BRENDA home
History
Information on EC 1.8.4.2 - protein-disulfide reductase (glutathione)
for references in articles please use BRENDA:EC1.8.4.2Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
1.8.4.2 protein-disulfide reductase (glutathione)IUBMB Comments
Reduces insulin and some other proteins.
Specify your search results
Word Map
- 1.8.4.2
-
tautomerase
-
insulin-degrading
-
5.3.4.1
- dsbas
- d-dopachrome
-
whib-like
-
thioredoxin-like
-
disulphide-isomerase
- 125i-insulin
- medicine
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
BbdC, BdbD, CatA protein, ccdA associated thiol-disulfide oxidoreductase, DcbA, desulfothioredoxin, DIP1880, disulphide interchange enzyme, DsbA1, DsbA2, 
more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
DIP1880
disulphide interchange enzyme
GIT
glutathione-insulin transhydrogenase
-
-
-
-
glutathione-protein disulfide oxidoreductase
-
-
-
-
GSH-insulin transhydrogenase
-
-
-
-
HP_0231
insulin reductase
-
-
-
-
MdbA
protein disulfide reductase (glutathione)
-
-
-
-
protein disulfide transhydrogenase
-
-
-
-
protein-disulfide interchange enzyme
-
-
-
-
protein-disulfide isomerase/oxidoreductase
-
-
-
-
reductase, protein disulfide (glutathione)
-
-
-
-
SdbA
TDOR
thiol-disulfide oxidoreductase
thiol-protein disulphide oxidoreductase
-
-
-
-
thiol:protein-disulfide oxidoreductase
-
-
-
-
WhiB1
WhiB1/Rv3219
additional information
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
-
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
-
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
-
DsbA protein family including periplasmic protein disulfide: thiol oxidoreductases with high homology in amino acid sequences
additional information
-
DsbA protein family including periplasmic protein disulfide: thiol oxidoreductases with high homology in amino acid sequences
additional information
-
thiol-disulfide oxidoreductase of the thioredoxin family
additional information
-
protein-disulfide isomerase EC 5.3.4.1 and protein-disulfide oxidoreductase EC 1.8.4.2 are identical and form the glutathione-insulin transhydrogenase
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
-
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
-
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
-
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2 glutathione + protein-disulfide = glutathione-disulfide + protein-dithiol
mechanism
-
2 glutathione + protein-disulfide = glutathione-disulfide + protein-dithiol
random 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
-
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
zinc finger protein with several CXXC motifs
-
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
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
insulin inducible
-
2 glutathione + protein-disulfide = glutathione-disulfide + protein-dithiol
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY SOURCE
PATHWAYS
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
glutathione:protein-disulfide oxidoreductase
Reduces insulin and some other proteins.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
9082-53-5
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
reduced dithiothreitol + NADP+
oxidized dithiothreitol + NADPH + H+
-
-
-
-
r
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, 394848, 394849, 394851
-
-
?
GSH + insulin
GSSG + reduced insulin chain A and B
-
-
-
-
?
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
-
-
?
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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL 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
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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Burkitt Lymphoma
Multiprotein complexes present at the MIF motifs flanking the promoter of the human c-myc gene.
Cardiovascular Diseases
MIF family cytokines in cardiovascular diseases and prospects for precision-based therapeutics.
Diabetic Nephropathies
TWEAK increases CD74 expression and sensitizes to DDT proinflammatory actions in tubular cells.
Endotoxemia
Differential regulation of macrophage activation by the MIF cytokine superfamily members MIF and MIF-2 in adipose tissue during endotoxemia.
Hyperinsulinism
Insulin degradation. XVIII. On the regulation of glutathione-insulin transhydrogenase in the hyperglycemic obese (ob/ob) mouse.
Hypersensitivity
Levodopa deactivates enzymes that regulate thiol-disulfide homeostasis and promotes neuronal cell death: implications for therapy of Parkinson's disease.
Insulin Resistance
Serum insulin concentration, insulin release and degradation, glucose tolerance and in vivo insulin sensitivity in cholesterol-fed rats.
