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Enzyme Nomenclature
Information on EC 1.8.4.2 - protein-disulfide reductase (glutathione)
for references in articles please use BRENDA:EC1.8.4.2
Word Map on EC 1.8.4.2
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The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
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EC NUMBER 
COMMENTARY 
1.8.4.2
-
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RECOMMENDED NAME
GeneOntology No.
protein-disulfide reductase (glutathione)
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2 glutathione + protein-disulfide = glutathione-disulfide + protein-dithiol
random and allosteric mechanism via multiple distinct reaction sites
-
2 glutathione + protein-disulfide = glutathione-disulfide + protein-dithiol
random and allosteric mechanism via multiple distinct reaction sites
-
2 glutathione + protein-disulfide = glutathione-disulfide + protein-dithiol
random and allosteric mechanism via multiple distinct reaction sites
-
2 glutathione + protein-disulfide = glutathione-disulfide + protein-dithiol
high similarity between enzymes of different species and sources, respectively
-
2 glutathione + protein-disulfide = glutathione-disulfide + protein-dithiol
insulin inducible
-
2 glutathione + protein-disulfide = glutathione-disulfide + protein-dithiol
random mechanism
-
2 glutathione + protein-disulfide = glutathione-disulfide + protein-dithiol
mechanism
-
2 glutathione + protein-disulfide = glutathione-disulfide + protein-dithiol
C-X-X-C motif in active site for disulfide bonding, either oxidizing, reducing and isomerising activity
-
2 glutathione + protein-disulfide = glutathione-disulfide + protein-dithiol
C-X-X-C motif in active site for disulfide bonding, either oxidizing, reducing and isomerising activity; zinc finger protein with several CXXC motifs
-
2 glutathione + protein-disulfide = glutathione-disulfide + protein-dithiol
C-X-X-C motif in active site for disulfide bonding, either oxidizing, reducing and isomerising activity
-
2 glutathione + protein-disulfide = glutathione-disulfide + protein-dithiol
C-X-X-C motif in active site for disulfide bonding, either oxidizing, reducing and isomerising activity
-
2 glutathione + protein-disulfide = glutathione-disulfide + protein-dithiol
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
glutathione:protein-disulfide oxidoreductase
Reduces insulin and some other proteins.
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CAS REGISTRY NUMBER
COMMENTARY
9082-53-5
-
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
3051, 394810, 394811, 394817, 394819, 394825, 394826, 394827, 394828, 394829, 394831, 394833, 394834, 394835, 394836, 394837, 394838, 394839, 394845, 394847, 394848, 394849, 394851
-
-
different forms of protein thiol:disulfide oxidoreductases with either oxidizing, gene DsbA, reducing, gene DsbB, or isomerising, gene DsbC and DsbD, activity exist in Escherichia coli; in periplasm: DsbA and DsbB enzymes
-
-
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
-
the enzyme affects multiple phenotypes in Streptococcus gordonii and is required for production of disulfide-bonded proteins like Anti-CR1 scFv
physiological function
physiological function
a significant portion of protein HP_0377 is present in the oxidized form in an HP_0231 mutant
physiological function
-
inactivation of SdbA results in enhanced biofilm formation. Biofilm formation is mediated by the interaction between the CiaRH and ComDE two-component signalling systems. CiaRH is upregulated in the SdbA mutant and is essential for the enhanced biofilm phenotype. The enhanced biofilm phenotype also corresponds to increased oral colonization in mice; SdbA mutants lack bacteriocin activity due to strong repression of bacteriocin gene. The Com pathway is functional but not activated in the SdbA mutant. Repression of bacteriocin production is mediated by the CiaRH two-component system, which is strongly upregulated in the sdbA mutant. The CiaRH-induced protease DegP is also upregulated in the SdbA mutant
physiological function
