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Information on EC 5.3.4.1 - protein disulfide-isomerase
for references in articles please use BRENDA:EC5.3.4.1
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EC Tree 5 Isomerases
5.3 Intramolecular oxidoreductases
5.3.4 Transposing S-S bonds
5.3.4.1 protein disulfide-isomerase
IUBMB Comments
Needs reducing agents or partly reduced enzyme; the reaction depends on sulfhydryl-disulfide interchange.
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
- 5.3.4.1
- collagen
- laminin
- integrins
- endothelial
- actin
- fibrosis
-
adhesive
-
basement
- mesenchymal
- vessel
- fiber
- metastasis
- proteoglycans
- vitronectin
- fibrinogen
- matrices
- nephropathy
- albumin
- gelatin
-
interstitial
-
mesangial
- platelet
- monolayer
- cytoskeleton
- glomerular
- rgd
- vimentin
- e-cadherin
-
cell-cell
- adhesions
- zeta
- myofibroblasts
- willebrand
-
epithelial-mesenchymal
- factor-beta
- fak
- fibrin
- metalloproteinases
-
preterm
-
dish
-
biomaterials
- procollagens
- heparan
-
alpha-smooth
- dermal
- tgf-beta
- plasminogen
-
fibrillar
- drug development
-
heparin-binding
- synthesis
- thrombospondin
- medicine
- industry
- diagnostics
- pharmacology
- biotechnology
- analysis
showSynonyms
fibronectin, pdi, protein disulfide isomerase, erp57, pdia3, protein disulphide isomerase, cabp1, erp44, disulfide isomerase, erp72, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
5'-MD
-
-
-
-
58 kDa glucose regulated protein
-
-
-
-
58 kDa microsomal protein
-
-
-
-
AGR2
CaBP1
-
-
-
-
CaBP2
Cellular thyroid hormone binding protein
-
-
-
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CYO1
Disulfide interchange enzyme
-
-
-
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Disulfide isomerase ER-60
-
-
-
-
DsbA
DsbC
DsbD
-
-
-
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endoplasmic reticulum protein EUG1
-
-
-
-
Eps1p
ER58
-
-
-
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ERcalcistorin/protein-disulfide isomerase
ERp-72 homolog
-
-
-
-
ERp27
ERp28
Erp46
ERp57
ERP59
-
-
-
-
ERP60
-
-
-
-
ERp72
fibronectin
-
extracellular matrix protein fibronectin contains an intrinsic protein-disulfide isomerase activity
HIP-70
-
-
-
-
Iodothyronine 5'-monodeiodinase
-
-
-
-
P4HB
P5
P55
-
-
-
-
P58
-
-
-
-
pancreas-specific protein disulfide isomerase
PDI
PDI-A
PDI1
PDI2
PDIA1
PDIA3
PDIp
protein disulfide isomerase
protein disulfide isomerase 1
protein disulfide isomerase A1
protein disulfide isomerase A3
Protein disulfide isomerase P5
-
-
-
-
protein disulfide isomerase-2
Protein disulfide isomerase-related protein
-
-
-
-
protein disulfide oxidoreductase
Protein disulphide isomerase
Protein ERp-72
-
-
-
-
protein-disulfide isomerase
R-cognin
-
-
-
-
RB60
Rearrangease
-
-
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Reduced ribonuclease reactivating enzyme
-
-
-
-
Retina cognin
-
-
-
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S-S rearrangase
-
-
-
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ScsC
SSO0192
SsPDO
suppressor of copper sensitivity protein C
Thyroid hormone-binding protein
-
-
-
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Thyroxine deiodinase
-
-
-
-
additional information
CaBP2
-
-
-
-
DsbA
-
-
-
-
DsbC
-
-
-
-
ERp57
-
-
-
-
ERp72
-
-
-
-
PDI
-
-
-
-
PDI
-
-
PDI
-
-
649103, 649415, 649853, 650065, 650318, 650485, 650995, 651254, 651977, 652289, 652434, 652503, 652576, 652604, 653808, 660877, 661243, 662298, 662348, 678056, 679421, 680805, 681934, 701629, 701912, 702795, 702858, 703456, 704927, 705291, 706459, 714598, 714600, 715531, 715935, 727242, 727573, 728220, 728627, 728758, 728766, 746998, 747197, 747829, 747833, 747835, 747836, 770232, 770423, 771304, 772530, 773451
PDI
-
-
PDIp
-
-
-
-
protein disulfide isomerase
-
-
protein disulfide isomerase
-
protein disulfide isomerase
-
-
protein disulfide isomerase
-
-
protein disulfide isomerase
-
Protein disulphide isomerase
-
-
-
-
additional information
the enzyme belongs to the family of protein disulfide isomerases
additional information
-
PDI, DsbC, and DbsG belong to the thioredoxin superfamily
additional information
-
the enzyme is a member of the thioredoxin fold superfamily
additional information
-
protein disulfide-isomerase is identical with the beta-subunit of the prolyl 4-hydroxylase tetramer
additional information
-
PDI and other PDI family proteins are members of the thioredoxin superfamily
additional information
-
protein disulfide isomerase is identical to the beta-subunit of prolyl-4-hydroxylase
additional information
-
protein disulfide isomerase is identical to the beta-subunit of prolyl-4-hydroxylase
additional information
-
the enzyme is a member of the protein disulfide isomerase family of oxidoreductases
additional information
-
thyroid hormone binding protein is apparently identical to protein disulfide isomerase
additional information
the enzyme belongs to the protein disulfide isomerase family
additional information
the enzyme belongs to the protein disulfide isomerase family
additional information
the enzyme belongs to the protein disulfide isomerase family
additional information
the enzyme belongs to the protein disulfide isomerase family
additional information
PDIp is a member of the protein disulfide isomerase PDI family
additional information
the enzyme belongs to the protein disulfide isomerase family
additional information
the enzyme belongs to the family of protein disulfide isomerases
additional information
-
protein disulfide isomerase is identical to the beta-subunit of prolyl-4-hydroxylase
additional information
-
PDI, Eug1p, Mpd1p, Mpd2p, and Eps1p belong to the thioredoxin superfamily
additional information
-
the enzymes yPDI, Mpd1p, Mpd2p, and Eug1p belong to the yeast yPDI enzyme family
additional information
-
the enzymes yPDI, Mpd1p, Mpd2p, and Eug1p belong to the yeast yPDI enzyme family
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
catalyses the rearrangement of -S-S- bonds in proteins
disulfide formation and isomerization mechanism by domains a and a', during transfer of oxidizing or reducing equivalents to substrates, the CXXC active site cycles between its oxidized, disulfide and reduced, thiol states
-
catalyses the rearrangement of -S-S- bonds in proteins
disulfide formation and isomerization mechanism by domains a and a', during transfer of oxidizing or reducing equivalents to substrates, the CXXC active site cycles between its oxidized, disulfide and reduced, thiol states
-
catalyses the rearrangement of -S-S- bonds in proteins
structure of oxidized and reduced active site, the active site motif is -C-X-X-C-
-
catalyses the rearrangement of -S-S- bonds in proteins
the catalytic domain, residues 88-231, shows a thioredoxin fold with a helical insert, and an active site motif -C-X-X-C-, active site structure
-
catalyses the rearrangement of -S-S- bonds in proteins
active site structure
-
catalyses the rearrangement of -S-S- bonds in proteins
protein with nonconsecutive disulfie bonds require activity of DsbC for their full activity, the disulfide bonds are formed during the translocation across the cytoplasmic membrane
-
catalyses the rearrangement of -S-S- bonds in proteins
PDI introduces disulfides into proteins, oxidase activity, and provides quality control by catalyzing the rearrangement of incorrect disulfides, isomerase activity
-
catalyses the rearrangement of -S-S- bonds in proteins
active site location, structure, and redox state
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catalyses the rearrangement of -S-S- bonds in proteins
disulfide formation and isomerization mechanism by domains a and a', during transfer of oxidizing or reducing equivalents to substrates, the CXXC active site cycles between its oxidized, disulfide and reduced, thiol states
-
catalyses the rearrangement of -S-S- bonds in proteins
disulfide formation and isomerization mechanism by domains a and a', during transfer of oxidizing or reducing equivalents to substrates, the CXXC active site cycles between its oxidized, disulfide and reduced, thiol states
-
catalyses the rearrangement of -S-S- bonds in proteins
mechanism of enzyme-assisted folding of plant cyclotides
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catalyses the rearrangement of -S-S- bonds in proteins
substrate binding and catalytic mechanism
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catalyses the rearrangement of -S-S- bonds in proteins
substrate binding and catalytic mechanism
-
catalyses the rearrangement of -S-S- bonds in proteins
substrate binding and catalytic mechanism
catalyses the rearrangement of -S-S- bonds in proteins
substrate binding and catalytic mechanism
catalyses the rearrangement of -S-S- bonds in proteins
substrate binding and catalytic mechanism
-
catalyses the rearrangement of -S-S- bonds in proteins
the nucleophilic C36 thiol of the protein disulfide isomerase a domain is positioned over the N-terminus of the alpha2 helix. The H38 amide in the reduced enzyme exhibits a maximum rate of exchange at pH 5 due to efficient general base catalysis by the neutral imidazole of its own side chain and suppression of its exchange by the ionization of the C36 thiol. Ionization of this thiol and deprotonation of the H38 side chain suppress the C39 amide hydroxide-catalyzed exchange by a million-fold. The electrostatic potential within the active site stabilizes the two distinct transition states that lead to substrate reduction and oxidation
catalyses the rearrangement of -S-S- bonds in proteins
NCgl2478 reduces S-mycothiolated mixed disulfides and intramolecular disulfides via a monothiol-disulfide and a dithiol-disulfide exchange mechanism, respectively. NCgl2478 reduces mycothiolated mixed disulfides preferably via a monothiol mechanism. NCgl2478 reduces intramolecular disulfide bonds via a dithiol mechanism. NCgl2478 lacks oxidase activity
catalyses the rearrangement of -S-S- bonds in proteins
NCgl2478 reduces S-mycothiolated mixed disulfides and intramolecular disulfides via a monothiol-disulfide and a dithiol-disulfide exchange mechanism, respectively. NCgl2478 reduces mycothiolated mixed disulfides preferably via a monothiol mechanism. NCgl2478 reduces intramolecular disulfide bonds via a dithiol mechanism. NCgl2478 lacks oxidase activity
-
-
catalyses the rearrangement of -S-S- bonds in proteins
NCgl2478 reduces S-mycothiolated mixed disulfides and intramolecular disulfides via a monothiol-disulfide and a dithiol-disulfide exchange mechanism, respectively. NCgl2478 reduces mycothiolated mixed disulfides preferably via a monothiol mechanism. NCgl2478 reduces intramolecular disulfide bonds via a dithiol mechanism. NCgl2478 lacks oxidase activity
-
-
catalyses the rearrangement of -S-S- bonds in proteins
NCgl2478 reduces S-mycothiolated mixed disulfides and intramolecular disulfides via a monothiol-disulfide and a dithiol-disulfide exchange mechanism, respectively. NCgl2478 reduces mycothiolated mixed disulfides preferably via a monothiol mechanism. NCgl2478 reduces intramolecular disulfide bonds via a dithiol mechanism. NCgl2478 lacks oxidase activity
-
-
catalyses the rearrangement of -S-S- bonds in proteins
NCgl2478 reduces S-mycothiolated mixed disulfides and intramolecular disulfides via a monothiol-disulfide and a dithiol-disulfide exchange mechanism, respectively. NCgl2478 reduces mycothiolated mixed disulfides preferably via a monothiol mechanism. NCgl2478 reduces intramolecular disulfide bonds via a dithiol mechanism. NCgl2478 lacks oxidase activity
-
-
catalyses the rearrangement of -S-S- bonds in proteins
NCgl2478 reduces S-mycothiolated mixed disulfides and intramolecular disulfides via a monothiol-disulfide and a dithiol-disulfide exchange mechanism, respectively. NCgl2478 reduces mycothiolated mixed disulfides preferably via a monothiol mechanism. NCgl2478 reduces intramolecular disulfide bonds via a dithiol mechanism. NCgl2478 lacks oxidase activity
-
-
catalyses the rearrangement of -S-S- bonds in proteins
NCgl2478 reduces S-mycothiolated mixed disulfides and intramolecular disulfides via a monothiol-disulfide and a dithiol-disulfide exchange mechanism, respectively. NCgl2478 reduces mycothiolated mixed disulfides preferably via a monothiol mechanism. NCgl2478 reduces intramolecular disulfide bonds via a dithiol mechanism. NCgl2478 lacks oxidase activity
-
-
catalyses the rearrangement of -S-S- bonds in proteins
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
intramolecular oxidoreduction
-
-
-
-
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.