Insulinoma
Insulin degradation in insulinoma: evidence for the occurrence of an inactive form of glutathione-insulin transhydrogenase and for the absence of insulin A and B chains degrading protease(s).
Lysosomal Storage Diseases
Inhibition of CatA: an emerging strategy for the treatment of heart failure.
Obesity
Insulin degradation. XVIII. On the regulation of glutathione-insulin transhydrogenase in the hyperglycemic obese (ob/ob) mouse.
Pneumonia
Interaction of MIF Family Proteins in Myocardial Ischemia/Reperfusion Damage and Their Influence on Clinical Outcome of Cardiac Surgery Patients.
Renal Insufficiency, Chronic
Elevated MIF-2 levels predict mortality in critically ill patients.
Tuberculosis
Characterization of Mycobacterium tuberculosis WhiB1/Rv3219 as a protein disulfide reductase.
Tuberculosis
Mechanistic insight into the nitrosylation of the [4Fe-4S] cluster of WhiB-like proteins.
Tuberculosis
Mycobacterium tuberculosis WhiB1 is an essential DNA-binding protein with a nitric oxide sensitive iron-sulphur cluster.
Tuberculosis
Mycobacterium tuberculosis WhiB1 represses transcription of the essential chaperonin GroEL2.
Tuberculosis
Redox biology of Mycobacterium tuberculosis H37Rv: protein-protein interaction between GlgB and WhiB1 involves exchange of thiol-disulfide.
Tuberculosis
Regulation of the expression of whiB1 in Mycobacterium tuberculosis: role of cAMP receptor protein.
Tuberculosis
Structural basis of non-canonical transcriptional regulation by the ?A-bound iron-sulfur protein WhiB1 in M. tuberculosis.
Tuberculosis
Structure of a Wbl protein and implications for NO sensing by M. tuberculosis.
Tuberculosis
Structure-function relationships of the Mycobacterium tuberculosis transcription factor WhiB1.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
-
additional information
additional information
-
Km in different tissues for GSH and insulin
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
DsbA homologous
-
-
brenda
DsbA homologous
-
-
brenda
-
3051, 394810, 394811, 394817, 394819, 394825, 394826, 394827, 394828, 394829, 394831, 394833, 394834, 394835, 394836, 394837, 394838, 394839, 394845, 394847, 394848, 394849, 394851
-
-
brenda
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
-
-
brenda
macrophage migration inhibitory factor is a cytokine and pituitary hormone
-
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
brenda
-
-
3051, 3052, 394810, 394817, 394825, 394827, 394828, 394829, 394832, 394834, 394835, 394836, 394838, 394839, 394840, 394847
brenda
-
-
3067, 394810, 394812, 394813, 394814, 394815, 394816, 394817, 394818, 394820, 394821, 394823, 394830, 394832, 394847
brenda
-
-
brenda
additional information
-
higher activity in mononuclear cells than in polymorphonuclear cells
brenda
additional information
-
relative activities of enzyme in various tissues
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
of alpha and beta cells of islets of Langerhans
brenda
-
membrane-associated with its thioredoxin-like domain on the outside of the cytoplasmic membrane
brenda
-
outer cytoplasmic membrane, protein termini localised in the periplasm
brenda
-
weakly bound on cisternal surface of microsomes via phospholipids
-
brenda
-
DsbA protein soluble, DsbB protein is membrane intrinsic
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
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
-
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
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
physiological function
-
loss of isoform DsbA2 has no impact on motility and autoagglutination phenotypes. DsbA2 is crucial for the activity of arylsulfotransferase AstA
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
-
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
-
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
-
physiological function
-
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
-
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
-
Show AA Sequence and Transmembrane Helices (643 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PDB
SCOP
CATH
UNIPROT
ORGANISM
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
120000
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
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
-
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
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 * 14056, unmodified recombinant WhiB1, MALDI-TOF mass spectrometry
homodimer
-
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 * 14056, unmodified recombinant WhiB1, MALDI-TOF mass spectrometry
-
homodimer
-
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
phospholipoprotein
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PROTEIN VARIANTS
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
60
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
systematic gene function analysis programm, expression of diverse constructs in Escherichia coli and Bacillus subtilis
-
characterization of cDNA for human glutathione-insulin transhydrogenase, amino acid sequence analysis, 94% homology to rat amino acid sequence
-
characterization of cDNA for human glutathione-insulin transhydrogenase, amino acid sequence analysis, 94% homology to rat amino acid sequence
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hillson, D.A.; Freedman, R.B.