reoxidation of MdbA involves bacterial vitamin K epoxide reductase-like protein that contains four cysteine residues, C93/C101 and C175/C178. Mutation C101A in this protein results in a high molecular weight complex of MdbA and bacterial vitamin K epoxide reductase-like protein
physiological function
gene deletion results in a severe growth defect at 37°C. By electron microscopy, the MdbA mutant is indistinguishable from wild-type at 30°C. At 37°C, the mutant becomes chained, clumped and coccoid in appearance. The mutant also fails to assemble pilus structures and is greatly defective in toxin production
physiological function
isoform DsbA1 is essential for the motility and autoagglutination phenotypes, and plays a critical role in the oxidative folding of alkaline phosphatase PhoX; loss of isoform DsbA2 has no impact on motility and autoagglutination phenotypes. DsbA2 is crucial for the activity of arylsulfotransferase AstA
physiological function
-
gene deletion results in a severe growth defect at 37°C. By electron microscopy, the MdbA mutant is indistinguishable from wild-type at 30°C. At 37°C, the mutant becomes chained, clumped and coccoid in appearance. The mutant also fails to assemble pilus structures and is greatly defective in toxin production
-
physiological function
-
a significant portion of protein HP_0377 is present in the oxidized form in an HP_0231 mutant
-
physiological function
-
inactivation of SdbA results in enhanced biofilm formation. Biofilm formation is mediated by the interaction between the CiaRH and ComDE two-component signalling systems. CiaRH is upregulated in the SdbA mutant and is essential for the enhanced biofilm phenotype. The enhanced biofilm phenotype also corresponds to increased oral colonization in mice; SdbA mutants lack bacteriocin activity due to strong repression of bacteriocin gene. The Com pathway is functional but not activated in the SdbA mutant. Repression of bacteriocin production is mediated by the CiaRH two-component system, which is strongly upregulated in the sdbA mutant. The CiaRH-induced protease DegP is also upregulated in the SdbA mutant
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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
2,3-dimercaptopropanol + protein disulfide
2,3-dimercaptopropanol disulfide + protein-dithiol
2,3-dimercaptopropanol + protein disulfide
2,3-dimercaptopropanol disulfide + protein-dithiol
-
-
-
-
?
2,3-dimercaptopropanol + protein disulfide
2,3-dimercaptopropanol disulfide + protein-dithiol
-
-
-
-
?
2,3-dimercaptopropanol + protein disulfide
2,3-dimercaptopropanol disulfide + protein-dithiol
-
-
-
-
?
2,3-dimercaptopropanol + protein disulfide
2,3-dimercaptopropanol disulfide + protein-dithiol
-
-
-
-
?
2-mercaptoethanol + protein disulfide
2-mercaptoethanol disulfide + protein-dithiol
-
-
-
-
?
2-mercaptoethanol + protein disulfide
2-mercaptoethanol disulfide + protein-dithiol
-
-
-
-
?
apocytochrome c + glutathione disulfide
apocytochrome c disulfide + 2 glutathione
-
-
-
?
apocytochrome c + glutathione disulfide
apocytochrome c disulfide + 2 glutathione
-
-
-
?
dithiothreitol + protein disulfide
?
-
protein disulfide: insulin or thioredoxin
-
-
r
GSH + insulin
GSSG + reduced insulin chain A and B
-
-
3052, 394817, 394819, 394825, 394826, 394827, 394828, 394829, 394831, 394832, 394833, 394834, 394835, 394836, 394837, 394838, 394839, 394840, 394845, 394847, 394849, 394851
-
-
-
GSH + insulin
GSSG + reduced insulin chain A and B
-
proinsulin
-
-
-
GSH + protein disulfide
GSSG + protein-dithiol
-
protein disulfide: e.g. of alcohol dehydrogenase, hexokinase, fructose-1,6-diphosphatase, malate dehydrogenase, glyceraldehyde phosphate dehydrogenase, glycerol phosphate dehydrogenase
-
?
GSH + protein disulfide
GSSG + protein-dithiol
-
prolactin is a poor substrate
-
?
GSH + protein disulfide
GSSG + protein-dithiol
-
reductive degradation and assembly of proteins
-
-
?
GSH + protein disulfide
GSSG + protein-dithiol
-
modulation of enzymatic activity from latent to active form and vice versa
-
-
?
GSH + protein disulfide
GSSG + protein-dithiol
-
feedback control via insulin in the liver
-
-
?