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CAS REGISTRY NUMBER
COMMENTARY
37318-49-3
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
Agp mutant
?
-
Substrates: folding of Agp mutant, DsbC, mutant of Agp, an AppA homologue, containing the AppA nonconsecutive disulfide bond
Products: -
Products: -
?
alpha-globulin
?
Substrates: PDIL1-1 facilitates the oxidative folding of alpha-globulin
Products: -
Products: -
?
apolipoprotein B100
?
-
Substrates: the enzyme assists in the oxidative folding of apolipoprotein B100
Products: -
Products: -
?
ApV1 phytase
?
Substrates: the enzyme is essential to circumvent folding complexity and enable the correct formation of the additional disulfide bond in ApV1
Products: -
Products: -
?
carboxypeptidase Y
?
-
Substrates: maturation of carboxypeptidase Y
Products: -
Products: -
?
cholera toxin
?
-
Substrates: reduced (but not oxidized) protein-disulfide isomerase displaces the cholera toxin A1 subunit from the holotoxin without unfolding the A1 subunit
Products: -
Products: -
?
citrate synthase
stabilized citrate synthase
-
Substrates: DsbG suppresses aggregation of luciferase at 43°C, enzyme has both PDI and chaperone activity
Products: -
Products: -
?
conotoxins sTx3.1
?
Substrates: disulfide formation, macromolecular crowding has little effect on the protein disulfide isomerase-catalyzed oxidative folding and disulfide isomerization of conotoxin
Products: -
Products: -
?
conotoxins tx3a
?
Substrates: disulfide formation, macromolecular crowding has little effect on the protein disulfide isomerase-catalyzed oxidative folding and disulfide isomerization of conotoxin
Products: -
Products: -
?
creatine kinase
?
-
Substrates: 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
Products: -
Products: -
?
degenerated RNase type III
?
Substrates: 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
Products: -
Products: -
?
denatured D-glceraldehyde-3-phosphate dehydrogenase
refolded D-glceraldehyde-3-phosphate dehydrogenase
-
Substrates: interaction of PDI with cyclophilin B increases its chaperone activity
Products: -
Products: -
?
denatured D-glyceraldehyde-3-phosphate dehydrogenase
refolded D-glyceraldehyde-3-phosphate dehydrogenase
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Substrates: chaperone activity of PDI
Products: -
Products: -
?
denatured eclosion hormone
active eclosion hormon
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Substrates: PDI acts as a chaperone and refolds the insect neuropeptide eclosion hormone
Products: -
Products: -
?
denatured lysozyme
?
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Substrates: PDI catalyzes the formation, rearrangement, and breakage of disulfide bonds, oxidative refolding by PDI almost completely restores lysozyme activity, overview
Products: -
Products: -
?
denatured rhodanese
?
-
Substrates: PDI exhibits chaperone activity with rhodanese
Products: -
Products: -
?
denatured RNase A
?
Substrates: recombinant CYO1 renatures RNase A
Products: -
Products: -
?
denatured RNase A + GSH
renatured RNase A + GSSG
-
Substrates: -
Products: -
Products: -
?
denatured-reduced lysozyme
?
-
Substrates: oxidase activity of PDI
Products: -
Products: -
?
dieosin glutathione disulfide
eosin glutathione sulfide
Substrates: -
Products: -
Products: -
?
E2A homodimer
E2A-basic helix-loop-helix protein heterodimer
-
Substrates: 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
Products: -
Products: -
?
envelope glycoprotein 120
envelope glycoprotein 120
-
Substrates: i.e. human immunodeficiency virus gp120
Products: -
Products: -
?
folded cholera toxin
unfolded cholera toxin
-
Substrates: 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
Products: -
Products: -
?
glycoprotein 120
glycoprotein 120
-
Substrates: PDI may play a role in HIV-1 infection by reducing HIV-1 envelope glycoprotein 120
Products: -
Products: -
?
GSSG
GSH
-
Substrates: disulfide reduction of GSSG, the disulfide reduction activity of both PDI-thioredoxin reductase and PDI-DTT is reduced
Products: -
Products: -
?
insulin + DTT
?
Substrates: bovine substrate, reductase activity with DTT
Products: -
Products: -
?
Insulin-(SS) + dithiothreitol
Insulin-(SH)2 + oxidized dithiothreitol
-
Substrates: -
Products: -
Products: -
?
integrin subunit alpha11
?
-
Substrates: the enzyme activates integrin subunit alpha11
Products: -
Products: -
?
integrin subunit beta1
?
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Substrates: the enzyme activates integrin subunit beta1
Products: -
Products: -
?
kalata B1
?
-
Substrates: and derivatives, PDI dramatically enhanced the correct oxidative folding of linear and cyclic kalata B1 at physiological pH, determination of folding intermediates
Products: -
Products: -
?
lactate dehydrogenase
?
-
Substrates: 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
Products: -
Products: -
?
luciferase
stabilized luciferase
-
Substrates: DsbG suppresses aggregation of luciferase at 43°C, enzyme has both PDI and chaperone activity
Products: -
Products: -
?
lysozyme
?
Substrates: 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
Products: -
Products: -
?
lysozyme
aggregated lysozyme
-
Substrates: PDI has antichaperone activity facilitating protein aggregation
Products: -
Products: -
?
NADP malate dehydrogenase
?
-
Substrates: substrate for isoform PDI-M only
Products: -
Products: -
?
NADPH thioredoxin reductase
?
-
Substrates: -
Products: -
Products: -
?
neuronal nitric oxide synthase
?
-
Substrates: the enzyme catalyzes neuronal nitric oxide synthase dimerization
Products: -
Products: -
?
oxidized insulin + dithiothreitol
reduced insulin
Substrates: gPDI-2, low activity with gPDI-3, no activity with gPDI-1
Products: -
Products: -
?
oxidoreductase Ero1
?
-
Substrates: disulfide bond formation in the oxidoreductase Ero1, endoplasmic reticular protein interacts with PDILT
Products: -
Products: -
?
phytase
?
-
Substrates: 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
Products: -
Products: -
?
Pipe
?
-
Substrates: 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
Products: -
Products: -
?
reduced bovine pancreatic trypsin inhibitor
oxidized bovine pancreatic trypsin inhibitor
Substrates: gPDI-2, no cativity with gPDI-1 and gPDI-3
Products: -
Products: -
?
reduced denatured RNase A + GSH
reduced renatured RNase A + GSSG
-
Substrates: -
Products: -
Products: -
?
reduced glutathione peroxidase 7
oxidized glutathione peroxidase 7
-
Substrates: -
Products: -
Products: -
?
reduced glutathione peroxidase 8
oxidized glutathione peroxidase 8
-
Substrates: -
Products: -
Products: -
?
reduced ribonuclease
?
-
Substrates: refolding of reduced ribonuclease in presence of glutathione, isomerase activity of PDI
Products: -
Products: -
?
reduced ribonuclease A
denatured ribonuclease A
Substrates: -
Products: -
Products: -
?
refolding of RNase
?
-
Substrates: renaturation of reduced RNase
Products: -
Products: -
?
riboflavin binding protein
?
-
Substrates: 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
Products: -
Products: -
?
ribonuclease A
?
-
Substrates: 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
Products: -
Products: -
?
ricin
?
-
Substrates: reductive activation of ricin and ricin A-chain immunotoxins, assay system involving thioredoxin reductase and NADPH, overview
Products: -
Products: -
?
ricin A-chain immunotoxins
?
-
Substrates: reductive activation of ricin and ricin A-chain immunotoxins, assay system involving thioredoxin reductase and NADPH, overview
Products: -
Products: -
?
RNase B
?
Substrates: 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
Products: -
Products: -
?
scrambled reoxidized lysozyme
?
-
Substrates: isomerase activity of PDI
Products: -
Products: -
?
scrambled RNAse
?
Substrates: -
Products: -
Products: -
?
thrombospondin-1 + alpha-thrombin + antithrombin III
thrombospondin-1-S-S-alpha-thrombin-S-S-antithrombin III
-
Substrates: PDI catalyzes formation of disulfide linked complexes of thrombospondin
Products: -
Products: -
?
thyroid hormone receptor alpha
?
-
Substrates: the enzyme modulates thyroid hormone receptor by its thiol reductase/isomerase activity
Products: -
Products: -
?
thyroid hormone receptor beta
?
-
Substrates: the enzyme modulates thyroid hormone receptor by its thiol reductase/isomerase activity
Products: -
Products: -
?
tyramine-S-S-poly(D-lysine)
tyramine-SH + HS-poly(D-lysine)
-
Substrates: -
Products: -
Products: -
?
unfolded acidic phospholipase A2
refolded acidic phospholipase A2
-
Substrates: 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%
Products: -
Products: -
?
unfolded bovine pancreatic ribonuclease A + oxidized glutathione
refolded bovine pancreatic ribonuclease A + reduced glutathione
-
Substrates: oxidative folding of RNase A, 12fold rate acceleration in the presence of PDI
Products: -
Products: -
?
unfolded bovine pancreatic trypsin inhibitor
folded bovine pancreatic trypsin inhibitor
Substrates: -
Products: -
Products: -
?
unfolded bovine pancreatic trypsin inhibitor
refolded bovine pancreatic trypsin inhibitor + oxidized glutathione
-
Substrates: oxidative refolding of denatured bovine pancreatic trypsin inhibitor
Products: -
Products: -
?
unfolded disulfide-bonded protein
refolded disulfide-bonded protein
-
Substrates: -
Products: -
Products: -
?
unfolded insulin
folded insulin
Substrates: -
Products: -
Products: -
?
unfolded insulin + reduced glutathione
refolded insulin + oxidized glutathione
-
Substrates: -
Products: -
Products: -
?
unfolded insulin beta-chain
refolded insulin beta-chain
-
Substrates: -
Products: -
Products: -
?
unfolded lysozyme
refolded lysozyme
-
Substrates: oxidative refolding of reduced and denatured lysozyme in glutathione redox buffer
Products: -
Products: -
?
unfolded mitochondrial malate dehydrogenase
refolded mitochondrial malate dehydrogenase
-
Substrates: maximum refolding when the PDI concentration is 20fold higher than the malate dehydrogenase concentration
Products: -
Products: -
?
unfolded pro-carboxypeptidase Y
refolded pro-carboxypeptidase Y
-
Substrates: -
Products: -
Products: -
?
unfolded proinsulin
refolded proinsulin
-
Substrates: 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
Products: -
Products: -
?
unfolded RNase A + reduced glutathione
refolded RNase A + oxidized glutathione
-
Substrates: -
Products: -
Products: -
?
unfolded rRNaSe
refolded rRNase
-
Substrates: refolding of reduced rRNaSe
Products: -
Products: -
?
unofolded bovine pancreatic ribonuclease A + oxidized dithiothreitol
refolded bovine pancreatic ribonuclease A + reduced dithiothreitol
-
Substrates: oxidative folding of RNase A
Products: -
Products: -
?
vitronectin + thrombin + antithrombin
vitronectin-thrombin-antithrombin
-
Substrates: PDI catalyzes the formation of disulfide-linked complexes of vitronectin with thrombin-antithrombin
Products: -
Products: -
?
alkaline protease inhibitor
?
-
Substrates: folding and rearrangement of alkaline protease inhibitor
Products: -
Products: -
?
alkaline protease inhibitor
?
-
Substrates: folding and rearrangement of alkaline protease inhibitor, PDI contains 2 cysteine residues in the active site which are involved in rearrangement of disulfide bonds by function in thiol/disulfide exchange
Products: -
Products: -
?
alkaline protease inhibitor
?
-
Substrates: folding and rearrangement of alkaline protease inhibitor
Products: -
Products: -
?
alkaline protease inhibitor
?