Resolution of protein disulphide-isomerase and glutathione-insulin transhydrogenase activities by covalent chromatography
Biochem. J.
191
373-388
1980
Bos taurus
brenda
Hawkins, H.C.; Freedman, R.B.
Thiol-protein disulphide oxidoreductases. Differences between protein disulphide-isomerase and glutathione-insulin transhydrogenase activities in ox liver
Biochem. J.
159
385-393
1976
Bos taurus
brenda
Ibbetson, A.L.; Freedman, R.B.
Thiol-protein disulphide oxidoreductases. Assay of microsomal membrane-bound glutathione-insulin transhydrogenase and comparison with protein disulphide-isomerase
Biochem. J.
159
377-384
1976
Rattus norvegicus
brenda
Varandani, P.T.
Glutathione-insulin transhydrogenase (protein-disulfide interchange enzyme)
Coenzymes and cofactors, Glutathione, Chem. Biochem. Med. Aspects Pt. A (Dolphin D, Poulson R, Avromonic O, eds. ) John Wiley & Sons, New York
3
753-765
1989
Bos taurus, Homo sapiens, Mus musculus, Rattus norvegicus
-
brenda
Varandani, P.T.
Mechanistic and structural aspects of glutathione-insulin transhydogenase (protein-disulfide interchange enzyme)
Dev. Biochem.
1
29-42
1978
Bos taurus, Homo sapiens, Rattus norvegicus
-
brenda
Morris, J.I.; Varandani, P.T.
Characterization of a cDNA for human glutathione-insulin transhydrogenase (protein-disulfide isomerase/oxidoreductase)
Biochim. Biophys. Acta
949
169-180
1988
Homo sapiens, Rattus norvegicus
brenda
Chowdhary, B.K.; Smith, G.D.; Mahler, R.; Peters, T.J.
Studies on the subcellular localization and role of glutathione-insulin transhydrogenase in rat liver
Biosci. Rep.
3
323-329
1983
Rattus norvegicus
brenda
Hern, E.P.; Varandani, P.T.
Nonlatent and latent hepatic glutathione-insulin transhydrogenase activity during perinatal development and liver regeneration in rats and in rat placenta
Biochem. Biophys. Res. Commun.
116
909-915
1983
Rattus norvegicus
brenda
Spolter, P.D.; Vogel, J.M.
Rat-liver thiol: protein-disulphide oxidoreductase
Biochim. Biophys. Acta
167
525-537
1968
Rattus norvegicus
brenda
Varandani, P.T.
Insulin degradation. I. Purification and properties of glutathione-insulin transhydrogenase of rat liver
Biochim. Biophys. Acta
286
126-135
1972
Rattus norvegicus
brenda
Chandler, M.L.; Varandani, P.T.
Insulin degradation. II. The widespread distribution of glutathione-insulin transhydrogenase in the tissues of the rat
Biochim. Biophys. Acta
286
136-145
1972
Bos taurus, Rattus norvegicus
brenda
Varandani, P.T.
Insulin degradation. V. Unmasking of glutathione-insulin transhydrogenase in rat liver microsomal membrane
Biochim. Biophys. Acta
304
642-659
1973
Rattus norvegicus
brenda
Chandler, M.L.; Varandani, P.T.
Insulin degradation. 8. Protein thiols as co-substrates for glutathione-insulin transhydrogenase
Biochim. Biophys. Acta
320
258-266
1973
Bos taurus
brenda
Ansorge, S.; Bohley, P.; Kirschke, H.; Langner, J.; Wiederanders, B.; Hanson, H.
Metabolism of insulin and glucagon. Glutathione-insulin transhydrogenase from microsomes of rat liver
Eur. J. Biochem.
