Information on EC 5.3.4.1 - Protein disulfide-isomerase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea

EC NUMBER
COMMENTARY hide
5.3.4.1
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RECOMMENDED NAME
GeneOntology No.
Protein disulfide-isomerase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
catalyses the rearrangement of -S-S- bonds in proteins
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
intramolecular oxidoreduction
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isomerization
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SYSTEMATIC NAME
IUBMB Comments
Protein disulfide-isomerase
Needs reducing agents or partly reduced enzyme; the reaction depends on sulfhydryl-disulfide interchange.
CAS REGISTRY NUMBER
COMMENTARY hide
37318-49-3
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
a tick cultured on rabbit hosts, constitutive gene
SwissProt
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
strain 2137a
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Manually annotated by BRENDA team
a marine snail
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Manually annotated by BRENDA team
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SwissProt
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
isoform Pdi-2
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
Homo sapiens ATCC 6706839
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Manually annotated by BRENDA team
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SwissProt
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
Leishmania major MHOM/TN/94/GLC94
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Manually annotated by BRENDA team
Mus musculus C57BL/6
PDIA3; C57BL/6 mice
UniProt
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
cultivar Kinmaze
UniProt
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
strain ANKA, isozyme PDI-8
SwissProt
Manually annotated by BRENDA team
strain ANKA, isozyme PDI-8
SwissProt
Manually annotated by BRENDA team
chabaudi
UniProt
Manually annotated by BRENDA team
strain H, isozyme PDI-8
SwissProt
Manually annotated by BRENDA team
strain H, isozyme PDI-8
SwissProt
Manually annotated by BRENDA team
strain Sal1, isozyme PDI-8
SwissProt
Manually annotated by BRENDA team
strain Sal1, isozyme PDI-8
SwissProt
Manually annotated by BRENDA team
isozyme PDI-8
SwissProt
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
strain trg1/TRG1
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Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
precursor; strain KP1
UniProt
Manually annotated by BRENDA team
Sea urchin
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Manually annotated by BRENDA team
NCIM 5127
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Manually annotated by BRENDA team
Streptomyces sp. NCIM 5127
NCIM 5127
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
Agp mutant
?
show the reaction diagram
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folding of Agp mutant, DsbC, mutant of Agp, an AppA homologue, containing the AppA nonconsecutive disulfide bond
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?
alkaline protease inhibitor
?
show the reaction diagram
alpha-globulin
?
show the reaction diagram
PDIL1-1 facilitates the oxidative folding of alpha-globulin
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?
carboxypeptidase Y
?
show the reaction diagram
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maturation of carboxypeptidase Y
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?
cholera toxin
?
show the reaction diagram
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reduced (but not oxidized) protein-disulfide isomerase displaces the cholera toxin A1 subunit from the holotoxin without unfolding the A1 subunit
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citrate synthase
stabilized citrate synthase
show the reaction diagram
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DsbG suppresses aggregation of luciferase at 43°C, enzyme has both PDI and chaperone activity
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?
conotoxins sTx3.1
?
show the reaction diagram
disulfide formation, macromolecular crowding has little effect on the protein disulfide isomerase-catalyzed oxidative folding and disulfide isomerization of conotoxin
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?
conotoxins tx3a
?
show the reaction diagram
disulfide formation, macromolecular crowding has little effect on the protein disulfide isomerase-catalyzed oxidative folding and disulfide isomerization of conotoxin
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-
?
creatine kinase
?
show the reaction diagram
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refolding of creatine kinase, creatine kinase substrate is denatured by 3 M guanidine-HCl, catalysis of creatine kinase refolding by PDI involves disulfide cross-link and dimer to tetramer switch, PDI suppresses aggregation of denatured inactive casein kinase
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?
degenerated RNase type III
?
show the reaction diagram
refolding of degenerated RNase type III, bovine pancreatic substrate, recombinant GST-tagged PDI, the coupled-assay method involves reduction of insulin in presence of DTT
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?
dehydroascorbate
ascorbate
show the reaction diagram
denatured D-glceraldehyde-3-phosphate dehydrogenase
refolded D-glceraldehyde-3-phosphate dehydrogenase
show the reaction diagram
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interaction of PDI with cyclophilin B increases its chaperone activity
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?