-
Substrates: folding and rearrangement of alkaline protease inhibitor, PDI contains 2 cysteine residues in the active site which are involved in rearrangement of disulfide bonds by function in thiol/disulfide exchange
Products: -
Products: -
?
denatured lysozyme
native lysozyme
Substrates: -
Products: -
Products: -
?
denatured rhodanese
refolded rhodanese
-
Substrates: interaction of PDI with cyclophilin B increases its chaperone activity
Products: -
Products: -
?
estrogen receptor alpha
?
-
Substrates: i.e. ERalpha, PDI plays a critical role in estrogen responsiveness by functioning as a molecular chaperone and assisting the receptor in differentially regulating target gene expression, PDI alters estrogen-mediated transactivation, overview, PDI enhances ERalpha-DNA interactions in presence of an oxidizing agent
Products: -
Products: -
?
estrogen receptor alpha
?
-
Substrates: i.e. ERalpha, PDI colocalizes with ERalpha in MCF-7 nuclei, alters ERalpha conformation, enhances the ERalpha-estrogen response element interaction in the absence and presence of an oxidizing agent, influences the ability of ERalpha to mediate changes in gene expression, and associates with promoter regions of two endogenous estrogen-responsive genes, overview
Products: -
Products: -
?
insulin
?
Substrates: recombinant CYO1 accelerates disulfide bond reduction in the model substrate insulin
Products: -
Products: -
?
insulin
?
-
Substrates: reduction of insulin, turbidometry assay including glutathione reduction and alkylation of 4-acetamido-4'-maleimidyl-stilbene-2,2'-disulfonate, as well as treatment with DTT and iodoacetamide or iodoacetate for subsequent insulin reduction, isomerase activity, overview
Products: -
Products: -
?
insulin
?
-
Substrates: PDI exhibits reductase activity with insulin
Products: -
Products: -
?
insulin
?
-
Substrates: bovine substrate, reduction of disulfide bonds
Products: -
Products: -
?
insulin
?
-
Substrates: disulfide-bond reduction in substrate insulin, reduction activity by Holmgren's turbimetric method
Products: -
Products: -
?
insulin
?
Substrates: reduction of insulin disulfide bonds
Products: -
Products: -
?
insulin
?
Substrates: reduction of insulin disulfide bonds
Products: -
Products: -
?
Insulin-(SS) + GSH
Insulin-(SH)2 + GSSG
-
Substrates: -
Products: -
Products: -
?
Insulin-(SS) + GSH
Insulin-(SH)2 + GSSG
-
Substrates: -
Products: -
Products: -
?
Insulin-(SS) + GSH
Insulin-(SH)2 + GSSG
-
Substrates: protein disulfide isomerase supports proinsulin folding as chaperone and isomerase
Products: -
Products: -
?
Insulin-(SS) + GSH
Insulin-(SH)2 + GSSG
-
Substrates: -
Products: -
Products: -
?
mycothiol-coupled hydroxyethyl disulfide
mycothiol + hydroxyethyl disulfide
Substrates: a mixed disulfide
Products: -
Products: -
?
mycothiol-coupled hydroxyethyl disulfide
mycothiol + hydroxyethyl disulfide
Substrates: a mixed disulfide
Products: -
Products: -
?
mycothiol-coupled hydroxyethyl disulfide
mycothiol + hydroxyethyl disulfide
Substrates: a mixed disulfide
Products: -
Products: -
?
mycothiol-coupled hydroxyethyl disulfide
mycothiol + hydroxyethyl disulfide
Substrates: a mixed disulfide
Products: -
Products: -
?
mycothiol-coupled hydroxyethyl disulfide
mycothiol + hydroxyethyl disulfide
Substrates: a mixed disulfide
Products: -
Products: -
?
mycothiol-coupled hydroxyethyl disulfide
mycothiol + hydroxyethyl disulfide
Substrates: a mixed disulfide
Products: -
Products: -
?
mycothiol-coupled hydroxyethyl disulfide
mycothiol + hydroxyethyl disulfide
Substrates: a mixed disulfide
Products: -
Products: -
?
NRCSQGSCWN
?
-
Substrates: disulfide-bond formation within the thiol substrate peptide NRCSQGSCWN, oxidation activity requires GSH/GSSG
Products: -
Products: -
?
Proteins
?
-
Substrates: facilitates the formation of the correct disulfide bonds within newly synthesized polypeptides
Products: -
Products: -
?
Proteins
?
-
Substrates: catalyzes disulfide cleavage in membrane-bound diphtheria toxin or the membrane-bound conjugate, iodotyramine conjugated with poly(D-Lys) via a 3,3'-dithiobis(propionic acid) spacer
Products: -
Products: -
?
Proteins
?
-
Substrates: involved in cotranslational disulfide bond formation
Products: -
Products: -
?
Proteins
?
-
Substrates: native, reduced or with wrong disulfide bonds
Products: -
Products: -
?
Proteins
?
-
Substrates: implicated in the biosynthesis of secretory proteins
Products: -
Products: -
?
Proteins
?
-
Substrates: enzyme may play a physiological role in the catalysis of S-S-bond formation in prolactin
Products: -
Products: -
?
Proteins
?
-
Substrates: may play a role in the formation of disulfide bonds in extracellular and periplasmic proteins
Products: -
Products: -
?
Proteins
?
-
Substrates: native, reduced or with wrong disulfide bonds
Products: -
Products: -
?
Proteins
?
-
Substrates: facilitates the formation of disulfides during the folding and processing of membrane and secretory proteins
Products: -
Products: -
?
Proteins
?
-
Substrates: enzyme may be involved in the formation of intra-chain and inter-chain disulfide bonds in procollagen
Products: -
Products: -
?
Proteins
?
-
Substrates: may play a role in retaining prolyl 4-hydroxylase in its native conformation
Products: -
Products: -
?
Proteins
?
-
Substrates: enzyme may be involved in the formation of intra-chain and inter-chain disulfide bonds in procollagen
Products: -
Products: -
?
Proteins
?
-
Substrates: platelet enzyme may play a role in the various haemostatic and tissue remodelling processes in which platelets are involved
Products: -
Products: -
?
Proteins
?
-
Substrates: native, reduced or with wrong disulfide bonds
Products: -
Products: -
?
Proteins
?
-
Substrates: implicated in the biosynthesis of secretory proteins
Products: -
Products: -
?
Proteins
?
-
Substrates: may play a role in the formation of disulfide bonds in extracellular and periplasmic proteins
Products: -
Products: -
?
Proteins
?
-
Substrates: native, reduced or with wrong disulfide bonds
Products: -
Products: -
?
Proteins
?
-
Substrates: when present in large stoichiometric excess relative to an unfolded protein substrate, the enzyme can exhibit chaperone activity, inhibiting aggregation and increasing the recovery of native protein
Products: -
Products: -
?
Proteins
?
-
Substrates: may play a role in the formation of disulfide bonds in extracellular and periplasmic proteins
Products: -
Products: -
?
Proteins
?
-
Substrates: native, reduced or with wrong disulfide bonds
Products: -
Products: -
?
Proteins
?
-
Substrates: enzyme may be involved in the formation of intra-chain and inter-chain disulfide bonds in procollagen
Products: -
Products: -
?
Proteins
?
-
Substrates: may play a role in the formation of disulfide bonds in extracellular and periplasmic proteins
Products: -
Products: -
?
Proteins
?
-
Substrates: native, reduced or with wrong disulfide bonds
Products: -
Products: -
?
Proteins
?
-
Substrates: may play a role in the formation of disulfide bonds in extracellular and periplasmic proteins
Products: -
Products: -
?
Proteins
?
-
Substrates: native, reduced or with wrong disulfide bonds
Products: -
Products: -
?
Proteins
?
-
Substrates: may play a role in the formation of disulfide bonds in extracellular and periplasmic proteins
Products: -
Products: -
?
Proteins
?
-
Substrates: native, reduced or with wrong disulfide bonds
Products: -
Products: -
?
Proteins
?
-
Substrates: proposed physiological role as catalyst of formation of native disulfide bonds in nascent and newly synthesized secretory proteins
Products: -
Products: -
?
Proteins
?
-
Substrates: involved in cotranslational disulfide bond formation
Products: -
Products: -
?
Proteins
?
-
Substrates: native, reduced or with wrong disulfide bonds
Products: -
Products: -
?
Proteins
?
-
Substrates: implicated in the biosynthesis of secretory proteins
Products: -
Products: -
?
Proteins
?
-
Substrates: may play a role in the formation of disulfide bonds in extracellular and periplasmic proteins
Products: -
Products: -
?
Proteins
?
-
Substrates: native, reduced or with wrong disulfide bonds
Products: -
Products: -
?
Proteins
?
-
Substrates: involved in the assembly of wheat storage proteins within the endoplasmic reticulum
Products: -
Products: -
?
Proteins
?
-
Substrates: plays a role in the formation of disulfide bonds during biosynthesis of wheat storage proteins
Products: -
Products: -
?
Proteins
?
-
Substrates: native, reduced or with wrong disulfide bonds
Products: -
Products: -
?
Proteins
Proteins
-
Substrates: native, reduced or with wrong disulfide bonds
Products: with correct disulfide bonds
Products: with correct disulfide bonds
?
Proteins
Proteins
-
Substrates: native, reduced or with wrong disulfide bonds
Products: with correct disulfide bonds
Products: with correct disulfide bonds
?
Proteins
Proteins
-
3034, 3042, 3046, 3048, 3051, 3052, 3054, 3061, 3066, 3069, 3077, 3080, 3081, 3083, 3089, 3090, 3093
Substrates: native, reduced or with wrong disulfide bonds
Products: with correct disulfide bonds
Products: with correct disulfide bonds
?
Proteins
Proteins
-
Substrates: cosubstrate: DTT, 2-mercaptoethanol, GSH, or Cys
Products: with correct disulfide bonds
Products: with correct disulfide bonds
?
Proteins
Proteins
-
Substrates: cosubstrate dithiothreitol can be replaced by GSH, cysteamine, 2-mercaptoethanol, thioglycollic acid or L-Cys, but at significantly higher concentrations
Products: with correct disulfide bonds
Products: with correct disulfide bonds
?
Proteins
Proteins
-
Substrates: incorrectly disulfide-linked ribonuclease
Products: with correct disulfide bonds
Products: with correct disulfide bonds
?
Proteins
Proteins
-
Substrates: native, reduced or with wrong disulfide bonds
Products: with correct disulfide bonds
Products: with correct disulfide bonds
?
Proteins
Proteins
-
Substrates: native, reduced or with wrong disulfide bonds
Products: with correct disulfide bonds
Products: with correct disulfide bonds
?
Proteins
Proteins
-
Substrates: native, reduced or with wrong disulfide bonds
Products: with correct disulfide bonds
Products: with correct disulfide bonds
?
Proteins
Proteins
-
Substrates: native, reduced or with wrong disulfide bonds
Products: with correct disulfide bonds
Products: with correct disulfide bonds
?
Proteins
Proteins
-
Substrates: refolding and activation of human carbonic anhydrase IV, GSSG promotes the activation
Products: with correct disulfide bonds
Products: with correct disulfide bonds
?
Proteins
Proteins
-
Substrates: native, reduced or with wrong disulfide bonds
Products: with correct disulfide bonds
Products: with correct disulfide bonds
?
Proteins
Proteins
-
Substrates: native, reduced or with wrong disulfide bonds
Products: with correct disulfide bonds
Products: with correct disulfide bonds
?
Proteins
Proteins
-
Substrates: incorrectly disulfide-linked bovine pancreatic ribonuclease
Products: with correct disulfide bonds
Products: with correct disulfide bonds
?
Proteins
Proteins
-
Substrates: native, reduced or with wrong disulfide bonds
Products: with correct disulfide bonds
Products: with correct disulfide bonds
?
Proteins
Proteins
-
Substrates: incorrectly disulfide-linked Bowman Birk soybean trypsin
Products: with correct disulfide bonds
Products: with correct disulfide bonds
?
Proteins
Proteins
-
Substrates: incorrectly disulfide-linked lysozyme
Products: with correct disulfide bonds
Products: with correct disulfide bonds
?
Proteins
Proteins
-
Substrates: incorrectly disulfide-linked RNAse
Products: with correct disulfide bonds
Products: with correct disulfide bonds
?
Proteins
Proteins
-
Substrates: refolding of scrambled ribonuclease
Products: with correct disulfide bonds
Products: with correct disulfide bonds
?