GSH + protein disulfide
GSSG + protein-dithiol
-
protein disulfide: thioredoxin
-
-
r
GSH + protein disulfide
GSSG + protein-dithiol
-
very rapid disulfide interchange reaction
-
-
r
GSH + protein disulfide
GSSG + protein-dithiol
-
protein disulfide: enzyme itself
-
r
GSH + protein disulfide
GSSG + protein-dithiol
-
disulfide bonding step in folding pathway of many periplasmic and outer membrane proteins with structural disulfide bonds
-
-
r
GSH + protein disulfide
GSSG + protein-dithiol
-
reductive degradation and assembly of proteins
-
-
?
GSH + protein disulfide
GSSG + protein-dithiol
-
modulation of enzymatic activity from latent to active form and vice versa
-
-
?
GSH + protein disulfide
GSSG + protein-dithiol
-
feedback control via insulin in the liver
-
-
?
GSH + protein disulfide
GSSG + protein-dithiol
-
reductive degradation and assembly of proteins
-
-
?
GSH + protein disulfide
GSSG + protein-dithiol
-
modulation of enzymatic activity from latent to active form and vice versa
-
-
?
GSH + protein disulfide
GSSG + protein-dithiol
-
major contributor to the inactivation of oxytoxin by lactating mammary gland
-
-
?
GSH + protein disulfide
GSSG + protein-dithiol
-
feedback control via insulin in the liver
-
-
?
GSH + protein disulfide
GSSG + protein-dithiol
-
synthesis of protein disulfide bond
-
-
?
GSH + protein disulfide
GSSG + protein-dithiol
-
enzyme plays a role in formation of intramonomer bonds common to all immunoglobulin molecules
-
-
?
GSH + protein disulfide
GSSG + protein-dithiol
-
physiological function
-
-
?
GSH + protein disulfide
GSSG + protein-dithiol
-
reductive degradation and assembly of proteins
-
-
?
GSH + protein disulfide
GSSG + protein-dithiol
-
modulation of enzymatic activity from latent to active form and vice versa
-
-
?
GSH + protein disulfide
GSSG + protein-dithiol
-
enzyme not directly involved in the subcellular processing of receptor-bound internalized insulin
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-
?
GSH + protein disulfide
GSSG + protein-dithiol
-
feedback control via insulin in the liver
-
-
?
GSH + protein disulfide
GSSG + protein-dithiol
-
initial step in sequential insulin degradation
-
-
?
insulin disulfide + dithiothreitol
insulin + dithiothreitol disulfide
-
-
-
?
insulin disulfide + dithiothreitol
insulin + dithiothreitol disulfide
-
-
-
?
additional information
?
-
-
bdbC and bdbD catalyze the formation of disulfide bonds that are essential for the DNA binding and uptake machinery
-
-
-
additional information
?
-
-
bdbC and bdbD catalyze the formation of disulfide bonds that are essential for the DNA binding and uptake machinery
-
-
-
additional information
?
-
-
ResA, probably together with another thiol-disulfide oxidoreductase, CcdA, is required for the the reduction of the cysteinyls in the heme binding site of apocytochrome c
-
-
-
additional information
?
-
-
StoA is a thiol-disulfide oxidoreductase that is involved in breaking disulfide bonds in cortex components or in proteins important for cortex synthesis
-
-
-
additional information
?
-
-
the two activities, cleavage and formation of protein-disulfide bonds, present alternate activities of the same enzyme
-
-
-
additional information
?
-
-
the two activities, cleavage and formation of protein-disulfide bonds, present alternate activities of the same enzyme
-
-
-
additional information
?
-
-
the two activities, cleavage and formation of protein-disulfide bonds, present alternate activities of the same enzyme
-
-
-
additional information
?
-
-
the two activities, cleavage and formation of protein-disulfide bonds, present alternate activities of the same enzyme
-
-
-
additional information
?
-
-
glutathione-insulin transhydrogenase EC 1.8.4.2 and protein disulfide-isomerase EC 5.3.4.1 activities are not both catalyzed by a single enzyme species
-
-
-
additional information
?
