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Information on EC 1.8.4.2 - protein-disulfide reductase (glutathione)
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1.8.4.2 protein-disulfide reductase (glutathione)IUBMB Comments
Reduces insulin and some other proteins.
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Word Map
- 1.8.4.2
-
tautomerase
- glutaredoxins
-
insulin-degrading
- d-dopachrome
-
5.3.4.1
- dsbas
-
whib-like
-
thioredoxin-like
- 125i-insulin
-
disulphide-isomerase
- medicine
The enzyme appears in viruses and cellular organisms
Synonyms
glutathione-insulin transhydrogenase, whib1, mif-2, dsba2, dsba1, thiol disulfide oxidoreductase, grxs12, insulin reductase, gsh-insulin transhydrogenase, thiol:protein-disulfide oxidoreductase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
COA6
DIP1880
disulphide interchange enzyme
DsbA
GIT
glutathione-insulin transhydrogenase
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glutathione-protein disulfide oxidoreductase
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GSH-insulin transhydrogenase
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HP_0231
insulin reductase
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MdbA
MdbACm
protein disulfide reductase (glutathione)
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protein disulfide transhydrogenase
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protein-disulfide interchange enzyme
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protein-disulfide isomerase/oxidoreductase
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RCAP_rcc01743
reductase, protein disulfide (glutathione)
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SdbA
SGO_2006
Streptococcus disulfide bond protein A
TDOR
thiol-disulfide oxidoreductase
thiol-protein disulphide oxidoreductase
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thiol:protein-disulfide oxidoreductase
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WhiB1
WhiB1/Rv3219
YMR244C-A
additional information
additional information
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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
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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
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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
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the two activities, cleavage and formation of protein-disulfide bonds, present alternate activities of the same enzyme
additional information
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the two activities, cleavage and formation of protein-disulfide bonds, present alternate activities of the same enzyme
additional information
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the two activities, cleavage and formation of protein-disulfide bonds, present alternate activities of the same enzyme
additional information
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the two activities, cleavage and formation of protein-disulfide bonds, present alternate activities of the same enzyme
additional information
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thiol:protein-disulfide oxidoreductase EC 1.8.4.2 and thiol:protein-disulfide isomerase EC 5.3.4.1 are immunological identical
additional information
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thiol:protein-disulfide oxidoreductase EC 1.8.4.2 and thiol:protein-disulfide isomerase EC 5.3.4.1 are immunological identical
additional information
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thiol:protein-disulfide oxidoreductase EC 1.8.4.2 and thiol:protein-disulfide isomerase EC 5.3.4.1 are immunological identical
additional information
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DsbA protein family including periplasmic protein disulfide: thiol oxidoreductases with high homology in amino acid sequences
additional information
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DsbA protein family including periplasmic protein disulfide: thiol oxidoreductases with high homology in amino acid sequences
additional information
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thiol-disulfide oxidoreductase of the thioredoxin family
additional information
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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
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the two activities, cleavage and formation of protein-disulfide bonds, present alternate activities of the same enzyme
additional information
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the two activities, cleavage and formation of protein-disulfide bonds, present alternate activities of the same enzyme
additional information
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thiol:protein-disulfide oxidoreductase EC 1.8.4.2 and thiol:protein-disulfide isomerase EC 5.3.4.1 are immunological identical
additional information
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thiol:protein-disulfide oxidoreductase EC 1.8.4.2 and thiol:protein-disulfide isomerase EC 5.3.4.1 are immunological identical
additional information
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the two activities, cleavage and formation of protein-disulfide bonds, present alternate activities of the same enzyme
additional information
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thiol:protein-disulfide oxidoreductase EC 1.8.4.2 and thiol:protein-disulfide isomerase EC 5.3.4.1 are immunological identical
additional information
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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
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thiol:protein-disulfide oxidoreductase EC 1.8.4.2 and thiol:protein-disulfide isomerase EC 5.3.4.1 are immunological identical
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2 glutathione + protein-disulfide = glutathione-disulfide + protein-dithiol
mechanism
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2 glutathione + protein-disulfide = glutathione-disulfide + protein-dithiol
random mechanism
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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
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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
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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
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2 glutathione + protein-disulfide = glutathione-disulfide + protein-dithiol
zinc finger protein with several CXXC motifs
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2 glutathione + protein-disulfide = glutathione-disulfide + protein-dithiol
high similarity between enzymes of different species and sources, respectively
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2 glutathione + protein-disulfide = glutathione-disulfide + protein-dithiol
random and allosteric mechanism via multiple distinct reaction sites
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2 glutathione + protein-disulfide = glutathione-disulfide + protein-dithiol
random and allosteric mechanism via multiple distinct reaction sites
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2 glutathione + protein-disulfide = glutathione-disulfide + protein-dithiol
random and allosteric mechanism via multiple distinct reaction sites
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2 glutathione + protein-disulfide = glutathione-disulfide + protein-dithiol
insulin inducible
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2 glutathione + protein-disulfide = glutathione-disulfide + protein-dithiol
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
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redox reaction
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reduction
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-
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PATHWAY SOURCE
PATHWAYS
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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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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 glutathione + SCO2-disulfide
glutathione-disulfide + SCO2-dithiol
-
-
-
?
