1.8.4.2: protein-disulfide reductase (glutathione)
This is an abbreviated version!
For detailed information about protein-disulfide reductase (glutathione), go to the full flat file.
Word Map on EC 1.8.4.2
-
1.8.4.2
-
tautomerase
-
glutaredoxins
-
insulin-degrading
-
d-dopachrome
-
5.3.4.1
-
dsbas
-
whib-like
-
thioredoxin-like
-
125i-insulin
-
disulphide-isomerase
-
medicine
- 1.8.4.2
-
tautomerase
- glutaredoxins
-
insulin-degrading
- d-dopachrome
-
5.3.4.1
- dsbas
-
whib-like
-
thioredoxin-like
- 125i-insulin
-
disulphide-isomerase
- medicine
Reaction
2 glutathione
+
Synonyms
BbdC, BdbD, C1orf31, CatA protein, ccdA associated thiol-disulfide oxidoreductase, COA6, DcbA, desulfothioredoxin, DIP1880, disulfide bond-forming thiol-disulfide oxidoreductase, disulphide interchange enzyme, DsbA, DsbA1, DsbA2, Dtrx, ERp57, GIT, glutathione-insulin transhydrogenase, glutathione-protein disulfide oxidoreductase, GRX1, GRX2, GRX3, GRX5, GRX6, GrxS12, GSH-dependent protein disulfide oxidoreductase, GSH-insulin transhydrogenase, HP_0231, insulin reductase, mcrophage migration inhibitory factor-2, MdbA, MdbACm, membrane-bound thiol-disulfide oxidoreductase, Mif-2, More, protein disulfide reductase (glutathione), protein disulfide transhydrogenase, protein-disulfide interchange enzyme, protein-disulfide isomerase/oxidoreductase, RCAP_rcc01743, reductase, protein disulfide (glutathione), ResA, SdbA, SGO_2006, SpyM18_2037, StoA, Streptococcus disulfide bond protein A, TDOR, thiol disulfide oxidoreductase, thiol-disulfide oxidoreductase, thiol-protein disulphide oxidoreductase, thiol:disulfide oxidoreductase, thiol:protein-disulfide oxidoreductase, WhiB1, WhiB1/Rv3219, YkuV, YMR244C-A
ECTree
1.8.4.2 protein-disulfide reductase (glutathione)Advanced search results
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results (Substrates Products
Substrates Products on EC 1.8.4.2 - protein-disulfide reductase (glutathione)
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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+
-
-
-
-
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
-
-
-
?
2 glutathione + COX2-disulfide
glutathione-disulfide + COX2-dithiol
-
-
-
?
2 glutathione + COX2-disulfide
glutathione-disulfide + COX2-dithiol
-
-
-
?
2 glutathione + insulin disulfide
glutathione disulfide + insulin
-
-
-
?
2 glutathione + insulin disulfide
glutathione disulfide + insulin
-
-
-
?
2 glutathione + pilin FimA-disulfide
glutathione-disulfide + pilin FimA-dithiol
-
-
-
-
?
2 glutathione + pilin FimA-disulfide
glutathione-disulfide + pilin FimA-dithiol
-
recombinant FimA expressed in Escherichia coli
-
-
?
2 glutathione + pilin FimA-disulfide
glutathione-disulfide + pilin FimA-dithiol
-
-
-
-
?
2 glutathione + pilin FimA-disulfide
glutathione-disulfide + pilin FimA-dithiol
-
recombinant FimA expressed in Escherichia coli
-
-
?
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
-
-
-
?
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
-
-
-
?
2 glutathione + protein AtlS-disulfide
glutathione-disulfide + protein AtlS-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 + 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
-
-
-
-
?
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
-
-
-
-
?
2-mercaptoethanol glutathione disulfide + glutathione
2-mercaptoethanol disulfide + glutathione disulfide
-
-
-
?
2-mercaptoethanol glutathione disulfide + glutathione
2-mercaptoethanol disulfide + glutathione disulfide
-
-
-
?
2-mercaptoethanol glutathione disulfide + glutathione
2-mercaptoethanol disulfide + glutathione disulfide
-
-
-
-
?
apocytochrome c + glutathione disulfide
apocytochrome c disulfide + 2 glutathione
-
-
-
?
apocytochrome c + glutathione disulfide
apocytochrome c disulfide + 2 glutathione
-
-
-
?
dithiothreitol + insulin disulfide
dithiothreitol disulfide + insulin
-
-
-
?
dithiothreitol + insulin disulfide
dithiothreitol disulfide + insulin
-
-
-
?
dithiothreitol + protein disulfide
?
-
protein disulfide: insulin or thioredoxin
-
-
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
-
substrate is glutathionylated isocitrate lyase of Chlamydomonas rheinhardtii
-
-
?
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
-
-
-
?
SdbA carrying a disulfide bond + superantigen SpeA with reduced L-cysteine residues
SdbA with reduced L-cysteine residues + superantigen SpeA carrying a disulfide bond
-
-
-
-
?