-
-
glutathione-insulin transhydrogenase EC 1.8.4.2 and protein disulfide-isomerase EC 5.3.4.1 activities are not both catalyzed by a single enzyme species
-
-
-
additional information
?
-
-
glutathione-insulin transhydrogenase EC 1.8.4.2 and protein disulfide-isomerase EC 5.3.4.1 activities are not both catalyzed by a single enzyme species
-
-
-
additional information
?
-
-
thiol:protein-disulfide oxidoreductase EC 1.8.4.2 and thiol:protein-disulfide isomerase EC 5.3.4.1 are immunological identical
-
-
-
additional information
?
-
-
thiol:protein-disulfide oxidoreductase EC 1.8.4.2 and thiol:protein-disulfide isomerase EC 5.3.4.1 are immunological identical
-
-
-
additional information
?
-
-
thiol:protein-disulfide oxidoreductase EC 1.8.4.2 and thiol:protein-disulfide isomerase EC 5.3.4.1 are immunological identical
-
-
-
additional information
?
-
-
enzyme also catalyzes reactivation and folding of protein containing incorrectly paired disulfide bond, e.g.: scrambled ribonuclease
-
-
-
additional information
?
-
-
enzyme also catalyzes reactivation and folding of protein containing incorrectly paired disulfide bond, e.g.: scrambled ribonuclease
-
-
-
additional information
?
-
-
enzyme also catalyzes reactivation and folding of protein containing incorrectly paired disulfide bond, e.g.: scrambled ribonuclease
-
-
-
additional information
?
-
-
the enzyme is unable to reduce insulin
-
-
-
additional information
?
-
-
redox reaction between different Dsn proteins
-
-
-
additional information
?
-
-
DsbB protein re-oxidizes the reduced DsbA protein
-
-
-
additional information
?
-
-
DsbB protein re-oxidizes the reduced DsbA protein
-
-
-
additional information
?
-
-
the enzyme is required for efficient disulfide bond formation in the periplasm
-
-
-
additional information
?
-
-
the two activities, cleavage and formation of protein-disulfide bonds, present alternate activities of the same enzyme
-
-
-
additional information
?
-
-
the two activities, cleavage and formation of protein-disulfide bonds, present alternate activities of the same enzyme
-
-
-
additional information
?
-
-
thiol:protein-disulfide oxidoreductase EC 1.8.4.2 and thiol:protein-disulfide isomerase EC 5.3.4.1 are immunological identical
-
-
-
additional information
?
-
-
thiol:protein-disulfide oxidoreductase EC 1.8.4.2 and thiol:protein-disulfide isomerase EC 5.3.4.1 are immunological identical
-
-
-
additional information
?
-
-
enzyme also catalyzes reactivation and folding of protein containing incorrectly paired disulfide bond, e.g.: scrambled ribonuclease
-
-
-
additional information
?
-
-
enzyme also catalyzes reactivation and folding of protein containing incorrectly paired disulfide bond, e.g.: scrambled ribonuclease
-
-
-
additional information
?
-
-
multifunctional enzyme that efficiently catalyzes disulfide reduction, disulfide isomerization, and dithiol oxidation
-
-
-
additional information
?
-
-
the two activities, cleavage and formation of protein-disulfide bonds, present alternate activities of the same enzyme
-
-
-
additional information
?
-
-
thiol:protein-disulfide oxidoreductase EC 1.8.4.2 and thiol:protein-disulfide isomerase EC 5.3.4.1 are immunological identical
-
-
-
additional information
?
-
-
enzyme also catalyzes reactivation and folding of protein containing incorrectly paired disulfide bond, e.g.: scrambled ribonuclease
-
-
-
additional information
?
-
-
the two activities, cleavage and formation of protein-disulfide bonds, present alternate activities of the same enzyme
-
-
-
additional information
?
-
-
the two activities, cleavage and formation of protein-disulfide bonds, present alternate activities of the same enzyme
-
-
-
additional information
?
-
-
glutathione-insulin transhydrogenase EC 1.8.4.2 and protein disulfide-isomerase EC 5.3.4.1 activities are not both catalyzed by a single enzyme species
-
-
-
additional information
?