2,3-dimercaptopropanol + protein disulfide
2,3-dimercaptopropanol disulfide + protein-dithiol
2-mercaptoethanol glutathione disulfide + glutathione
2-mercaptoethanol disulfide + glutathione disulfide
glutathionylated glyceraldehyde-3-phosphate dehydrogenase + glutathione
glutathione disulfide + glyceraldehyde-3-phosphate dehydrogenase
glutathionylated glyceraldehyde-3-phosphate dehydrogenase + reduced GRX3
glutathione + glyceraldehyde-3-phosphate dehydrogenase + oxidized GRX3
substrate is glutathionylated A4-GAPDH. A4-GAPDH activity is reversibly inhibited by glutathionylation
-
-
?
glutathionylated isocitrate lyase + dithiothreitol
glutathione dithiothreitol disulfide + isocitrate lyase
-
-
-
?
reduced dithiothreitol + NADP+
oxidized dithiothreitol + NADPH + H+
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-
-
-
r
SdbA carrying a disulfide bond + superantigen SpeA with reduced L-cysteine residues
SdbA with reduced L-cysteine residues + superantigen SpeA carrying a disulfide bond
2 glutathione + COX2-disulfide
glutathione-disulfide + COX2-dithiol
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-
-
?
2 glutathione + COX2-disulfide
glutathione-disulfide + COX2-dithiol
-
-
-
?
2 glutathione + COX2-disulfide
glutathione-disulfide + COX2-dithiol
-
-
-
?
2 glutathione + insulin disulfide
glutathione disulfide + insulin
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-
-
?
2 glutathione + insulin disulfide
glutathione disulfide + insulin
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-
-
?
2 glutathione + pilin FimA-disulfide
glutathione-disulfide + pilin FimA-dithiol
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-
-
-
?
2 glutathione + pilin FimA-disulfide
glutathione-disulfide + pilin FimA-dithiol
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recombinant FimA expressed in Escherichia coli
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-
?
2 glutathione + pilin FimA-disulfide
glutathione-disulfide + pilin FimA-dithiol
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-
-
-
?
2 glutathione + pilin FimA-disulfide
glutathione-disulfide + pilin FimA-dithiol
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recombinant FimA expressed in Escherichia coli
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-
?
2 glutathione + protein AtlS-disulfide
glutathione-disulfide + protein AtlS-dithiol
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-
-
?
2 glutathione + protein AtlS-disulfide
glutathione-disulfide + protein AtlS-dithiol
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-
-
?
2 glutathione + protein AtlS-disulfide
glutathione-disulfide + protein AtlS-dithiol
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-
-
?
2 glutathione + protein AtlS-disulfide
glutathione-disulfide + protein AtlS-dithiol
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-
-
?
2 glutathione + protein AtlS-disulfide
glutathione-disulfide + protein AtlS-dithiol
-
-
-
?
2 glutathione + protein AtlS-disulfide
glutathione-disulfide + protein AtlS-dithiol
-
-
-
?
2 glutathione + protein AtlS-disulfide
glutathione-disulfide + protein AtlS-dithiol
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-
-
?
2 glutathione + protein-disulfide
glutathione-disulfide + protein-dithiol
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-
-
-
?
2 glutathione + protein-disulfide
glutathione-disulfide + protein-dithiol
-
-
-
-
?
2 glutathione + protein-disulfide
glutathione-disulfide + protein-dithiol
-
-
-
?
2 glutathione + protein-disulfide
glutathione-disulfide + protein-dithiol
-
-
-
?