32
27-35
1973
Rattus norvegicus
brenda
Varandani, P.T.
Insulin degradation. X. Identification of insulin degrading activity of rat liver plasma membrane as glutathione-insulin transhydrogenase
Biochem. Biophys. Res. Commun.
55
689-696
1973
Rattus norvegicus
brenda
Hern, E.P.; Varandani, P.T.
Topology of glutathione-insulin transhydrogenase in rat liver microsomes
Biochim. Biophys. Acta
732
170-178
1983
Rattus norvegicus
brenda
Kohnert, K.D.; Hahn, H.J.; Zuhlke, H.; Schmidt, S.; Fiedler, H.
Breakdown of exogenous insulin by Langerhans islets of the pancreas in vitro
Biochim. Biophys. Acta
338
68-77
1974
Mus musculus, Rattus norvegicus
-
brenda
Schneider, F.; Schauer, R.; Martini, O.; Hahn, J.
Reversibility of glutathione-insulin-transhydrogenation (protein disulfide-reductase reaction)
Hoppe-Seyler's Z. Physiol. Chem.
348
391-400
1967
Bos taurus
brenda
Varandani, P.T.
Insulin degradation. XII. The amino acid composition, amino-terminal, and carbohydrate content of beef pancreatic glutathione-insulin transhydrogenase
Biochim. Biophys. Acta
371
577-581
1974
Bos taurus
brenda
Bjelland, S.; Wallevik, K.; Kroll, J.; Dixon, J.E.; Morin, J.E.; Freedman, R.B.; Lambert, N.; Varandani, P.T.; Nafz, M.A.
Immunological identity between bovine preparations of thiol:protein-disulphide oxidoreductase, glutathione-insulin transhydrogenase and protein-disulphide isomerase
Biochim. Biophys. Acta
747
197-199
1983
Bos taurus
brenda
Bjelland, S.
Tissue distribution and molecular heterogeneity of bovine thiol:protein-disulphide oxidoreductase (disulphide interchange enzyme)
Comp. Biochem. Physiol. B
87
907-914
1987
Bos taurus
brenda
Bjelland, S.; Foltmann, B.; Wallevik, K.
Purification of thiol:protein-disulfide oxidoreductase from bovine liver
Anal. Biochem.
142
463-466
1984
Bos taurus
brenda
Roth, R.A.
Bacitracin: an inhibitor of the insulin degrading activity of glutathione-insulin transhydrogenase
Biochem. Biophys. Res. Commun.
98
431-438
1981
Rattus norvegicus
brenda
Varandani, P.T.; Plumley, H.
Mechanism of action of glutathione-insulin transhydrogenase. Presence of a functional sulfhydryl group for activity
Biochim. Biophys. Acta
151
273-275
1968
Bos taurus
brenda
Barbieri, L.; Batelli, M.G.; Stirpe, F.
Reduction of ricin and other plant toxins by thiol:protein disulfide oxidoreductases
Arch. Biochem. Biophys.
216
380-383
1982
Bos taurus, Rattus norvegicus
brenda
Chandler, M.L.; Varandani, P.T.
Insulin degradation. XV. Use of different assay methods for the study of mechanism of action of glutathione-insulin transhydrogenase
Biochim. Biophys. Acta
397
307-317
1975
Bos taurus
brenda
Moss, J.; Stanley, S.J.; Morin, J.E.; Dixon, J.E.
Activation of choleragen by thiol: protein disulfide oxidoreductase
J. Biol. Chem.
255
11085-11087
1980
Bos taurus
brenda
Pace, M.; Pietta, P.G.; Fiorino, A.; Pocaterra, E.; Dixon, J.E.
Nonspecific reaction of a thiol: protein disulfide oxidoreductase with the disulfide bonds of insulin
Experientia
41
1332-1335
1985
Bos taurus
brenda
Pace, M.; Dixon, J.E.
The nature of the multiple forms of bovine thiol:protein disulfide oxidoreductase
Int. J. Pept. Protein Res.
14
409-413
1979
Bos taurus
brenda
Varandani, P.T.; Nafz, M.A.; Chandler, M.L.