Proteins
Proteins
-
Substrates: native, reduced or with wrong disulfide bonds
Products: with correct disulfide bonds
Products: with correct disulfide bonds
?
Proteins
Proteins
-
Substrates: native, reduced or with wrong disulfide bonds
Products: with correct disulfide bonds
Products: with correct disulfide bonds
?
Proteins
Proteins
-
Substrates: native, reduced or with wrong disulfide bonds
Products: with correct disulfide bonds
Products: with correct disulfide bonds
?
Proteins
Proteins
-
Substrates: native, reduced or with wrong disulfide bonds
Products: with correct disulfide bonds
Products: with correct disulfide bonds
?
Proteins
Proteins
-
Substrates: native, reduced or with wrong disulfide bonds
Products: with correct disulfide bonds
Products: with correct disulfide bonds
?
Proteins
Proteins
-
Substrates: refolding of scrambled ribonuclease
Products: with correct disulfide bonds
Products: with correct disulfide bonds
?
Proteins
Proteins
-
Substrates: native, reduced or with wrong disulfide bonds
Products: with correct disulfide bonds
Products: with correct disulfide bonds
?
Proteins
Proteins
-
Substrates: refolding of scrambled lysosyme
Products: with correct disulfide bonds
Products: with correct disulfide bonds
?
Proteins
Proteins
-
Substrates: native, reduced or with wrong disulfide bonds
Products: with correct disulfide bonds
Products: with correct disulfide bonds
?
Proteins
Proteins
-
Substrates: native, reduced or with wrong disulfide bonds
Products: with correct disulfide bonds
Products: with correct disulfide bonds
?
Proteins
Proteins
-
Substrates: native, reduced or with wrong disulfide bonds
Products: with correct disulfide bonds
Products: with correct disulfide bonds
?
Proteins
Proteins
-
Substrates: native, reduced or with wrong disulfide bonds
Products: with correct disulfide bonds
Products: with correct disulfide bonds
?
Proteins
Proteins
-
Substrates: native, reduced or with wrong disulfide bonds
Products: with correct disulfide bonds
Products: with correct disulfide bonds
?
Proteins
Proteins
-
3034, 3038, 3039, 3041, 3043, 3047, 3049, 3054, 3059, 3066, 3067, 3075, 3077, 3079, 3080, 3087, 3093, 3094, 3095
Substrates: native, reduced or with wrong disulfide bonds
Products: with correct disulfide bonds
Products: with correct disulfide bonds
?
Proteins
Proteins
-
Substrates: eduction of insulin and oxidative folding of ribonuclease A
Products: with correct disulfide bonds
Products: with correct disulfide bonds
?
Proteins
Proteins
-
Substrates: incorrectly disulfide-linked RNAse
Products: with correct disulfide bonds
Products: with correct disulfide bonds
?
Proteins
Proteins
-
Substrates: native, reduced or with wrong disulfide bonds
Products: with correct disulfide bonds
Products: with correct disulfide bonds
?
Proteins
Proteins
-
Substrates: refolding of scrambled ribonuclease
Products: with correct disulfide bonds
Products: with correct disulfide bonds
?
Proteins
Proteins
-
Substrates: native, reduced or with wrong disulfide bonds
Products: with correct disulfide bonds
Products: with correct disulfide bonds
?
Proteins
Proteins
-
Substrates: cosubstrate: DTT, 2-mercaptoethanol, GSH, or Cys
Products: with correct disulfide bonds
Products: with correct disulfide bonds
?
Proteins
Proteins
-
Substrates: native, reduced or with wrong disulfide bonds
Products: with correct disulfide bonds
Products: with correct disulfide bonds
?
Proteins
Proteins
-
Substrates: native, reduced or with wrong disulfide bonds
Products: with correct disulfide bonds
Products: with correct disulfide bonds
?
Proteins
Proteins
-
Substrates: native, reduced or with wrong disulfide bonds
Products: with correct disulfide bonds
Products: with correct disulfide bonds
?
rhodanese
?
-
Substrates: the protein substrate is devoid of disulfide bonds, chaperone activity
Products: -
Products: -
?
rhodanese
?
-
Substrates: prevention of rhodanese degeneration, chaperone activity
Products: -
Products: -
?
rhodanese
?
-
Substrates: prevention of rhodanese degeneration, chaperone activity
Products: -
Products: -
?
ribonuclease
?
-
Substrates: refolding of ribonuclease, isomerase activity, renaturation of reduced ribonuclease, in presence of GSH and GSSG
Products: -
Products: -
?
RNase
?
-
Substrates: refolding of RNase, renaturation of reduced bovine pancreatic RNase
Products: -
Products: -
?
RNase
?
-
Substrates: the enzyme is able to renature the denatured and reduced RNase
Products: -
Products: -
?
RNase
?
-
Substrates: refolding of RNase, renaturation of reduced and of scrambled RNase with almost equal activity
Products: -
Products: -
?
RNase A
?
-
Substrates: reconstitution of the Ero1-Lalpha/protein disulfide isomerase oxidative folding system in vitro. The a' domain of protein disulfide isomerase is much more active than the a domain in Ero1-Lalpha-mediated folding. The minimal element for binding to Ero1-Lalpha are core element b, linker x and the a domain
Products: -
Products: -
?
RNase A
?
Substrates: PDI catalyzes the refolding of denatured bovine RNase A. The protein disulfide isomerase exhibits a saturable, substrate binding site. NMR structural analysis of peptide binding pocket of b and b' domains, overview
Products: -
Products: -
?
RNase A
?
-
Substrates: PDI exhibits isomerase activity with RNase A
Products: -
Products: -
?
RNase A
?
-
Substrates: reduced and denatured substrate, oxidase/isomerase activity on the refolding of the substrate
Products: -
Products: -
?
RNase A
?
-
Substrates: reduced and denatured substrate from bovine pancreas
Products: -
Products: -
?
RNase A + DTT
?
Substrates: the enzyme contains a WCGHCQ active site
Products: -
Products: -
?
RNase A + DTT
?
Substrates: the enzyme contains a WCGHCK active site
Products: -
Products: -
?
scrambled RNAse A
?
Substrates: the enzyme catalyzes intramolecular disulfide interchange in scrambled RNase A and restores both native disulfide pairing and ribonuclease activity
Products: -
Products: -
?
scrambled RNAse A
?
Substrates: the enzyme catalyzes intramolecular disulfide interchange in scrambled RNase A and restores both native disulfide pairing and ribonuclease activity
Products: -
Products: -
?
tissue factor
?
-
Substrates: PDI switches tissue factor from coagulation to signaling by targeting the allosteric Cys186-Cys209 disulfide, the tissue factor coagulant function is enhanced by protein-disulfide isomerase independent of oxidoreductase activity, the chaperone activity is sufficient, PDI enhances factor VIIa-dependent substrate factor X activation 5-10fold in the presence of wild-type, oxidized soluble TF but not TF mutants that contain an unpaired Cys186 or Cys209, PDI has no effect on fully active TF on either negatively charged phospholipids or in activating detergent, indicating that PDI selectively acts upon cryptic TF to facilitate ternary complex formation and macromolecular substrate turnover, overview
Products: -
Products: -
?
tissue factor
?
-
Substrates: recombinant wild-type and mutant TFs expressed in Escherichia coli, PDI is a functional oxidoreductase and exhibits both protein disulfide isomerase and chaperone activity, PDI facilitates ternary complex formation and substrate Turnover, overview
Products: -
Products: -
?
unfolded bovine pancreatic trypsin inhibitor
refolded bovine pancreatic trypsin inhibitor
-
Substrates: -
Products: -
Products: -
?
unfolded bovine pancreatic trypsin inhibitor
refolded bovine pancreatic trypsin inhibitor
-
Substrates: -
Products: -
Products: -
?
unfolded bovine pancreatic trypsin inhibitor
refolded bovine pancreatic trypsin inhibitor
-
Substrates: -
Products: -
Products: -
?
unfolded RNase
refolded RNase
Substrates: -
Products: -
Products: -
?
unfolded RNase
refolded RNase
-
Substrates: -
Products: -
Products: -
?
unfolded RNase
refolded RNase
-
Substrates: oxidative folding of RNase
Products: -
Products: -
?
unfolded RNase
refolded RNase
Substrates: PDI is a multifunctional enzyme that acts as a subunit in prolyl 4-hydroxylases and the microsomal triglyceride transfer protein, and as a chaperone that binds various peptides and assists their folding
Products: -
Products: -
?
unfolded RNase A
refolded RNase A
-
Substrates: all five consecutive PDI domains, a-b-b'-a'-c are necessary for PDI's disulfide isomerase and chaperone activity
Products: -
Products: -
?
unfolded RNase A
refolded RNase A
-
Substrates: PDI binds to DNA and may be involved in DNA-nuclear matrix anchoring
Products: -
Products: -
?
unfolded RNase A
refolded RNase A
-
Substrates: PDI catalyzes disulfide isomerization of misfolded, i.e. scrambled RNaseA into native RNase A
Products: -
Products: -
?
unfolded RNase A
refolded RNase A
-
Substrates: PDI functions in a plasma environment
Products: -
Products: -
?
unfolded RNase A
refolded RNase A
-
Substrates: reduced and denatured bovine pancreatic RNase A, glutathione redox buffer, PDI catalyzes the entire RNase A folding by enhancing the formation and reduction of mixed disulfides with glutathione and the formation of intramolecular disulfides
Products: -
Products: -
?
unfolded RNase A
refolded RNase A
-
Substrates: tyrosine and tryptophane residues in peptides are the recognition motifs for their binding
Products: -
Products: -
?
additional information
?
-
Substrates: PDI has an important function in the correct folding of nascent polypeptides, which is a crucial step in the mechanism which delivers tick proteins to the secretion pathway important for blood feeding
Products: -
Products: -
?
additional information
?
-
-
Substrates: PDI has an important function in the correct folding of nascent polypeptides, which is a crucial step in the mechanism which delivers tick proteins to the secretion pathway important for blood feeding
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme shows dithiol-disulfide-oxidoreductase activity, and contains a conserved WCGHC active site and two thioredoxin domains
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme shows dithiol-disulfide-oxidoreductase activity, and contains a conserved WCGHC active site and two thioredoxin domains
Products: -
Products: -
?
additional information
?
-
Substrates: the cotyledon-specific chloroplast biogenesis factor CYO1 is a protein disulfide isomerase and has a chaperone-like activity required for thylakoid biogenesis in cotyledons, mutation of Cyo1 affects the photosynthesis in cotyledons, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: the cotyledon-specific chloroplast biogenesis factor CYO1 is a protein disulfide isomerase and has a chaperone-like activity required for thylakoid biogenesis in cotyledons, mutation of Cyo1 affects the photosynthesis in cotyledons, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: structure and mechanism of PDI in disulfide formation and oxidative protein folding, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: PDI oxidizes pairs of cysteines to form disulfide bonds and can also shuffle incorrect disulfides into their correct pairings, function and mechanism of PDI, PDI has the ability to catalyze dithiol-disulfide exchange reactions, chaperone activity and propensity to form subunits of multi-enzyme complexes, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme has oxidative folding activity
Products: -
Products: -
?
additional information
?
-
-
Substrates: 3,3',5-triiodo-L-thyronine-binding activity
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme may be significant in the action of triiodothyronine towards the target cells
Products: -
Products: -
?
additional information
?
-
-
Substrates: modeling of disulfide formation, the enzyme catalyzes disulfide formation and isomerization and acts as a chaperone inhibiting aggregation, enzyme assists in the system of chaperones and folding catalysts to ensure proper connection of disulfides and protein folding without improper interactions, mechanism of incorrect disulfide recognition
Products: -
Products: -
?
additional information
?
-
-
Substrates: substrate specificity of PDI
Products: -
Products: -
?
additional information
?
-
-
Substrates: PDI is a better thiol oxidant than a disulfide protein reductant
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme shows disulfide reduction and chaperone activities and contains a WCGHC active site, overview, tertiary structure and function analysis under pressure conditions above 100 MPa, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: PDI enhances factor X activation by factor VIIa soluble tissue factor in a dose-dependent manner. The inclusion of annexin V or detergent abolishes the stimulation effect. The presence of 25 nM bovine PDI lowers the apparent Km of factor VIIa for factor X from far above 0.01 mM to 0.001-0.002 mM
Products: -
Products: -
?
additional information
?