-
-
scrambled trypsin inhibitor and proinsulin
-
-
-
additional information
?
-
-
thiol:protein-disulfide oxidoreductase EC 1.8.4.2 and thiol:protein-disulfide isomerase EC 5.3.4.1 are immunological identical
-
-
-
additional information
?
-
-
thiol:protein-disulfide oxidoreductase EC 1.8.4.2 and thiol:protein-disulfide isomerase EC 5.3.4.1 are immunological identical
-
-
-
additional information
?
-
-
enzyme also catalyzes reactivation and folding of protein containing incorrectly paired disulfide bond, e.g.: scrambled ribonuclease
-
-
-
additional information
?
-
-
enzyme also catalyzes reactivation and folding of protein containing incorrectly paired disulfide bond, e.g.: scrambled ribonuclease
-
-
-
additional information
?
-
-
reduction of ricin and other plant thiols
-
-
-
additional information
?
-
-
addition of GSH-dependent protein disulfide oxidoreductase to flour significantly increases dough extensibility (from 17 to 49% for cultivars with different quality), which implies the ability of the enzyme to disrupt disulfide bonds in high-molecular-weight gluten polymers
-
-
-
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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
GSH + protein disulfide
GSSG + protein-dithiol
-
reductive degradation and assembly of proteins
-
-
?
GSH + protein disulfide
GSSG + protein-dithiol
-
modulation of enzymatic activity from latent to active form and vice versa
-
-
?
GSH + protein disulfide
GSSG + protein-dithiol
-
feedback control via insulin in the liver
-
-
?
GSH + protein disulfide
GSSG + protein-dithiol
-
disulfide bonding step in folding pathway of many periplasmic and outer membrane proteins with structural disulfide bonds
-
-
r
GSH + protein disulfide
GSSG + protein-dithiol
-
reductive degradation and assembly of proteins
-
-
?
GSH + protein disulfide
GSSG + protein-dithiol
-
modulation of enzymatic activity from latent to active form and vice versa
-
-
?
GSH + protein disulfide
GSSG + protein-dithiol
-
feedback control via insulin in the liver
-
-
?
GSH + protein disulfide
GSSG + protein-dithiol
-
reductive degradation and assembly of proteins
-
-
?
GSH + protein disulfide
GSSG + protein-dithiol
-
modulation of enzymatic activity from latent to active form and vice versa
-
-
?
GSH + protein disulfide
GSSG + protein-dithiol
-
major contributor to the inactivation of oxytoxin by lactating mammary gland
-
-
?
GSH + protein disulfide
GSSG + protein-dithiol
-
feedback control via insulin in the liver
-
-
?
GSH + protein disulfide
GSSG + protein-dithiol
-
synthesis of protein disulfide bond
-
-
?
GSH + protein disulfide
GSSG + protein-dithiol
-
enzyme plays a role in formation of intramonomer bonds common to all immunoglobulin molecules
-
-
?
GSH + protein disulfide
GSSG + protein-dithiol
-
physiological function
-
-
?
GSH + protein disulfide
GSSG + protein-dithiol
-
reductive degradation and assembly of proteins
-
-
?
GSH + protein disulfide
GSSG + protein-dithiol
-
modulation of enzymatic activity from latent to active form and vice versa
-
-
?
GSH + protein disulfide
GSSG + protein-dithiol
-
enzyme not directly involved in the subcellular processing of receptor-bound internalized insulin
-
-
?
GSH + protein disulfide
GSSG + protein-dithiol
-
feedback control via insulin in the liver
-
-
?
GSH + protein disulfide
GSSG + protein-dithiol
-
initial step in sequential insulin degradation
-
-
?
additional information
?
-
-
bdbC and bdbD catalyze the formation of disulfide bonds that are essential for the DNA binding and uptake machinery
-
-
-
additional information
?
-
-
bdbC and bdbD catalyze the formation of disulfide bonds that are essential for the DNA binding and uptake machinery
-
-
-
additional information
?