Interaction of insulin analogs, glucagon, growth hormone, vasopressin, oxytocin, and scrambled forms of ribonuclease and lysozyme with glutathione-insulin transhydrogenase (thiol: protein-disulfide oxidoreductase): dependence upon conformation
Biochemistry
14
2115-2120
1975
Bos taurus
brenda
Carmichael, D.F.; Morin, J.E.; Dixon, J.E.
Purification and characterization of a thiol:protein disulfide oxidoreductase from bovine liver
J. Biol. Chem.
252
7163-7167
1977
Bos taurus
brenda
Hillson, D.A.; Freedman, R.B.
Bovine liver thiol-protein disulphide oxidoreductases. An alternative method for differential purification and resolution of protein disulphide-isomerase and glutathione-insulin transhydrogenase
Biochem. J.
191
389-393
1980
Bos taurus
brenda
Tomizawa, H.H.
Glutathione-insulin transhydrogenase (steer liver)
Methods Enzymol.
17B
515-519
1971
Bos taurus
-
brenda
Morin, J.E.; Dixon, J.E.; Chang, P.P.; Moss, J.
Identification of thiol:protein disulfide oxidoreductase activity in cultured human fibroblasts: dependence of enzyme activity on growth conditions
Biochem. Biophys. Res. Commun.
111
872-877
1983
Homo sapiens
brenda
Ferrier, B.M.; Hendrie, J.M.; Cardy, C.A.
Glutathione-insulin transhydrogenase activity in pregnant mouse mammary gland: hormonal influences studied in tissue culture
Can. J. Biochem.
55
340-345
1977
Mus musculus
brenda
Kohnert, K.D.; Jahr, H.; Schmidt, S.; Hahn, H.J.; Zuhlke, H.
Demonstration of insulin degradation by thiol-protein disulfide oxidoreductase (glutathione-insulin transhydrogenase) and proteinases of pancreatic islets
Biochim. Biophys. Acta
422
254-259
1976
Rattus norvegicus
brenda
Roth, R.A.; Koshland, M.E.
Role of disulfide interchange enzyme in immunoglobulin synthesis
Biochemistry
20
6594-6599
1981
Mus musculus
brenda
Lambert, N.; Freedman, R.B.
Kinetics and specificity of homogeneous protein disulphide-isomerase in protein disulphide isomerization and in thiol-protein-disulphide oxidoreduction
Biochem. J.
213
235-243
1983
Bos taurus
brenda
Varandani, P.T.
Insulin degradation in insulinoma: evidence for the occurrence of an inactive form of glutathione-insulin transhydrogenase and for the absence of insulin A and B chains degrading protease(s)
Biochem. Biophys. Res. Commun.
60
1119-1126
1974
Homo sapiens
brenda
Varandani, P.T.; Nafz, M.A.
Interaction of glutathione-insulin transhydrogenase (disulfide interchange enzyme) with phospholipids
Biochim. Biophys. Acta
438
358-369
1976
Bos taurus, Rattus norvegicus
brenda
Morin, J.E.; Carmichael, C.F.; Dixon, J.E.
Characterization, kinetics and comparative properties of thiol:protein disulfide oxidoreductase
Arch. Biochem. Biophys.
189
354-363
1978
Bos taurus
brenda
Varandani, P.T.; Nafz, M.A.
Inhibition of glutathione-insulin transhydrogenase by metal ions and activation by histidine and other chelating agents
Biochim. Biophys. Acta
832
7-13
1985
Bos taurus
brenda
Chandler, M.L.; Varandani, P.T.
Kinetic analysis of the mechanism of insulin degradation by glutathione-insulin transhydrogenase (thiol: protein-disulfide oxidoreductase)
Biochemistry
14
2107-2115
1975
Bos taurus
brenda
Fabianek, R.A.; Hennecke, H.; Thony-Meyer, L.
Periplasmic protein thiol:disulfide oxidoreductases of Escherichia coli
FEMS Microbiol. Rev.