SdbA carrying a disulfide bond + superantigen SpeA with reduced L-cysteine residues
SdbA with reduced L-cysteine residues + superantigen SpeA carrying a disulfide bond
-
the superantigen SpeA contains 3 cysteine residues (Cys 87, Cys90, and Cys98) and has a disulfide bond formed between Cys87 and Cys98
-
-
?
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
?
-
GRX1is a typical CPYC-type GRX, which is reduced by GSH and exhibits disulfide reductase, dehydroascorbate reductase, and deglutathionylation activities
-
-
-
additional information
?
-
GRX1is a typical CPYC-type GRX, which is reduced by GSH and exhibits disulfide reductase, dehydroascorbate reductase, and deglutathionylation activities
-
-
-
additional information
?
-
no substrate: insulin disulfide, 2-mercaptoethanol glutathione disulfide
-
-
-
additional information
?
-
no substrate: insulin disulfide, 2-mercaptoethanol glutathione disulfide
-
-
-
additional information
?
-
-
MdbACm directly catalyzes disulfide bond formation in proteins in vitro
-
-
-
additional information
?
-
-
MdbACm directly catalyzes disulfide bond formation in proteins in vitro
-
-
-
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
?
-
COA6 interacts with COX2 and SCO proteins in vivo
-
-
-
additional information
?
-
at least in vitro SCO1 is the dominant interacting partner of COA6 compared to SCO2. H3 and C-terminal residues of COA6 are critical for its interaction with SCO1
-
-
-
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
?
-
COA6 interacts with COX2 and SCO proteins in vivo
-
-
-
additional information
?
-
yeast Coa6 interacts with both Sco1 and Sco2
-
-
-
additional information
?
-
COA6 interacts with COX2 and SCO proteins in vivo
-
-
-
additional information
?
-
yeast Coa6 interacts with both Sco1 and Sco2
-
-
-
additional information
?
-
oxidase activity of SdbA, thiol-disulfide oxidoreductase-associated lipoprotein SdbB, and CcdA2 is analyzed in the RNase A refolding assay. In this assay, denatured and reduced RNase A is incubated with the test protein, and the activity of refolded RNase A to cleave cCMP is monitored at A296. The disulfide exchange reactions between SdbA and SdbB and between SdbA and CcdA2 are performed
-
-
-
additional information
?
-
oxidase activity of SdbA, thiol-disulfide oxidoreductase-associated lipoprotein SdbB, and CcdA2 is analyzed in the RNase A refolding assay. In this assay, denatured and reduced RNase A is incubated with the test protein, and the activity of refolded RNase A to cleave cCMP is monitored at A296. The disulfide exchange reactions between SdbA and SdbB and between SdbA and CcdA2 are performed
-
-
-
additional information
?
-
oxidase activity of SdbA, thiol-disulfide oxidoreductase-associated lipoprotein SdbB, and CcdA2 is analyzed in the RNase A refolding assay. In this assay, denatured and reduced RNase A is incubated with the test protein, and the activity of refolded RNase A to cleave cCMP is monitored at A296. The disulfide exchange reactions between SdbA and SdbB and between SdbA and CcdA2 are performed
-
-
-
additional information
?
-
oxidase activity of SdbA, thiol-disulfide oxidoreductase-associated lipoprotein SdbB, and CcdA2 is analyzed in the RNase A refolding assay. In this assay, denatured and reduced RNase A is incubated with the test protein, and the activity of refolded RNase A to cleave cCMP is monitored at A296. The disulfide exchange reactions between SdbA and SdbB and between SdbA and CcdA2 are performed
-
-
-
additional information
?
-
oxidase activity of SdbA, thiol-disulfide oxidoreductase-associated lipoprotein SdbB, and CcdA2 is analyzed in the RNase A refolding assay. In this assay, denatured and reduced RNase A is incubated with the test protein, and the activity of refolded RNase A to cleave cCMP is monitored at A296. The disulfide exchange reactions between SdbA and SdbB and between SdbA and CcdA2 are performed
-
-
-
additional information
?
-
oxidase activity of SdbA, thiol-disulfide oxidoreductase-associated lipoprotein SdbB, and CcdA2 is analyzed in the RNase A refolding assay. In this assay, denatured and reduced RNase A is incubated with the test protein, and the activity of refolded RNase A to cleave cCMP is monitored at A296. The disulfide exchange reactions between SdbA and SdbB and between SdbA and CcdA2 are performed
-
-
-
additional information
?
-
oxidase activity of SdbA, thiol-disulfide oxidoreductase-associated lipoprotein SdbB, and CcdA2 is analyzed in the RNase A refolding assay. In this assay, denatured and reduced RNase A is incubated with the test protein, and the activity of refolded RNase A to cleave cCMP is monitored at A296. The disulfide exchange reactions between SdbA and SdbB and between SdbA and CcdA2 are performed
-
-
-
additional information
?
-
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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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