-
-
Substrates: PDI is able to renature reduced-denatured RNase. Plasma transglutaminase-coagulation factor XIII, FXIII, also shows PDI activity with reduced-denatured RNase, its PDI activity is located on the A subunit
Products: -
Products: -
?
additional information
?
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Substrates: PDI is able to renature reduced-denatured bovine pancreas RNase A. Plasma transglutaminase-coagulation factor XIII, FXIII, a plasmatic pro-transglutaminase, also shows PDI activity with reduced-denatured RNase, its PDI activity is located on the A subunit. Both FXIII and tissue transglutaminase exhibit PDI activity sdespite the fact that they lack either the essential amino acid sequence, Cys-X-X-Cys, for PDI activity or its related sequences, Cys-Leu-His-Ser or Cys-Ile-His-Ser, which have been reported to impart such activity, overview
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Substrates: PDI catalyzes the isomerization of disulfide bonds on misfolded proteins
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Substrates: study on the interaction of disulfide dyes 2-[(2,4-dinitrophenyl)amino]-3-sulfanylpropanoic acid and 8-[[7,12-diammonio-2-(1H-imidazo[2,1-c][1,2,4]benzotriazin-10-ium-8-yl)-6,13-dioxo-5,14-dioxa-9,10-dithia-2-azahexadecan-16-yl](methyl)amino]-1H-imidazo[2,1-c][1,2,4]benzotriazin-10-ium
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Substrates: PDI is a multifunctional protein required for many aspects of protein folding and transit through the endoplasmic reticulum, the PDI activity is essential for viability, collagen biogenesis and extracellular matrix formation, PDI-2 is required for the normal function of prolyl 4-hydroxylase, a key collagen-modifying enzyme, overview, PDI-2 is required for normal post-embryonic development, all isozymes are synergistically essential for embryonic development in this nematode
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Substrates: PDI is a multifunctional protein required for many aspects of protein folding and transit through the endoplasmic reticulum, the PDI activity is essential for viability, collagen biogenesis and extracellular matrix formation, overview, all isozymes are synergistically essential for embryonic development in this nematode
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Substrates: RB60 is an atypical PDI that functions as a member of a redox regulatory protein complex controlling translation in the chloroplast, the enzyme is essential in the endoplasmic reticulum
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Substrates: RB60 is involved in the light-regulated translation of the psbA mRNA in the chloroplast of the unicellular alga Chlamydomonas reinhardtii, light controls the redox regulation of RB47 function via the coupling of RB47 and RB60 redox states, overview
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Substrates: structure and mechanism of PDI in disulfide formation and oxidative protein folding, overview
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Substrates: RB60 binds to RB47 and modulates its activity via redox and phosphorylation events, RB60 attacks the disulfide bond Cys143-Cys259 of RB47, the redox states of the protein redox partners are coupled, overview, recombinant His-tagged RB47 expressed in Escherichia coli
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Substrates: PDI oxidizes pairs of cysteines to form disulfide bonds and can also shuffle incorrect disulfides into their correct pairings, function and mechanism of PDI, PDI has the ability to catalyze dithiol-disulfide exchange reactions, chaperone activity and propensity to form subunits of multi-enzyme complexes, overview
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Substrates: RB60 is an atypical PDI that functions as a member of a redox regulatory protein complex controlling translation in the chloroplast, the enzyme is essential in the endoplasmic reticulum
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Substrates: in vivo, disulfide bond formation is mainly catalyzed by protein disulfide isomerase
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Substrates: in vivo, disulfide bond formation is mainly catalyzed by protein disulfide isomerase
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Substrates: the enzyme shows oxidase and isomerase activities, overview
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Substrates: the enzyme shows oxidase and isomerase activities, overview
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Substrates: NCgl2478 reduces S-mycothiolated mixed disulfides and intramolecular disulfides via a monothiol-disulfide and a dithiol-disulfide exchange mechanism, respectively. NCgl2478 lacks oxidase activity. HED-SSM is a mixed disulfide between monothiol-disulfide (MSH) and 2-hydroxyethyl disulfide (HED) and a substrate of the enzyme. The enzyme performs reduction of insulin occurred via a dithiol mechanism
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Substrates: NCgl2478 reduces S-mycothiolated mixed disulfides and intramolecular disulfides via a monothiol-disulfide and a dithiol-disulfide exchange mechanism, respectively. NCgl2478 lacks oxidase activity. HED-SSM is a mixed disulfide between monothiol-disulfide (MSH) and 2-hydroxyethyl disulfide (HED) and a substrate of the enzyme. The enzyme performs reduction of insulin occurred via a dithiol mechanism
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Substrates: NCgl2478 reduces S-mycothiolated mixed disulfides and intramolecular disulfides via a monothiol-disulfide and a dithiol-disulfide exchange mechanism, respectively. NCgl2478 lacks oxidase activity. HED-SSM is a mixed disulfide between monothiol-disulfide (MSH) and 2-hydroxyethyl disulfide (HED) and a substrate of the enzyme. The enzyme performs reduction of insulin occurred via a dithiol mechanism
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Substrates: NCgl2478 reduces S-mycothiolated mixed disulfides and intramolecular disulfides via a monothiol-disulfide and a dithiol-disulfide exchange mechanism, respectively. NCgl2478 lacks oxidase activity. HED-SSM is a mixed disulfide between monothiol-disulfide (MSH) and 2-hydroxyethyl disulfide (HED) and a substrate of the enzyme. The enzyme performs reduction of insulin occurred via a dithiol mechanism
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Substrates: NCgl2478 reduces S-mycothiolated mixed disulfides and intramolecular disulfides via a monothiol-disulfide and a dithiol-disulfide exchange mechanism, respectively. NCgl2478 lacks oxidase activity. HED-SSM is a mixed disulfide between monothiol-disulfide (MSH) and 2-hydroxyethyl disulfide (HED) and a substrate of the enzyme. The enzyme performs reduction of insulin occurred via a dithiol mechanism
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Substrates: NCgl2478 reduces S-mycothiolated mixed disulfides and intramolecular disulfides via a monothiol-disulfide and a dithiol-disulfide exchange mechanism, respectively. NCgl2478 lacks oxidase activity. HED-SSM is a mixed disulfide between monothiol-disulfide (MSH) and 2-hydroxyethyl disulfide (HED) and a substrate of the enzyme. The enzyme performs reduction of insulin occurred via a dithiol mechanism
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Substrates: NCgl2478 reduces S-mycothiolated mixed disulfides and intramolecular disulfides via a monothiol-disulfide and a dithiol-disulfide exchange mechanism, respectively. NCgl2478 lacks oxidase activity. HED-SSM is a mixed disulfide between monothiol-disulfide (MSH) and 2-hydroxyethyl disulfide (HED) and a substrate of the enzyme. The enzyme performs reduction of insulin occurred via a dithiol mechanism
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Substrates: NCgl2478 reduces S-mycothiolated mixed disulfides and intramolecular disulfides via a monothiol-disulfide and a dithiol-disulfide exchange mechanism, respectively. NCgl2478 lacks oxidase activity. HED-SSM is a mixed disulfide between monothiol-disulfide (MSH) and 2-hydroxyethyl disulfide (HED) and a substrate of the enzyme. The enzyme performs reduction of insulin occurred via a dithiol mechanism
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Substrates: the enzyme is involved in diphtheria toxin sensitivity and is required for toxin entry, Chlamydia trachomatis or Chlamydia psittaci, intracellular pathogens of humans, require the enzyme for attachment to mammalian CHO6 cells, host cell invasion is obligatory for survival, growth and pathogenesis, overview
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Substrates: the PDI protein is necessary for Chlamydia attachment, but the bacteria apparently do not bind directly to cell-associated PDI, suggesting that Chlamydia attaches to a host protein(s) associated with PDI. PDI enzymatic activity is necessary for bacterial entry but not for attachment, cell surface PDI-mediated reduction triggers Chlamydia entry into cells, molecular mechanism, overview
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Substrates: the active-site cysteine residues of the functional domains, Trx-domains, are essential for catalysis of disulfide bond formation in polypeptides and proteins, such as the bacterial alkaline phosphatase
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Substrates: PDI behaves mainly as an oxidase/isomerase and exhibits chaperone-like activity
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Substrates: the enzyme plays a crucial role in folding periplasmatically excreted proteins
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Substrates: DsbC resolves incorrect disulfides whose formation has been catalyzed by redox-active copper
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Substrates: the enzyme catalyzes disulfide formation and isomerization and acts as a chaperone inhibiting aggregation, enzyme assists in the system of chaperones and folding catalysts to ensure proper connection of disulfides and protein folding without improper interactions
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Substrates: Cys98 and Cys101 form the reversible disulfide bond in the active site, the enzyme is active in reduced state which is stabilized by hydrogen bond interactions of the active cysteine residues with Thr94 and Thr182
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Substrates: substrate disulfide bonds, overview, the AppA homologue Agp, a periplasmic phosphatase, lacks nonconsecutive disulfide bonds and is no substrate for DsbC
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Substrates: DsbC and DbsG also possess thioredoxin-like domains, substrate specificity of PDI
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Substrates: DsbB is an integral membrane protein responsible for the de novo synthesis of disulfide bonds in the Escherichia coli periplasm, disulfide bond formation is catalyzed by the DsbA/DsbB system, DsbA is critical for catalyzing disulfide bond formation in proteins in the bacterial periplasm, which it accomplishes by directly oxidizing substrate proteins via dithiol-disulfide exchange, DsbA donates its disulfide bond directly to substrate proteins, in the process of transferring electrons from DsbA to a tightly bound ubiquinone cofactor, DsbB undergoes an unusual spectral transition, DsbA must be reoxidized by an electron acceptor, mechanism, overview
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Substrates: PDI oxidizes pairs of cysteines to form disulfide bonds and can also shuffle incorrect disulfides into their correct pairings, function and mechanism of PDI, bacterial machinery for disulfide formation and oxidative protein folding, overview
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Substrates: kinetic cycle of DsbB, thew enzyme uses a tightly bound ubiquinone cofactor, which becomes oxidized to hydroquinone and is regenerated by the electron transport chain and O2, overview
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Substrates: PDI has the ability to catalyze dithiol-disulfide exchange reactions, chaperone activity and propensity to form subunits of multi-enzyme complexes, overview
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Substrates: the enzyme shows disulfide reduction and chaperone activities, it facilitates the folding of secreted proteins with multiple disulfide bonds by catalyzing disulfide-bond rearrangement
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Substrates: PDI is a subunit of the enzyme prolyl-4-hydroxylase, which catalyzes the formation of 4-hydroxyprolyl residues in nascent collagen-like polypeptides. PDI is also a subunit of a triacylglycerol transfer protein, which facilitates the incorporation of lipids into newly synthesized core lipoproteins within the endoplasmic reticulum. The function of PDI is to maintain the alpha-subunit of this enzyme in an active form
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Substrates: the enzyme acts as a thyroid-hormone binding protein
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Substrates: the enzyme plays important roles in the folding of nascent polypeptides and the formation of disulfide bonds in the endoplasmic reticulum, PDIS-1 associates with proglycinin, a precursor of the seed storage protein glycinin, in the cotyledon, seed-dependent aggregation of amyloid beta-peptide (1-40) monomers is inhibited by both PDIS-1 and PDIS-2, both are involved in seed development, overview
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Substrates: PDIS-1 and PDIS-2 show both an oxidative refolding activity of denatured ribonuclease A and a chaperone activity, PDIS-1 and PDIS-2 both possess a putative N-terminal secretory signal sequence and two tandem thioredoxin-like motifs, with a CGHC active site
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Substrates: enzyme is involved in the proper folding or quality control of storage proteins
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Substrates: GmPDIL-1 and GmPDIL-2 function as molecular chaperones, and prevent the aggregation of unfolded rhodanese, while GmPDIL-3a and GmPDIL-3b do not
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Substrates: recombinant GmPDIL-3a and GmPDIL-3b do not function as oxidoreductases or as molecular chaperones in vitro, although a proportion of each protein formed complexes in both thiol-dependent and thiol-independent ways in the endoplasmic reticulum. GmPDIL-3a and GmPDIL-3b have no stimulatory effect on the oxidative refolding of RNase A by GmPDIL-1 and GmPDIL-2 when mixed together, further confirming that the functional properties of GmPDIL-3a and GmPDIL-3b are probably unique
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Substrates: HlPDI-1 might be involved in tick blood feeding and Babesia parasite infection in ticks
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Substrates: HlPDI-1 might be involved in tick blood feeding and Babesia parasite infection in ticks
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Substrates: HlPDI-1 might be involved in tick blood feeding and Babesia parasite infection in ticks
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Substrates: HlPDI-1 might be involved in tick blood feeding and Babesia parasite infection in ticks
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Substrates: HlPDI-3 might be involved in tick blood feeding and Babesia parasite infection in ticks
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Substrates: HlPDI-3 might be involved in tick blood feeding and Babesia parasite infection in ticks
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Substrates: HlPDI-3 might be involved in tick blood feeding and Babesia parasite infection in ticks
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Substrates: HlPDI-3 might be involved in tick blood feeding and Babesia parasite infection in ticks
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Substrates: protein disulfide isomerases are involved in blood feeding, viability and oocyte development, probably by mediating the formation of disulfide bond-containing proteins of the ticks and the formation of basement membrane and cuticle components such as extracellular matrix
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Substrates: protein disulfide isomerases are involved in blood feeding, viability and oocyte development, probably by mediating the formation of disulfide bond-containing proteins of the ticks and the formation of basement membrane and cuticle components such as extracellular matrix
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Substrates: protein disulfide isomerases are involved in blood feeding, viability and oocyte development, probably by mediating the formation of disulfide bond-containing proteins of the ticks and the formation of basement membrane and cuticle components such as extracellular matrix
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Substrates: protein disulfide isomerases are involved in blood feeding, viability and oocyte development, probably by mediating the formation of disulfide bond-containing proteins of the ticks and the formation of basement membrane and cuticle components such as extracellular matrix
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Substrates: modeling of disulfide formation, the enzyme catalyzes disulfide formation and isomerization and acts as a chaperone inhibiting aggregation, enzyme assists in the system of chaperones and folding catalysts to ensure proper connection of disulfides and protein folding without improper interactions, the pancreatic enzyme is responsible for folding of a subset of secreted pancreatic zymogens