denatured D-glyceraldehyde-3-phosphate dehydrogenase
refolded D-glyceraldehyde-3-phosphate dehydrogenase
show the reaction diagram
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chaperone activity of PDI
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?
denatured eclosion hormone
active eclosion hormon
show the reaction diagram
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PDI acts as a chaperone and refolds the insect neuropeptide eclosion hormone
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?
denatured lysozyme
?
show the reaction diagram
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PDI catalyzes the formation, rearrangement, and breakage of disulfide bonds, oxidative refolding by PDI almost completely restores lysozyme activity, overview
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?
denatured rhodanese
?
show the reaction diagram
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PDI exhibits chaperone activity with rhodanese
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?
denatured rhodanese
refolded rhodanese
show the reaction diagram
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interaction of PDI with cyclophilin B increases its chaperone activity
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?
denatured RNase A
?
show the reaction diagram
recombinant CYO1 renatures RNase A
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?
denatured Rnase A
active Rnase A
show the reaction diagram
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?
denatured RNase A + GSH
renatured RNase A + GSSG
show the reaction diagram
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?
denatured-reduced lysozyme
?
show the reaction diagram
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oxidase activity of PDI
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?
E2A homodimer
E2A-basic helix-loop-helix protein heterodimer
show the reaction diagram
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PDI I and PDI II foster heterodimer formation between E proteins, i.e. basic-loop-helix proteins of the E2A gene products, by a redox mechanism
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?
envelope glycoprotein 120
envelope glycoprotein 120
show the reaction diagram
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i.e. human immunodeficiency virus gp120
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?
estrogen receptor alpha
?
show the reaction diagram
folded cholera toxin
unfolded cholera toxin
show the reaction diagram
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PDI binds in the reduced state to the A chain of cholera toxin, in the oxidized state it releases it, PDI may be involved in the retrograde protein transport into the cytosol
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?
glycoprotein 120
glycoprotein 120
show the reaction diagram
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PDI may play a role in HIV-1 infection by reducing HIV-1 envelope glycoprotein 120
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?
GSSG
GSH
show the reaction diagram
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disulfide reduction of GSSG, the disulfide reduction activity of both PDI-thioredoxin reductase and PDI-DTT is reduced
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?
insulin
?
show the reaction diagram
insulin + DTT
?
show the reaction diagram
bovine substrate, reductase activity with DTT
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?
Insulin-(SS) + dithiothreitol
Insulin-(SH)2 + oxidized dithiothreitol
show the reaction diagram
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Insulin-(SS) + GSH
Insulin-(SH)2 + GSSG
show the reaction diagram
kalata B1
?
show the reaction diagram
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and derivatives, PDI dramatically enhanced the correct oxidative folding of linear and cyclic kalata B1 at physiological pH, determination of folding intermediates
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?
lactate dehydrogenase
?
show the reaction diagram
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reactivation of self-aggregated denatured lactate dehydrogenase, guanidine HCl-denatured LDH, chaperone activity, both recombinant wild-type PDI and mutant abb'a' interact with self-aggregated lactate dehydrogenase enhancing LDH reactivation and reducing aggregation
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?
luciferase
stabilized luciferase
show the reaction diagram
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DsbG suppresses aggregation of luciferase at 43°C, enzyme has both PDI and chaperone activity
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?
lysozyme
?
show the reaction diagram
PDI exhibits both chaperone and antichaperone activities when catalyzing the refolding of reduced/denatured lysozyme in HEPES buffer, effect of macromolecular crowding on the PDI-catalyzed folding, overview
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?
lysozyme
aggregated lysozyme
show the reaction diagram
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PDI has antichaperone activity facilitating protein aggregation
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?