24
303-316
2000
Escherichia coli, Pectobacterium carotovorum, Dickeya chrysanthemi, Haemophilus influenzae, Klebsiella sp., Yersinia pestis, Salmonella enterica subsp. enterica serovar Typhimurium, Salmonella enterica subsp. enterica serovar Enteritidis, Shigella flexneri, Vibrio cholerae serotype O1, Pseudomonas syringae (O52376), Pseudomonas aeruginosa (P0C2B2), Legionella pneumophila (P50024), Lelliottia amnigena (Q9XDP0), Yersinia pestis DsbA homologous, Dickeya chrysanthemi DsbA homologous, Vibrio cholerae serotype O1 DsbA homologous, Salmonella enterica subsp. enterica serovar Enteritidis DsbA homologous, Salmonella enterica subsp. enterica serovar Typhimurium DsbA homologous, Haemophilus influenzae DsbA homologous, Klebsiella sp. DsbA homologous, Pectobacterium carotovorum DsbA homologous, Legionella pneumophila DsbA homologous (P50024), Pseudomonas syringae DsbA homologous (O52376), Shigella flexneri DsbA homologous, Pseudomonas aeruginosa DsbA homologous (P0C2B2), Lelliottia amnigena DsbA homologous (Q9XDP0)
brenda
Biaglow, J.E.; Donahue, J.; Tuttle, S.; Held, K.; Chrestensen, C.; Mieyal, J.
A method for measuring disulfide reduction by cultured mammalian cells: relative contributions of glutathione-dependent and glutathione-independent mechanisms
Anal. Biochem.
281
77-86
2000
Cricetulus griseus, Homo sapiens
brenda
Loferer, H.; Hennecke, H.
Protein disulfide oxidoreductases in bacteria
Trends Biochem. Sci.
19
169-171
1994
Escherichia coli, Haemophilus influenzae, Vibrio cholerae serotype O1, Vibrio cholerae serotype O1 DsbA homologous, Haemophilus influenzae DsbA homologous
brenda
Heuck, A.P.; Wolosiuk, R.A.
Di-fluoresceinthiocarbamyl-insulin: A fluorescent substrate for the assay of protein disulfide oxidoreductase activity
Anal. Biochem.
248
94-101
1997
Brassica napus
brenda
Moessner, E.; Iwai, H.; Glockshuber, R.
Influence of the pKa value of the buried, active-site cysteine on the redox properties of thioredoxin-like oxidoreductases
FEBS Lett.
477
21-26
2000
Escherichia coli
brenda
Tang, W.; Wang, C.C.
Zinc fingers and thiol-disulfide oxidoreductase activities of chaperone DnaJ
Biochemistry
40
14985-14994
2001
Escherichia coli
brenda
Ishihara, T.; Tomita, H.; Hasegawa, Y.; Tsukagoshi, N.; Yamagata, H.; Udaka, S.
Cloning and characterization of the gene for a protein thiol-disulfide oxidoreductase in Bacillus brevis
J. Bacteriol.
177
745-749
1995
Brevibacillus brevis
brenda
Meima, R.; Eschevins, C.; Fillinger, S.; Bolhuis, A.; Hamoen, L.W.; Dorenbos, R.; Quax, W.J.; Van Dijl, J.M.; Provvedi, R.; Chen, I.; Dubnau, D.; Bron, S.
The bdbDC operon of Bacillus subtilis encodes thiol-disulfide oxidoreductases required for competence development
J. Biol. Chem.
277
6994-7001
2002
Bacillus subtilis
brenda
Van Straaten, M.; Missiakas, D.; Raina, S.; Darby, N.J.
The functional properties of DsbG, a thiol-disulfide oxidoreductase from the periplasm of Escherichia coli
FEBS Lett.
428
255-258
1998
Escherichia coli
brenda
Dorenbos, R.; Stein, T.; Kabel, J.; Bruand, C.; Bolhuis, A.; Bron, S.; Quax, W.J.; Van Dijl, J.M.
Thiol-disulfide oxidoreductases are essential for the production of the lantibiotic sublancin 168
J. Biol. Chem.
277
16682-16688
2002
Bacillus subtilis
brenda
Kleemann, R.; Rorsman, H.; Rosengren, E.; Mischke, R.; Mai, N.T.; Bernhagen, J.