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Substrates: substrate specificity of PDI
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Substrates: the four domains a, b, b', and a' show cooperative properties in both isomerase and chaperone functions of PDi
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Substrates: isomerase activity is assayed using the insulin/glutathione coupled assay
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Substrates: the enzyme is involved in correct disulfide bond formation in secretory proteins as a key step in endoplasmic reticulum quality control, ERp57 works in conjunction with the endoplasmic reticulum lectin-like chaperones calnexin and calreticulin via the noncatalytic b' domain of the enzyme, the b' domains of ERp57 and PDI are very different, overview
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Substrates: the enzyme is involved in correct disulfide bond formation in secretory proteins as a key step in endoplasmic reticulum quality control, ERp57 works in conjunction with the endoplasmic reticulum lectin-like chaperones calnexin and calreticulin via the noncatalytic b' domain of the enzyme, the b' domains of ERp57 and PDI are very different, overview
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Substrates: the enzyme is involved in correct disulfide bond formation in secretory proteins as a key step in endoplasmic reticulum quality control, ERp57 works in conjunction with the endoplasmic reticulum lectin-like chaperones calnexin and calreticulin via the noncatalytic b' domain of the enzyme, the b' domains of ERp57 and PDI are very different, overview
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Substrates: the enzyme is involved in correct disulfide bond formation in secretory proteins as a key step in endoplasmic reticulum quality control, ERp57 works in conjunction with the endoplasmic reticulum lectin-like chaperones calnexin and calreticulin via the noncatalytic b' domain of the enzyme, the b' domains of ERp57 and PDI are very different, overview
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Substrates: the enzyme mediates rapid delivery of NO signalling into human platelets from the S-nitrosothiol compound S-nitrosoglutathione, NO delivery is blocked by inhibition of PDI, overview
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Substrates: PDI has two distinct functions: acting as a molecular chaperone to maintain properly folded proteins and regulating the redox state of proteins by catalyzing the thiol-disulfide exchange reaction through two thioredoxin-like domains
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Substrates: PDIis responsible for correct disulfide bond formation of proteins in the endoplasmic reticulum, it recognize unfolded proteins and can be selective for specific proteins or classes
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Substrates: structure and mechanism of PDI in disulfide formation and oxidative protein folding, overview
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Substrates: the enzyme catalyzes the oxidation, reduction, and isomerization of secretory proteins and plasma membrane proteins, substrate specificity, the enzyme contains a WCGHC active site, overview
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Substrates: the enzyme catalyzes the oxidation, reduction, and isomerization of secretory proteins and plasma membrane proteins, substrate specificity, the enzyme contains a WCGHC active site, overview
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Substrates: the enzyme catalyzes the oxidation, reduction, and isomerization of secretory proteins and plasma membrane proteins, substrate specificity, the enzyme contains a WCGHC active site, overview
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Substrates: the enzyme catalyzes the oxidation, reduction, and isomerization of secretory proteins and plasma membrane proteins, substrate specificity, the enzyme contains a WCGHC active site, overview
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Substrates: the enzyme shows disulfide exchange activity
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Substrates: ERp27 is non-catalytic and interacts with ERp57, ERp57 binds ERp27 by the Asp-Glu-Trp-Asp sequence in domain 2, reduced binding to R280A mutant ERp57, overview, it binds DELTA-somatostatin, the standard test peptide for protein disulfide isomerase-substrate binding, at its second domain, a significant conformational change in the b'-like domain of ERp27 occurs upon substrate binding, overview
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Substrates: ERp27 is non-catalytic and interacts with ERp57, ERp57 binds ERp27 by the Asp-Glu-Trp-Asp sequence in domain 2, reduced binding to R280A mutant ERp57, overview, it binds DELTA-somatostatin, the standard test peptide for protein disulfide isomerase-substrate binding, at its second domain, a significant conformational change in the b'-like domain of ERp27 occurs upon substrate binding, overview
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Substrates: ERp57 interacts with the lectin chaperone calnexin, binding structure, and active site structure, overview
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Substrates: PDI oxidizes pairs of cysteines to form disulfide bonds and can also shuffle incorrect disulfides into their correct pairings, function and mechanism of PDI, PDI has the ability to catalyze dithiol-disulfide exchange reactions, chaperone activity and propensity to form subunits of multi-enzyme complexes, overview
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Substrates: PDI can function as a high-capacity intracellular 17beta-estradiol-binding protein that increases the concentration and accumulation of 17beta-estradiol in live cells. The intracellular PDI-bound 17beta-estradiol can be released from PDI upon a drop in 17beta-estradiol levels and the released 17beta-estradiol can augment estrogen receptor-mediated transcriptional activity and mitogenic actions in cultured cells. The binding of 17beta-estradiol by PDI also reduces the rate of metabolic disposition of this hormone
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Substrates: protein disulfide isomerase contributes to the activation of cryptic initiator protein tissue factoron microvesicles in vitro
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Substrates: protein disulfide isomerase PDI directly interacts with thiol-containing fibrinogen receptor alphaIIbbeta3. PDI has greater ability to isomerize disulfide bonds than the alphaIIbbeta3 integrin
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Substrates: recombinant human PDI does not influence factor X activation by factor VIIa soluble tissue factor
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Substrates: reduced protein disulfide isomerase activates initiator protein tissue factor by isomerzation of a mixed disulfide and a free thiol to an intramolecular disulfide
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Substrates: in vivo, protein disulfide isomerase is present in two semi-oxidized forms in which either the first active site in the a domain or the second active site in the a' domain is oxidized. In HEK-293 cells, about 50% of enzyme is fully reduced, in 18% a domain is oxidized, a' reduced, in 15%, the a domain is reduced, a' oxidized, and 16% of enzyme are fully oxidized
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Substrates: presence of protein disulfide isomerase on the surface of platelet-derived microparticles. Enzyme is catalytically active and capable of both promoting platelet aggregation and disrupting insulin signaling. Platelet-derived microparticles increase the initial rates of aggregation by 4fold and the pro-aggregatory activity of micrparticles can be attenuated with an anti-PDI antibody. Anti-PDI antibodies are able to block the degradation of insulin, thereby restoring insulin signaling
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Substrates: the nucleophilic C36 thiol of the protein disulfide isomerase a domain is positioned over the N-terminus of the alpha2 helix. The H38 amide in the reduced enzyme exhibits a maximum rate of exchange at pH 5 due to efficient general base catalysis by the neutral imidazole of its own side chain and suppression of its exchange by the ionization of the C36 thiol. Ionization of this thiol and deprotonation of the H38 side chain suppress the C39 amide hydroxide-catalyzed exchange by a million-fold. The electrostatic potential within the active site stabilizes the two distinct transition states that lead to substrate reduction and oxidation
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Substrates: the nucleophilic C36 thiol of the protein disulfide isomerase a domain is positioned over the N-terminus of the alpha2 helix. The H38 amide in the reduced enzyme exhibits a maximum rate of exchange at pH 5 due to efficient general base catalysis by the neutral imidazole of its own side chain and suppression of its exchange by the ionization of the C36 thiol. Ionization of this thiol and deprotonation of the H38 side chain suppress the C39 amide hydroxide-catalyzed exchange by a million-fold. The electrostatic potential within the active site stabilizes the two distinct transition states that lead to substrate reduction and oxidation
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Substrates: the PDI protein is necessary for Chlamydia attachment, but the bacteria apparently do not bind directly to cell-associated PDI, suggesting that Chlamydia attaches to a host protein(s) associated with PDI. PDI enzymatic activity is necessary for bacterial entry but not for attachment, cell surface PDI-mediated reduction triggers Chlamydia entry into cells, molecular mechanism, overview
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Substrates: ER protein 57, ERP-57, also known as PDIA3, has disulfide oxidoreductase and isomerase activity. ERP-57 interacts with calnexin, CANX, a chaperone protein and a lectin that binds glycoproteins through a transient oligosaccharide intermediate, thought to prevent a rapid degradation, as well as endoplasmic reticulum retention, of misfolded proteins, overview
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Substrates: PDI catalyzes disulfide bond formation in the endoplasmic reticulum
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Substrates: PDI catalyzes disulfide bond formation in the endoplasmic reticulum
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Substrates: PDI specifically binds 3,3',5-triiodo-L-thyronine
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Substrates: PDIp also shows chaperone activity in preventing the aggregation of reduced insulin B chain and denatured D-glyceraldehyde-3-phosphate dehydrogenase, PDIp can form stable complexes with thermal-denatured substrate proteins, e.g. MCF-7 cellular proteins, independently of their enzymatic activity. The b-b' fragment of PDIp, which does not contain the active sites and is devoid of enzymatic activity, still has chaperone activity
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Substrates: PDIp also shows chaperone activity in preventing the aggregation of reduced insulin B chain and denatured D-glyceraldehyde-3-phosphate dehydrogenase, PDIp can form stable complexes with thermal-denatured substrate proteins, e.g. MCF-7 cellular proteins, independently of their enzymatic activity. The b-b' fragment of PDIp, which does not contain the active sites and is devoid of enzymatic activity, still has chaperone activity
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Substrates: PDI specifically associates with signal peptide peptidase, SPP, independently of human cytomegalovirus glycoprotein US2, but not with Derlin-1
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Substrates: the enzyme's isomerase activity comprises disulfide reduction, refolding, and oxidation of thiols requiring all four thioredoxin-folded domains in tandem link plus the C-terminal acidic extension
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Substrates: formation of active RNase from rRNase and sRNase in the presence of PDIp. The pancreas-specific PDI homolog PDIp can function independently as a chaperone in vitro and in vivo
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Substrates: formation of active RNase from rRNase and sRNase in the presence of PDIp. The pancreas-specific PDI homolog PDIp can function independently as a chaperone in vitro and in vivo
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additional information
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Substrates: PDI forms mixed disulfides in substrate molecules, substrates are Ero1alpha, clusterin, or PTX3, analysis of PDI substrate specificity, comparison to other members of the protein disulfide isomerase family of oxidoreductases, overview
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additional information
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Substrates: PDI directly interacts with calreticulin
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additional information
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Substrates: the enzyme has a single E2-binding site
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additional information
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Substrates: the enzyme has three catalytic activities including thiol-disulfide oxireductase, disulfide isomerase, and redox-dependent chaperone
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additional information
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Substrates: TXNDC5 directly interacts with Srx through its thioredoxin-like domains, binding and in vivo complexing analysis. The Srx-TXNDC5 interaction is not affected by the treatment of cells with exogenous H2O2
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additional information
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Substrates: TXNDC5 directly interacts with Srx through its thioredoxin-like domains, binding and in vivo complexing analysis. The Srx-TXNDC5 interaction is not affected by the treatment of cells with exogenous H2O2
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additional information
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-
Substrates: the enzyme catalyzes disulfide formation in a reduced substrate by transferring oxidizing equivalents from upstream sulfhydryl oxidase Ero1, which directly couples disulfide bond formation to the reduction of molecular oxygen. Alternatively, PDI can be oxidized by peroxiredoxin 4 and glutathione peroxidase 7 or 8, which utilize H2O2 to drive oxidization. In contrast, the enzyme catalyzes disulfide bond reduction to reduce/unfold a substrate by using reducing equivalent glutathione
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additional information
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Substrates: the enzyme has a single E2-binding site
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additional information
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Substrates: protein disulfide isomerase serves as a subunit of at least two enzymes, the beta-subunit of the enzyme prolyl hydroxylase and an ER triglyceride transferase
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additional information
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Substrates: PDILT forms intermolecular disulfide bonds in testis
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additional information
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Substrates: PDILT forms intermolecular disulfide bonds, but shows no intramolecular disulfide bonds
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additional information
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-
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Substrates: sperm surface protein disulfide isomerase activity plays a role in gamete fusion and sperm-egg interaction, the enzyme mediates conformational changes by thiol-disulfide exchange in fusion-active proteins, participation of ERp57, overview
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additional information
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Substrates: the enzyme mediates conformational changes by thiol-disulfide exchange
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additional information
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Substrates: PDI is required in vivo for both fibrin generation and platelet thrombus formation
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additional information
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Substrates: protein disulfide isomerase directly promotes initiator protein tissue factor-dependent fibrin production during thrombus formation in vivo
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additional information
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Substrates: enzyme converts initiator protein tissue factor cysteine residues from glutathionylated to disulfide state
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additional information
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Substrates: PDIA1, and probably also PDIA3, shows cytotoxic regulatory protein 2, CxRP2, activity in T-cells, acting as perforin inhibitor associated with cytotoxic T cell granules, overview. Perforin is a membrane-permeabilizing protein important to T cell cytotoxic action
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additional information
?