-
-
ResA, probably together with another thiol-disulfide oxidoreductase, CcdA, is required for the the reduction of the cysteinyls in the heme binding site of apocytochrome c
-
-
-
additional information
?
-
-
StoA is a thiol-disulfide oxidoreductase that is involved in breaking disulfide bonds in cortex components or in proteins important for cortex synthesis
-
-
-
additional information
?
-
-
the enzyme is required for efficient disulfide bond formation in the periplasm
-
-
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
iodoacetamide
-
treatment with thiol prior to incubation with GSH and substrate: no inhibition, preincubation with GSH and thiol reagent: inhibition
N-ethylmaleimide
-
treatment with thiol prior to incubation with GSH and substrate: no inhibition, preincubation with GSH and thiol reagent: inhibition
Scrambled forms of ribonuclease and lysozyme
-
inhibition of insulin degradation
-
iodoacetate
-
treatment with thiol prior to incubation with GSH and substrate: no inhibition, preincubation with GSH and thiol reagent: inhibition
additional information
-
enzyme preincubated with toxins, e.g. ricin and Viscum album lectin, enhances their inhibitory effects against protein synthesis
-
additional information
-
carboxylation of thiol groups abolish reduction activity
-
additional information
-
enzyme preincubated with toxins, e.g. ricin and Viscum album lectin, enhances their inhibitory effects against protein synthesis
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
cysteine disulfide
-
cysteine residues in the redox active catalytic center are essential for conformation stability
deoxycholate
-
activating the enzyme membrane-bound in the microsomal fraction
Triton X-100
-
activating the enzyme membrane-bound in the microsomal fraction
Chelating agents
-
e.g. EDTA, EGTA, 8-hydroxyquinoline, 1,10-phenanthroline, activation
Chelating agents
-
e.g. EDTA, EGTA, 8-hydroxyquinoline, 1,10-phenanthroline, activation
Chelating agents
-
e.g. EDTA, EGTA, 8-hydroxyquinoline, 1,10-phenanthroline, activation
Chelating agents
-
e.g. EDTA, EGTA, 8-hydroxyquinoline, 1,10-phenanthroline, activation
Phospholipids
-
slight activation by all phospholipids tested except for phosphatidic acid and phosphatidylserine, highest activation by phosphatidylethanolamine
Phospholipids
-
slight activation by all phospholipids tested except for phosphatidic acid and phosphatidylserine, highest activation by phosphatidylethanolamine
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
Km in different tissues for GSH and insulin
-
additional information
additional information
-
comparison of Km values in different assay methods
-
additional information
additional information
-
Km values for insulin at various fixed thiol concentrations and for various thiol compounds at fixed insulin concentrations
-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
specific activities of different human carcinoma cell lines with different thiol and disulfide substrates
additional information
-
1.56 U/mg in the cell extract, 8.17 U/mg after Ni2+-NTA chromatography purification, one unit is defined as the amount of protein that produces an increase in 0.1 OD in 1 min at 650 nm
additional information
-
hepatic enzyme activity, active and latent, during growth phases and during liver regeneration
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.2 - 10.2
-
pH 6.2: about 10% of activity maximum, pH 10.2: about 20% of activity maximum
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
-
glutathione-insulin transhydrogenase is present in an inactive state as a divalent metal ion complex that can be activated by EDTA and/or GSH
-
-
3051, 3052, 394810, 394817, 394825, 394827, 394828, 394829, 394832, 394834, 394835, 394836, 394838, 394839, 394840, 394847
-
-
3067, 394810, 394812, 394813, 394814, 394815, 394816, 394817, 394818, 394820, 394821, 394823, 394830, 394832, 394847
-
-
additional information
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higher activity in mononuclear cells than in polymorphonuclear cells
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
membrane-associated with its thioredoxin-like domain on the outside of the cytoplasmic membrane
-
outer cytoplasmic membrane, protein termini localised in the periplasm
-
majority of the enzyme located at; weakly bound on cisternal surface of microsomes via phospholipids
-
-
weakly bound on cisternal surface of microsomes via phospholipids
-
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PDB
SCOP
CATH
ORGANISM
UNIPROT
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
14056
-
2 * 14056, unmodified recombinant WhiB1, MALDI-TOF mass spectrometry
