disulfide oxidoreductase (SsPDO) as a substrate. Protein disulfide oxidoreductase (SsPDO) and the enzyme SsTR constitute a thioredoxin-like system in Sulfolobus solfataricus
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-
?
[protein disulfide oxidoreductase]-disulfide + NADPH + H+
[protein disulfide oxidoreductase]-dithiol + NADP+
-
the enzyme is able to reduce mutant protein-disulfide-oxidoreductase C41S/C44S and mutant protein-disulfide-oxidoreductase C173S/C178S with an affinity comparable with the wild-type protein-disulfide-oxidoreductase
-
-
?
[protein disulfide oxidoreductase]-disulfide + NADPH + H+
[protein disulfide oxidoreductase]-dithiol + NADP+
the highest activity is observed with protein disulfide oxidoreductase (SsPDO) as a substrate in the presence of FAD and NADPH as cofactors. The enzyme is not active with the putative thioredoxins TRxA1 (SSO0368) and TRxA2 (SSO2232)
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-
?
[protein disulfide oxidoreductase]-disulfide + NADPH + H+
[protein disulfide oxidoreductase]-dithiol + NADP+
the highest activity is observed with protein disulfide oxidoreductase (SsPDO) as a substrate. Protein disulfide oxidoreductase (SsPDO) and the enzyme SsTR constitute a thioredoxin-like system in Sulfolobus solfataricus
-
-
?
[protein disulfide oxidoreductase]-disulfide + NADPH + H+
[protein disulfide oxidoreductase]-dithiol + NADP+
the highest activity is observed with protein disulfide oxidoreductase (SsPDO) as a substrate in the presence of FAD and NADPH as cofactors. The enzyme is not active with the putative thioredoxins TRxA1 (SSO0368) and TRxA2 (SSO2232)
-
-
?
[protein disulfide oxidoreductase]-disulfide + NADPH + H+
[protein disulfide oxidoreductase]-dithiol + NADP+
-
the enzyme is able to reduce mutant protein-disulfide-oxidoreductase C41S/C44S and mutant protein-disulfide-oxidoreductase C173S/C178S with an affinity comparable with the wild-type protein-disulfide-oxidoreductase
-
-
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
[protein disulfide oxidoreductase]-disulfide + NADPH + H+
[protein disulfide oxidoreductase]-dithiol + NADP+
[protein disulfide oxidoreductase]-disulfide + NADPH + H+
[protein disulfide oxidoreductase]-dithiol + NADP+
Q97W27
the highest activity is observed with protein disulfide oxidoreductase (SsPDO) as a substrate. Protein disulfide oxidoreductase (SsPDO) and the enzyme SsTR constitute a thioredoxin-like system in Sulfolobus solfataricus
-
-
?
[protein disulfide oxidoreductase]-disulfide + NADPH + H+
[protein disulfide oxidoreductase]-dithiol + NADP+
Q97W27
the highest activity is observed with protein disulfide oxidoreductase (SsPDO) as a substrate. Protein disulfide oxidoreductase (SsPDO) and the enzyme SsTR constitute a thioredoxin-like system in Sulfolobus solfataricus
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-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FAD
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the highest activity is observed with protein disulfide oxidoreductase (SsPDO) as a substrate in the presence of FAD and NADPH as cofactors
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00012
[C173S/C178S mutant of protein-disulfide-oxidoreductase]-disulfide
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pH 7.0, 60°C
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0.00017
[C41S/C44S mutant of protein-disulfide-oxidoreductase]-disulfide
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pH 7.0, 60°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
wild-type enzyme and mutant enzymes C155S/C158S, C41S/C44S and C173S/C178S are expressed in Escherichi coli
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LINKS TO OTHER DATABASES (specific for EC-Number 1.8.1.B4)
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