-
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Substrates: AGR2 is essential for production of intestinal mucin MUC2, but is not required for establishment of intestinal secretory epithelial cell lineages
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additional information
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-
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Substrates: PDI specifically binds 3,3',5-triiodo-L-thyronine
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additional information
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Substrates: a cysteine residue in the thioredoxin-like domain of AGR2 forms mixed disulfide bonds with MUC2, mutational analysis of the AGR2-MUC2 interaction, overview
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additional information
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Substrates: the enzyme's isomerase activity comprises disulfide reduction, refolding, and oxidation of thiols requiring all four thioredoxin-folded domains in tandem link plus the C-terminal acidic extension
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additional information
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Substrates: PDIA1, and probably also PDIA3, shows cytotoxic regulatory protein 2, CxRP2, activity in T-cells, acting as perforin inhibitor associated with cytotoxic T cell granules, overview. Perforin is a membrane-permeabilizing protein important to T cell cytotoxic action
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additional information
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Substrates: PDI also functions as a dehydroascorbate reductase and a molecular chaperone besides its disulfide-isomerizing function
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additional information
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Substrates: PDI is a major protein in the endoplasmic reticulum, operating as an essential folding catalyst and molecular chaperone for disulfide-containing proteins by catalyzing the formation, rearrangement, and breakage of their disulfide bridges
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additional information
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Substrates: the enzyme has a modular structure with four thioredoxin-like domains, a, b, b', and a', along with a C-terminal extension. The homologous a and a' domains contain one cysteine pair in their active site directly involved in thiol-disulfide exchange reactions, while the b' domain putatively provides a primary binding site for unstructured regions of the substrate polypeptides, mechanistic model of PDI action, overview. The a' domain transfers its own disulfide bond into the unfolded protein accommodated on the hydrophobic surface of the substrate-binding region, which consequently changes into a closed form releasing the oxidized substrate, domain arrangements and redox behaviour, overview
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additional information
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Substrates: the enzyme is involved in the oxidative folding of cystine knot defense proteins and in in the biosynthesis of insecticidal cyclotides, overview, the Oldenlandia affinis plant accumulates knotted circular proteins called cyclotides
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additional information
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Substrates: PDI interacts with the cyclotide precursor protein Oak1, PDi is a functional oxidoreductase and exhibits both protein disulfide isomerase and chaperone activity, properties of disulfide species, overview
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additional information
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Substrates: PDIL2-3 activity is dispensable in the oxidative folding of alpha-globulin
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additional information
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Substrates: PDIL2-3 activity is dispensable in the oxidative folding of alpha-globulin
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additional information
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Substrates: PDIL2-3 activity is dispensable in the oxidative folding of alpha-globulin
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additional information
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Substrates: the enzyme assists protein folding in malaria parasites
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additional information
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Substrates: the enzyme is a potent oxido-reductase and facilitates the disulfide-dependent conformational folding of EBA-175, the enzyme contain two CGHC active sites within two thioredoxin domains
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additional information
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Substrates: the enzyme assists protein folding in malaria parasites
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additional information
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Substrates: the enzyme is a potent oxido-reductase and facilitates the disulfide-dependent conformational folding of EBA-175, the enzyme contain two CGHC active sites within two thioredoxin domains
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additional information
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Substrates: the enzyme assists protein folding in malaria parasites
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additional information
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Substrates: the enzyme is a potent oxido-reductase and facilitates the disulfide-dependent conformational folding of EBA-175, the enzyme contain two CGHC active sites within two thioredoxin domains
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additional information
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Substrates: the enzyme shows disulfide oxidase/isomerase, reductase, and chaperone activities, overview
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additional information
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Substrates: the enzyme assists protein folding in malaria parasites
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additional information
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-
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Substrates: the enzyme assists protein folding in malaria parasites
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additional information
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Substrates: the enzyme is a potent oxido-reductase and facilitates the disulfide-dependent conformational folding of EBA-175, the enzyme contain two CGHC active sites within two thioredoxin domains
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additional information
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-
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Substrates: the enzyme is a potent oxido-reductase and facilitates the disulfide-dependent conformational folding of EBA-175, the enzyme contain two CGHC active sites within two thioredoxin domains
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additional information
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Substrates: the enzyme assists protein folding in malaria parasites
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additional information
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Substrates: the enzyme is a potent oxido-reductase and facilitates the disulfide-dependent conformational folding of EBA-175, the enzyme contain two CGHC active sites within two thioredoxin domains
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additional information
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Substrates: the enzyme assists protein folding in malaria parasites
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additional information
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Substrates: the enzyme assists protein folding in malaria parasites
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additional information
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Substrates: the enzyme is a potent oxido-reductase and facilitates the disulfide-dependent conformational folding of EBA-175, the enzyme contain two CGHC active sites within two thioredoxin domains
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additional information
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Substrates: the enzyme is a potent oxido-reductase and facilitates the disulfide-dependent conformational folding of EBA-175, the enzyme contain two CGHC active sites within two thioredoxin domains
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?
additional information
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-
Substrates: the enzyme assists protein folding in malaria parasites
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additional information
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Substrates: the enzyme is a potent oxido-reductase and facilitates the disulfide-dependent conformational folding of EBA-175, the enzyme contain two CGHC active sites within two thioredoxin domains
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additional information
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Substrates: the enzyme assists protein folding in malaria parasites
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additional information
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-
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Substrates: the enzyme assists protein folding in malaria parasites
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additional information
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Substrates: the enzyme is a potent oxido-reductase and facilitates the disulfide-dependent conformational folding of EBA-175, the enzyme contains two CGHC active sites within two thioredoxin domains
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additional information
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-
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Substrates: the enzyme is a potent oxido-reductase and facilitates the disulfide-dependent conformational folding of EBA-175, the enzyme contains two CGHC active sites within two thioredoxin domains
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additional information
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-
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Substrates: isoform PDI-A shows no activity with insulin, NADPH thioredoxin reductase , NADP malate dehydrogenase, peroxiredoxin, or RNase A
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additional information
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Substrates: DsbA and DsbC are involved in disulfide bond formation and play an important role in the formation of extracellular enzymes, DsbA is important in lipase stability and excretion
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additional information
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Substrates: the enzyme catalyzes dithiol-disulfide exchange reactions with an essential -C-P-Y-C- active site motif with catalytic C35 and C146, enzyme shows oxidative, reductive, and isomerase activities as well as ATPase activity, the latter being related to the enzyme's chaperone function
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additional information
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Substrates: PDI has dehydroascorbate reductase activity
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additional information
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Substrates: PDI has dehydroascorbate reductase activity, PDI may play a role in the intraluminal dehydroascorbate reduction
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additional information
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Substrates: modeling of disulfide formation, the enzyme catalyzes disulfide formation and isomerization and acts as a chaperone inhibiting aggregation, enzyme assists in the system of chaperones and folding catalysts to ensure proper connection of disulfides and protein folding without improper interactions
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additional information
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Substrates: substrate specificity of PDI
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additional information
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-
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Substrates: PDI is a multifunctional protein that is critically involved in the folding, assembly, and shedding of many cellular proteins via its isomerase activity in addition to being considered to function as an intracellular hormone reservoir
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additional information
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Substrates: cell-surface PDI is required for transnitrosation of metallothionein by S-nitroso-albumin in intact pulmonary vascular endothelial cells, overview
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additional information
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Substrates: the enzyme shows hormone binding activity, e.g. of L-T3 and 17beta-estradiol hormones
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additional information
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Substrates: PDI possesses an anomalously low thiol pKa and is fine-tuned to catalyze oxidative folding in the lumen of the endoplasmic reticulum where the ambient pH of about 7 would otherwise retard thioldisulfide exchange reactions and hinder acquisition of the native fold
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additional information
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Substrates: PDIA1, and probably also PDIA3, shows cytotoxic regulatory protein 2, CxRP2, activity in T-cells, acting as perforin inhibitor associated with cytotoxic T cell granules, overview. Perforin is a membrane-permeabilizing protein important to T cell cytotoxic action
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additional information
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-
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Substrates: PDI is a catalyst of isomerization of substrate protein intra- and extramolecular disulfide bridges and also has 3,3',5-triiodo-L-thyronine-binding activity and molecular chaperone-like activity
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additional information
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Substrates: the oxidoreductase chaperone PDI has an effect on the critical structure-forming step during the oxidative maturation of model disulfide-bond-containing proteins, it inhibits the conformational folding step of oxidative fold maturation and, therefore, has limited overall catalytic efficiency as an oxidoreductase chaperone, impact of rat PDI, null PDI and enzyme domains on the structure-forming step, overview. Detrimental impact of the oxidoreductase activity PDI during conformational folding include peptidyl prolyl isomerase which facilitates cis-trans isomerization of prolines
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additional information
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-
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Substrates: PDI specifically binds 3,3',5-triiodo-L-thyronine
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additional information
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Substrates: oxidative refolding of redRNaseA by disulfide isomerization activity, suppression of the thermal aggregation of alcohol dehydrogenase by chaperone activity, binding activity of 3,3',5-triiodo-L-thyronine in GH3 cells
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additional information
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Substrates: ERp72 substrate specificity of ERp72, overview. Ep72 does not interact with calnexin
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additional information
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-
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Substrates: ERp72 substrate specificity of ERp72, overview. Ep72 does not interact with calnexin
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additional information
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-
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Substrates: the enzyme renatures denatured RNase A
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additional information
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-
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Substrates: the enzyme's isomerase activity comprises disulfide reduction, refolding, and oxidation of thiols requiring all four thioredoxin-folded domains in tandem link plus the C-terminal acidic extension
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additional information
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-
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Substrates: the enzyme has an essential role that is distinct from its function in formation of native disulphides
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additional information
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Substrates: the enzyme is an essential catalyst of disulfide formation with two cysteines in the active site facilitating thiol-disulfide exchange
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additional information
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Substrates: essential enzyme for yeast cell growth, both oxidase and isomerase activities are required
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additional information
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Substrates: PDI plays a key role in catalyzing the folding of secretory proteins
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additional information
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Substrates: the organism is completely dependent on PDI activity for growth
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additional information
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Substrates: regulation of PDI and PDI homologues activities, in vivo isomerase activity depends only on full-length PDI, not on PDI-homologues, modeling of disulfide formation, the enzyme catalyzes disulfide formation and isomerization and acts as a chaperone inhibiting aggregation, enzyme assists in the system of chaperones and folding catalysts to ensure proper connection of disulfides and protein folding without improper interactions
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additional information
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Substrates: non-active site cysteines form a disulfide bridges which destabilizes the N-terminal active site disulfide rendering it a 18fold better oxidant by this way