Dissection of the enzymatic and immunologic functions of macrophage migration inhibitory factor. Full immunologic activity of N-terminally truncated mutants
Eur. J. Biochem.
267
7183-7192
2000
Homo sapiens
brenda
Erlendsson, L.S.; Hederstedt, L.
Mutations in the thiol-disulfide oxidoreductases BdbC and BdbD can suppress cytochrome c deficiency of CcdA-defective Bacillus subtilis cells
J. Bacteriol.
184
1423-1429
2002
Bacillus subtilis
brenda
Erlendsson, L.S.; Moller, M.; Hederstedt, L.
Bacillus subtilis StoA Is a thiol-disulfide oxidoreductase important for spore cortex synthesis
J. Bacteriol.
186
6230-6238
2004
Bacillus subtilis
brenda
Philipps, B.; Glockshuber, R.
Randomization of the entire active-site helix alpha 1 of the thiol-disulfide oxidoreductase DsbA from Escherichia coli
J. Biol. Chem.
277
43050-43057
2002
Escherichia coli
brenda
Erlendsson, L.S.; Acheson, R.M.; Hederstedt, L.; Le Brun, N.E.
Bacillus subtilis ResA is a thiol-disulfide oxidoreductase involved in cytochrome c synthesis
J. Biol. Chem.
278
17852-17858
2003
Bacillus subtilis
brenda
Frickel, E.M.; Frei, P.; Bouvier, M.; Stafford, W.F.; Helenius, A.; Glockshuber, R.; Ellgaard, L.
ERp57 is a multifunctional thiol-disulfide oxidoreductase
J. Biol. Chem.
279
18277-18287
2004
Homo sapiens
brenda
Tanaka, R.; Mizukami, M.; Ishibashi, M.; Tokunaga, H.; Tokunaga, M.
Cloning and expression of the ccdA-associated thiol-disulfide oxidoreductase (catA) gene from Brevibacillus choshinensis: stimulation of human epidermal growth factor production
J. Biotechnol.
103
1-10
2003
Brevibacillus choshinensis
brenda
Crow, A.; Le Brun, N.E.; Oubrie, A.
The role of ResA in type II cytochrome c maturation
Biochem. Soc. Trans.
33
149-151
2005
Bacillus subtilis
brenda
Zhang, X.; Hu, Y.; Guo, X.; Lescop, E.; Li, Y.; Xia, B.; Jin, C.
The Bacillus subtilis YkuV is a thiol:disulfide oxidoreductase revealed by its redox structures and activity
J. Biol. Chem.
281
8296-8304
2006
Bacillus subtilis
brenda
Colbert, C.L.; Wu, Q.; Erbel, P.J.; Gardner, K.H.; Deisenhofer, J.
Mechanism of substrate specificity in Bacillus subtilis ResA, a thioredoxin-like protein involved in cytochrome c maturation
Proc. Natl. Acad. Sci. USA
103
4410-4415
2006
Bacillus subtilis
brenda
Garg, S.K.; Suhail Alam, M.; Soni, V.; Radha Kishan, K.V.; Agrawal, P.
Characterization of Mycobacterium tuberculosis WhiB1/Rv3219 as a protein disulfide reductase
Protein Expr. Purif.
52
422-432
2007
Mycobacterium tuberculosis
brenda
Tanaka, R.; Mizukami, M.; Tokunaga, M.
Novel processing and localization of catA, ccdA associated thiol-disulfide oxidoreductase, in protein hyper-producing bacterium Brevibacillus choshinensis
Protein Pept. Lett.
12
95-98
2005
Brevibacillus choshinensis
brenda
Osipova, S.; Permyakov, A.; Mitrofanova, T.; Trufanov, V.; Ermakova, M.; Chistyakova, A.; Pshenichnikova, T.
GSH-dependent protein disulfide oxidoreductase of wheat grain: activity in maturing wheat kernels, and relationship with rheological properties of dough
Cereal Res. Commun.