NRCSQGSCWN
?
show the reaction diagram
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disulfide-bond formation within the thiol substrate peptide NRCSQGSCWN, oxidation activity requires GSH/GSSG
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NRCSQGSCWN
NRCSQGSCWN
show the reaction diagram
oxidized insulin + dithiothreitol
reduced insulin
show the reaction diagram
gPDI-2, low activity with gPDI-3, no activity with gPDI-1
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?
oxidoreductase Ero1
?
show the reaction diagram
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disulfide bond formation in the oxidoreductase Ero1, endoplasmic reticular protein interacts with PDILT
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?
phytase
?
show the reaction diagram
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folding of phytase, i.e. AppA, substrate from Escherichia coli, contains 3 consecutive and 1 nonconsecutive disulfide bonds, DsbC, no activity of DsbC with an AppA mutant C155S/C430S lacking the nonconsecutive disulfide bond
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?
Pipe
?
show the reaction diagram
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processing and targeting of Pipe, Pipe is an essential Golgi transmembrane-O-sulfotransferase, protein disulfide isomerase-related chaperone Wind is required for processing and correct targeting of the substrate, mapping of multiple substrate binding sites in Pipe, one enzyme site in vicinity of an exposed cluster of tyrosine residues within the thioredoxin fold domain is essential for activity, a second enzyme site in the enzyme's D-domain is also necessary for processing activity, but competitive to the thioredoxin fold domain residue, overview
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?
Proteins
?
show the reaction diagram
Proteins
Proteins
show the reaction diagram
reduced bovine pancreatic trypsin inhibitor
oxidized bovine pancreatic trypsin inhibitor
show the reaction diagram
gPDI-2, no cativity with gPDI-1 and gPDI-3
-
?
reduced denatured RNase A + GSH
reduced renatured RNase A + GSSG
show the reaction diagram
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?
reduced ribonuclease
?
show the reaction diagram
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refolding of reduced ribonuclease in presence of glutathione, isomerase activity of PDI
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?
reduced RNase A
RNase A
show the reaction diagram
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?
refolding of RNase
?
show the reaction diagram
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renaturation of reduced RNase
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?
rhodanese
?
show the reaction diagram
riboflavin binding protein
?
show the reaction diagram
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protein disulfide isomerase and quiescin-sulfhydryl oxidase cooperate in vitro to generate native pairings in substrates ribonuclease A, with four disulfide bonds and 105 disulfide isomers of the fully oxidized protein, and avian riboflavin binding protein, with nine disulfide bonds and more than 34 million corresponding disulfide pairings. The isomerase is not a significant substrate of quiescin-sulfhydryl oxidase. Both reduced RNase and riboflavin binding protein can be efficiently refolded in an aerobic solution containing micromolar concentrations of reduced PDI and nanomolar levels of quiescin-sulfhydryl oxidase without any added oxidized PDI or glutathione redox buffer. In the absence of either quiescin-sulfhydryl oxidase or redox buffer, the fastest refolding of riboflavin binding protein is accomplished with excess reduced PDI and just enough oxidized PDI to generate nine disulfides in the protein client
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?
ribonuclease
?
show the reaction diagram
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refolding of ribonuclease, isomerase activity, renaturation of reduced ribonuclease, in presence of GSH and GSSG
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?
ribonuclease A
?
show the reaction diagram
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protein disulfide isomerase and quiescin-sulfhydryl oxidase cooperate in vitro to generate native pairings in ribonuclease A, with four disulfide bonds and 105 disulfide isomers of the fully oxidized protein, and avian riboflavin binding protein, with nine disulfide bonds and more than 34 million corresponding disulfide pairings. The isomerase is not a significant substrate of quiescin-sulfhydryl oxidase. Both reduced RNase and riboflavin binding protein can be efficiently refolded in an aerobic solution containing micromolar concentrations of reduced PDI and nanomolar levels of quiescin-sulfhydryl oxidase without any added oxidized PDI or glutathione redox buffer
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?
ricin
?
show the reaction diagram
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reductive activation of ricin and ricin A-chain immunotoxins, assay system involving thioredoxin reductase and NADPH, overview
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?
ricin A-chain immunotoxins
?
show the reaction diagram
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reductive activation of ricin and ricin A-chain immunotoxins, assay system involving thioredoxin reductase and NADPH, overview
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?