14284
-
2 * 14284, reduced protein after alkylation corresponding to the theoretical mass of the recombinant protein with four iodoacetamide mediated modifications of cysteines, MALDI-TOF mass spectrometry
20000
60000
120000
additional information
-
3 molecular forms: MW 56000 is the major form, MW 51000 is active and only present in spleen, possibly a proteolytic product of 56000 MW protein, MW 67000 is possibly a precursor of 56000 MW protein
60000
-
1 * 60000, SDS-PAGE; 2 * 60000, SDS-PAGE, dimerization after prolonged storage at -20°C, freeze-thawing or heating at 60°C, monomers held together by an intermolecular disulfide bond
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homodimer
monomer
trimer
-
enzyme contains 3 amino-terminal residues, therefore might be composed of 3 polypeptide chains or subunits
dimer
-
2 * 60000, SDS-PAGE, dimerization after prolonged storage at -20°C, freeze-thawing or heating at 60°C, monomers held together by an intermolecular disulfide bond
homodimer
-
2 * 14000, SDS-PAGE; 2 * 14056, unmodified recombinant WhiB1, MALDI-TOF mass spectrometry; 2 * 14284, reduced protein after alkylation corresponding to the theoretical mass of the recombinant protein with four iodoacetamide mediated modifications of cysteines, MALDI-TOF mass spectrometry
homodimer
-
2 * 14000, SDS-PAGE; 2 * 14056, unmodified recombinant WhiB1, MALDI-TOF mass spectrometry; 2 * 14284, reduced protein after alkylation corresponding to the theoretical mass of the recombinant protein with four iodoacetamide mediated modifications of cysteines, MALDI-TOF mass spectrometry
-
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
phospholipoprotein
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystallized at 25°C using the hanging-drop vapour-diffusion method, crystals belong to the space group I222 or I2(1)2(1)2(1), with unit-cell parameters a = 90.59, b = 102.43, c = 128.96 A
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homology modeling; homology modeling
to 1.77 A resolution. The structure harbors a thioredoxin-like domain and an extended alpha-helical domain
homology modeling.Csteine residues, Cys58 and Cys95 come in close proximity in the tertiary structure with pKa value 9. The residues are involved in the disulfide oxidoreductase catalytic activity
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
60
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
dimerization after prolonged storage at -20°C, freeze-thawing or heating at 60°C
-
EDTA 5mM, 37°C, phosphate buffer, total loss of activity within 30-60 min, can partially be prevented by NADPH
-
EDTA stabilizes during purification
metal ions required for activity and maintenance of the proper conformation of the enzyme
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, 90% of the enzyme is converted from its native form with MW 60000 to a fragment of MW 40000-45000
-
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme
-
-
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
characterization of cDNA for human glutathione-insulin transhydrogenase, amino acid sequence analysis, 94% homology to rat amino acid sequence
expression in Escherichia coli
successfully expressed in Brevibacillus choshinensis extracellularly using the secretion vector pNCMO2, and in Escherichia coli intracellularly with an amino-terminal His-tag. Coexpression of CatA protein with recombinant hEGF in the Brevibacillus choshinensis production system increases the yield of native hEGF
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systematic gene function analysis programm, expression of diverse constructs in Escherichia coli and Bacillus subtilis
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characterization of cDNA for human glutathione-insulin transhydrogenase, amino acid sequence analysis, 94% homology to rat amino acid sequence
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characterization of cDNA for human glutathione-insulin transhydrogenase, amino acid sequence analysis, 94% homology to rat amino acid sequence
-
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
H33G
-
the mutant shows a loss of the capacity of the protein to isomerize, or shuffle, incorrect disulfides of scrambled RNase A yielding 10% active RNase A only
additional information
-
DsbA and DsbB insertion mutants are sensitive to dithiothreitol and benzylpenicillin or Cd2+, Hg2+ and Zn2+, pleitropic phenotype
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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LINKS TO OTHER DATABASES (specific for EC-Number 1.8.4.2)
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