2 glutathione + protein-disulfide
glutathione-disulfide + protein-dithiol
-
-
-
?
2 glutathione + protein-disulfide
glutathione-disulfide + protein-dithiol
-
-
-
?
2 glutathione + protein-disulfide
glutathione-disulfide + protein-dithiol
-
-
-
?
2 glutathione + protein-disulfide
glutathione-disulfide + protein-dithiol
-
-
-
?
2 glutathione + protein-disulfide
glutathione-disulfide + protein-dithiol
-
-
-
?
2 glutathione + protein-disulfide
glutathione-disulfide + protein-dithiol
-
-
-
?
2 glutathione + protein-disulfide
glutathione-disulfide + protein-dithiol
-
-
-
?
2 glutathione + protein-disulfide
glutathione-disulfide + protein-dithiol
-
-
-
?
2 glutathione + protein-disulfide
glutathione-disulfide + protein-dithiol
-
-
-
?
2 glutathione + protein-disulfide
glutathione-disulfide + protein-dithiol
-
-
-
?
2 glutathione + protein-disulfide
glutathione-disulfide + protein-dithiol
-
-
-
?
2 glutathione + protein-disulfide
glutathione-disulfide + protein-dithiol
-
-
-
?
2 glutathione + SCO1-disulfide
glutathione-disulfide + SCO1-dithiol
-
-
-
?
2 glutathione + SCO1-disulfide
glutathione-disulfide + SCO1-dithiol
-
-
-
?
2 glutathione + SCO1-disulfide
glutathione-disulfide + SCO1-dithiol
-
-
-
?
2,3-dimercaptopropanol + protein disulfide
2,3-dimercaptopropanol disulfide + protein-dithiol
-
-
-
-
?
2,3-dimercaptopropanol + protein disulfide
2,3-dimercaptopropanol disulfide + protein-dithiol
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-
-
-
?
2,3-dimercaptopropanol + protein disulfide
2,3-dimercaptopropanol disulfide + protein-dithiol
-
-
-
-
?
2,3-dimercaptopropanol + protein disulfide
2,3-dimercaptopropanol disulfide + protein-dithiol
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-
-
-
?
2-mercaptoethanol + protein disulfide
2-mercaptoethanol disulfide + protein-dithiol
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-
-
-
?
2-mercaptoethanol + protein disulfide
2-mercaptoethanol disulfide + protein-dithiol
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-
-
-
?
2-mercaptoethanol glutathione disulfide + glutathione
2-mercaptoethanol disulfide + glutathione disulfide
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-
-
?
2-mercaptoethanol glutathione disulfide + glutathione
2-mercaptoethanol disulfide + glutathione disulfide
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-
-
?
2-mercaptoethanol glutathione disulfide + glutathione
2-mercaptoethanol disulfide + glutathione disulfide
-
-
-
-
?
apocytochrome c + glutathione disulfide
apocytochrome c disulfide + 2 glutathione
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-
-
?
apocytochrome c + glutathione disulfide
apocytochrome c disulfide + 2 glutathione
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-
-
?
dithiothreitol + insulin disulfide
dithiothreitol disulfide + insulin
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-
-
?
dithiothreitol + insulin disulfide
dithiothreitol disulfide + insulin
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-
-
?
dithiothreitol + protein disulfide
?
-
protein disulfide: insulin or thioredoxin
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-
r
glutathionylated glyceraldehyde-3-phosphate dehydrogenase + glutathione
glutathione disulfide + glyceraldehyde-3-phosphate dehydrogenase
substrate is glutathionylated A4-GAPDH. A4-GAPDH activity is reversibly inhibited by glutathionylation
-
-
?
glutathionylated glyceraldehyde-3-phosphate dehydrogenase + glutathione
glutathione disulfide + glyceraldehyde-3-phosphate dehydrogenase
substrate is glutathionylated A4-GAPDH. A4-GAPDH activity is reversibly inhibited by glutathionylation
-
-
?
glutathionylated isocitrate lyase + glutathione
glutathione disulfide + isocitrate lyase
-
-
-
?
glutathionylated isocitrate lyase + glutathione
glutathione disulfide + isocitrate lyase
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substrate is glutathionylated isocitrate lyase of Chlamydomonas rheinhardtii
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-
?
GSH + insulin
GSSG + reduced insulin chain A and B
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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
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-
-
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?
GSH + insulin
GSSG + reduced insulin chain A and B
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proinsulin
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-
?