RNase
?
show the reaction diagram
RNase A
?
show the reaction diagram
RNase A + DTT
?
show the reaction diagram
RNase B
?
show the reaction diagram
the ability of the ERp57-calnexin complex to mediate folding of 3H-labeled RNase B is completely dependent on a functional interaction between ERp57 and calnexin, overview
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?
scrambled reoxidized lysozyme
?
show the reaction diagram
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isomerase activity of PDI
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?
scrambled RNAse
?
show the reaction diagram
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?
scrambled RNAse A
?
show the reaction diagram
scrambled RNase A
RNase A
show the reaction diagram
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?
TAMRAX3CX4CX2-CONH2
?
show the reaction diagram
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-
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?
thrombospondin-1 + alpha-thrombin + antithrombin III
thrombospondin-1-S-S-alpha-thrombin-S-S-antithrombin III
show the reaction diagram
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PDI catalyzes formation of disulfide linked complexes of thrombospondin
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?
tissue factor
?
show the reaction diagram
tyramine-S-S-poly(D-lysine)
tyramine-SH + HS-poly(D-lysine)
show the reaction diagram
-
-
-
?
unfolded acidic phospholipase A2
refolded acidic phospholipase A2
show the reaction diagram
-
PDI at a molar ratio to acidic phospholipase A2 of 0.1 increases the reactivation of reduced and denatured acidic phospholipase A2 from 4% to 15%
-
?
unfolded bovine pancreatic ribonuclease A + oxidized glutathione
refolded bovine pancreatic ribonuclease A + reduced glutathione
show the reaction diagram
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oxidative folding of RNase A, 12fold rate acceleration in the presence of PDI
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?
unfolded bovine pancreatic trypsin inhibitor
folded bovine pancreatic trypsin inhibitor
show the reaction diagram
-
-
?
unfolded bovine pancreatic trypsin inhibitor
refolded bovine pancreatic trypsin inhibitor
show the reaction diagram
unfolded bovine pancreatic trypsin inhibitor
refolded bovine pancreatic trypsin inhibitor + oxidized glutathione
show the reaction diagram
-
oxidative refolding of denatured bovine pancreatic trypsin inhibitor
-
?
unfolded disulfide-bonded protein
refolded disulfide-bonded protein
show the reaction diagram
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-
?
unfolded insulin
folded insulin
show the reaction diagram
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-
?
unfolded insulin
refolded insulin
show the reaction diagram
-
-
-
?
unfolded insulin + reduced glutathione
refolded insulin + oxidized glutathione
show the reaction diagram
-
-
-
?
unfolded insulin beta-chain
refolded insulin beta-chain
show the reaction diagram
-
-
-
?
unfolded lysozyme
refolded lysozyme
show the reaction diagram
-
oxidative refolding of reduced and denatured lysozyme in glutathione redox buffer
-
?
unfolded mitochondrial malate dehydrogenase
refolded mitochondrial malate dehydrogenase
show the reaction diagram
-
maximum refolding when the PDI concentration is 20fold higher than the malate dehydrogenase concentration
-
?
unfolded pro-carboxypeptidase Y
refolded pro-carboxypeptidase Y
show the reaction diagram
-
-
-
?
unfolded proinsulin
refolded proinsulin
show the reaction diagram
-
PDI acts both as a chaperone and as an isomerase during folding and disulfid bond formation of proinsulin, chaperone and isomerization activity is required at the beginning of proinsulin folding, the late refolding process only depends on the isomerase activity
-
?
unfolded RNase
refolded RNase
show the reaction diagram
unfolded RNase A
refolded RNase
show the reaction diagram
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-
-
?
unfolded RNase A
refolded RNase A
show the reaction diagram
unfolded RNase A + reduced glutathione
refolded RNase A + oxidized glutathione
show the reaction diagram
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-
-
?
unfolded rRNaSe
refolded rRNase
show the reaction diagram
-
refolding of reduced rRNaSe
-
?
unofolded bovine pancreatic ribonuclease A + oxidized dithiothreitol
refolded bovine pancreatic ribonuclease A + reduced dithiothreitol
show the reaction diagram
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oxidative folding of RNase A
-
?
vitronectin + thrombin + antithrombin
vitronectin-thrombin-antithrombin
show the reaction diagram
-
PDI catalyzes the formation of disulfide-linked complexes of vitronectin with thrombin-antithrombin
-
?
additional information
?
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