35
1477-1486
2007
Triticum aestivum
-
brenda
Garcin, E.B.; Bornet, O.; Elantak, L.; Vita, N.; Pieulle, L.; Guerlesquin, F.; Sebban-Kreuzer, C.
Structural and mechanistic insights into unusual thiol disulfide oxidoreductase
J. Biol. Chem.
287
1688-1697
2012
Desulfovibrio vulgaris
brenda
Davey, L.; Ng, C.K.; Halperin, S.A.; Lee, S.F.
Functional analysis of paralogous thiol-disulfide oxidoreductases in Streptococcus gordonii
J. Biol. Chem.
288
16416-16429
2013
Streptococcus gordonii
brenda
D'Ambrosio, K.; De Simone, G.; Pedone, E.; Rossi, M.; Bartolucci, S.; Pedone, C.
Crystallization and preliminary X-ray diffraction studies of a protein disulfide oxidoreductase from Aeropyrum pernix K1
Acta Crystallogr. Sect. F
61
335-336
2005
Aeropyrum pernix, Aeropyrum pernix DSM 11879
brenda
Chauhan, N.; Hoti, S.L.
Role of cysteine-58 and cysteine-95 residues in the thiol di-sulfide oxidoreductase activity of macrophage migration inhibitory factor-2 of Wuchereria bancrofti
Acta Trop.
153
14-20
2016
Wuchereria bancrofti (A0A088FMA5)
brenda
Roszczenko, P.; Grzeszczuk, M.; Kobierecka, P.; Wywial, E.; Urbanowicz, P.; Wincek, P.; Nowak, E.; Jagusztyn-Krynicka, E.
Helicobacter pylori HP0377, a member of the Dsb family, is an untypical multifunctional CcmG that cooperates with dimeric thioldisulfide oxidase HP0231
BMC Microbiol.
15
135
2015
Helicobacter pylori (O25017), Helicobacter pylori ATCC 700392 (O25017)
brenda
Davey, L.; Halperin, S.; Lee, S.
Mutation of the thiol-disulfide oxidoreductase SdbA activates the CiaRH two-component system, leading to bacteriocin expression shutdown in Streptococcus gordonii
J. Bacteriol.
198
321-331
2016
Streptococcus gordonii, Streptococcus gordonii SecCR1
brenda
Luong, T.; Reardon-Robinson, M.; D.Siegel, S.; Ton-That, H.
Reoxidation of the thiol-disulfide oxidoreductase MdbA by a bacterial vitamin K epoxide reductase in the biofilm-forming actinobacterium Actinomyces oris
J. Bacteriol.
199
e00817
2017
Actinomyces oris (A0A0M3KL32)
brenda
Reardon-Robinson, M.E.; Osipiuk, J.; Jooya, N.; Chang, C.; Joachimiak, A.; Das, A.; Ton-That, H.
A thiol-disulfide oxidoreductase of the Gram-positive pathogen Corynebacterium diphtheriae is essential for viability, pilus assembly, toxin production and virulence
Mol. Microbiol.
98
1037-1050
2015
Corynebacterium diphtheriae (Q6NFK7), Corynebacterium diphtheriae ATCC 700971 (Q6NFK7)
brenda
Grabowska, A.D.; Wywial, E.; Dunin-Horkawicz, S.; Lasica, A.M.; Woesten, M.M.; Nagy-Staron, A.; Godlewska, R.; Bocian-Ostrzycka, K.; Pienkowska, K.; Laniewski, P.; Bujnicki, J.M.; van Putten, J.P.; Jagusztyn-Krynicka, E.K.
Functional and bioinformatics analysis of two Campylobacter jejuni homologs of the thiol-disulfide oxidoreductase, DsbA
PLoS ONE
9
e106247
2014
Campylobacter jejuni subsp. jejuni
brenda
Select items on the left to see more content.
EXTERNAL LINKS (specific for EC-Number 1.8.4.2)
html completed
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
About BRENDA
Help
Download
Contribution
member of
curated at
curated at
Server: brenda4 Ver: 9edf756-main (2022-05-17 10:30:03 +0200)