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additional information
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Substrates: all 5 domains of PDI are required for full catalytic activity
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additional information
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Substrates: the yPDI enzyme family members Mpd1p, Mpd2p, and Eug1p show high chaperone activity, but low isomerase activity compared to PDI, isomerase activity is assayed using the insulin/glutathione coupled assay, chaperone activity is also measured utilizing mastoparan as substrate
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additional information
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Substrates: Eug1p, Mpd1p, Mpd2p, and Eps1p partially compensate for PDI, substrate specificity of PDI
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additional information
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Substrates: structure and mechanism of PDI in disulfide formation and oxidative protein folding, overview
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additional information
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Substrates: structure and mechanism of PDI in disulfide formation and oxidative protein folding, overview
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additional information
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Substrates: PDI oxidizes pairs of cysteines to form disulfide bonds and can also shuffle incorrect disulfides into their correct pairings, function and mechanism of PDI, PDI has the ability to catalyze dithiol-disulfide exchange reactions, chaperone activity and propensity to form subunits of multi-enzyme complexes, overview
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additional information
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Substrates: PDI oxidizes pairs of cysteines to form disulfide bonds and can also shuffle incorrect disulfides into their correct pairings, function and mechanism of PDI, PDI has the ability to catalyze dithiol-disulfide exchange reactions, chaperone activity and propensity to form subunits of multi-enzyme complexes, overview
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additional information
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Substrates: protein disulfide isomerase has a concentration-dependent chaperone-activity and inhibits the aggregation of rhodanese, which has no disulfide bonds
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additional information
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Substrates: interactions between the C-terminal domain of Mnl1p and PDI, which include an intermolecular disulfide bond, are essential for subsequent introduction of a disulfide bond into the mannosidase homology domain of Mnl1p by PDI. This disulfide bond is essential for the ER-associated degradation activity of Mnl1p and in turn stabilizes the prolonged association of PDI with Mnl1p
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additional information
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Substrates: PDI first recognizes the C-terminal domain of Mnl1p containing Asp607, Glu627, and Trp636 , PDI forms an intermolecular disulfide bond with C5 or C6 of Mnl1p. PDI introduces a disulfide bond between C1 and C3 in the MHDof Mnl1p, the disulfide bond between C1 and C3 in turn stabilizes association of PDI with Mnl1p, and the intermolecular disulfide bond between PDI and C5 or C6 of Mnl1p is partially reduced,whereas maintaining association of PDI and Mnl1p
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additional information
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Substrates: the organism is completely dependent on PDI activity for growth
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additional information
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Substrates: the yPDI enzyme family members Mpd1p, Mpd2p, and Eug1p show high chaperone activity, but low isomerase activity compared to PDI, isomerase activity is assayed using the insulin/glutathione coupled assay, chaperone activity is also measured utilizing mastoparan as substrate
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additional information
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Substrates: interactions between the C-terminal domain of Mnl1p and PDI, which include an intermolecular disulfide bond, are essential for subsequent introduction of a disulfide bond into the mannosidase homology domain of Mnl1p by PDI. This disulfide bond is essential for the ER-associated degradation activity of Mnl1p and in turn stabilizes the prolonged association of PDI with Mnl1p
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additional information
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Substrates: PDI first recognizes the C-terminal domain of Mnl1p containing Asp607, Glu627, and Trp636 , PDI forms an intermolecular disulfide bond with C5 or C6 of Mnl1p. PDI introduces a disulfide bond between C1 and C3 in the MHDof Mnl1p, the disulfide bond between C1 and C3 in turn stabilizes association of PDI with Mnl1p, and the intermolecular disulfide bond between PDI and C5 or C6 of Mnl1p is partially reduced,whereas maintaining association of PDI and Mnl1p
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additional information
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Substrates: PDI is involved in the cellular growth and response to nutritional and oxidative stress, regulation, overview
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additional information
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Substrates: PDI is involved in the cellular growth and response to nutritional and oxidative stress, regulation, overview
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additional information
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Substrates: PDI is involved in the cellular growth and response to nutritional and oxidative stress, regulation, overview
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additional information
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Substrates: both chaperone and isomerase functions of PDI are essential for acceleration of the oxidative refolding and reactivation of dimeric alkaline protease inhibitor API, PDI acts as isomerase/chaperone for a few monomeric proteins assisting in disulfide bond formation and rearrangement of secreted proteins
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additional information
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Substrates: both chaperone and isomerase functions of PDI are essential for acceleration of the oxidative refolding and reactivation of dimeric alkaline protease inhibitor API, PDI acts as isomerase/chaperone for a few monomeric proteins assisting in disulfide bond formation and rearrangement of secreted proteins
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additional information
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Substrates: PDIA3 shows chaperone activity to promote oxidative refolding of reduced denatured lysozyme, meanwhile PDI-P5 exhibits anti-chaperone activity to inhibit oxidative refolding of lysozyme at an equimolar ratio
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additional information
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Substrates: PDIA3 shows chaperone activity to promote oxidative refolding of reduced denatured lysozyme, meanwhile PDI-P5 exhibits anti-chaperone activity to inhibit oxidative refolding of lysozyme at an equimolar ratio
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additional information
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Substrates: the isozymes catalyze refolding of reduced and denatured lysozyme
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additional information
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Substrates: the isozymes catalyze refolding of reduced and denatured lysozyme
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additional information
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Substrates: the single domain PDI-1 and the class 1 PDI-2 are not essential for the organism
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additional information
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Substrates: the single domain PDI-1 and the class 1 PDI-2 are not essential for the organism
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additional information
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Substrates: the single domain PDI-1 and the class 1 PDI-2 of the organism both posses isomerase activity, but only the single domain PDI has reducing activity
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additional information
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Substrates: the single domain PDI-1 and the class 1 PDI-2 of the organism both posses isomerase activity, but only the single domain PDI has reducing activity
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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
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
apolipoprotein B100
?
-
Substrates: the enzyme assists in the oxidative folding of apolipoprotein B100
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carboxypeptidase Y
?
-
Substrates: maturation of carboxypeptidase Y
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denatured RNase A + GSH
renatured RNase A + GSSG
-
Substrates: -
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E2A homodimer
E2A-basic helix-loop-helix protein heterodimer
-
Substrates: 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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estrogen receptor alpha
?
-
Substrates: i.e. ERalpha, PDI plays a critical role in estrogen responsiveness by functioning as a molecular chaperone and assisting the receptor in differentially regulating target gene expression, PDI alters estrogen-mediated transactivation, overview, PDI enhances ERalpha-DNA interactions in presence of an oxidizing agent
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integrin subunit alpha11
?
-
Substrates: the enzyme activates integrin subunit alpha11
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integrin subunit beta1
?
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Substrates: the enzyme activates integrin subunit beta1
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neuronal nitric oxide synthase
?
-
Substrates: the enzyme catalyzes neuronal nitric oxide synthase dimerization
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?
reduced denatured RNase A + GSH
reduced renatured RNase A + GSSG
-
Substrates: -
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reduced ribonuclease A
denatured ribonuclease A
Substrates: -
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unfolded RNase
refolded RNase
Substrates: -
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?
alkaline protease inhibitor
?
-
Substrates: folding and rearrangement of alkaline protease inhibitor
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alkaline protease inhibitor
?
-
Substrates: folding and rearrangement of alkaline protease inhibitor
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Insulin-(SS) + GSH
Insulin-(SH)2 + GSSG
-
Substrates: -
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Insulin-(SS) + GSH
Insulin-(SH)2 + GSSG
-
Substrates: protein disulfide isomerase supports proinsulin folding as chaperone and isomerase
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Insulin-(SS) + GSH
Insulin-(SH)2 + GSSG
-
Substrates: -
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mycothiol-coupled hydroxyethyl disulfide
mycothiol + hydroxyethyl disulfide
Substrates: a mixed disulfide
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mycothiol-coupled hydroxyethyl disulfide
mycothiol + hydroxyethyl disulfide
Substrates: a mixed disulfide
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mycothiol-coupled hydroxyethyl disulfide
mycothiol + hydroxyethyl disulfide
Substrates: a mixed disulfide
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mycothiol-coupled hydroxyethyl disulfide
mycothiol + hydroxyethyl disulfide
Substrates: a mixed disulfide
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mycothiol-coupled hydroxyethyl disulfide
mycothiol + hydroxyethyl disulfide
Substrates: a mixed disulfide
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mycothiol-coupled hydroxyethyl disulfide
mycothiol + hydroxyethyl disulfide
Substrates: a mixed disulfide
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mycothiol-coupled hydroxyethyl disulfide
mycothiol + hydroxyethyl disulfide
Substrates: a mixed disulfide
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Proteins
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Substrates: facilitates the formation of the correct disulfide bonds within newly synthesized polypeptides
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Proteins
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Substrates: catalyzes disulfide cleavage in membrane-bound diphtheria toxin or the membrane-bound conjugate, iodotyramine conjugated with poly(D-Lys) via a 3,3'-dithiobis(propionic acid) spacer
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Proteins
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Substrates: involved in cotranslational disulfide bond formation
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Proteins
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Substrates: native, reduced or with wrong disulfide bonds
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Proteins
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Substrates: implicated in the biosynthesis of secretory proteins
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Proteins
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Substrates: enzyme may play a physiological role in the catalysis of S-S-bond formation in prolactin
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Proteins
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Substrates: may play a role in the formation of disulfide bonds in extracellular and periplasmic proteins
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Proteins
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Substrates: native, reduced or with wrong disulfide bonds
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Proteins
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Substrates: facilitates the formation of disulfides during the folding and processing of membrane and secretory proteins
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Proteins
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Substrates: enzyme may be involved in the formation of intra-chain and inter-chain disulfide bonds in procollagen
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Proteins
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Substrates: may play a role in retaining prolyl 4-hydroxylase in its native conformation
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Proteins
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Substrates: enzyme may be involved in the formation of intra-chain and inter-chain disulfide bonds in procollagen
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Proteins
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Substrates: platelet enzyme may play a role in the various haemostatic and tissue remodelling processes in which platelets are involved
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Proteins
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Substrates: native, reduced or with wrong disulfide bonds
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Proteins
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Substrates: implicated in the biosynthesis of secretory proteins
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Proteins
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Substrates: may play a role in the formation of disulfide bonds in extracellular and periplasmic proteins
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Proteins
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Substrates: native, reduced or with wrong disulfide bonds
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Proteins
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Substrates: when present in large stoichiometric excess relative to an unfolded protein substrate, the enzyme can exhibit chaperone activity, inhibiting aggregation and increasing the recovery of native protein
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Proteins
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Substrates: may play a role in the formation of disulfide bonds in extracellular and periplasmic proteins
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Proteins
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Substrates: native, reduced or with wrong disulfide bonds
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Proteins
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Substrates: enzyme may be involved in the formation of intra-chain and inter-chain disulfide bonds in procollagen
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Proteins
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Substrates: may play a role in the formation of disulfide bonds in extracellular and periplasmic proteins
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Proteins
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Substrates: native, reduced or with wrong disulfide bonds
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Proteins
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Substrates: may play a role in the formation of disulfide bonds in extracellular and periplasmic proteins
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Proteins
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Substrates: native, reduced or with wrong disulfide bonds
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Proteins
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Substrates: may play a role in the formation of disulfide bonds in extracellular and periplasmic proteins
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Proteins
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Substrates: native, reduced or with wrong disulfide bonds
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Proteins
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Substrates: proposed physiological role as catalyst of formation of native disulfide bonds in nascent and newly synthesized secretory proteins
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Proteins
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Substrates: involved in cotranslational disulfide bond formation
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Proteins
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Substrates: native, reduced or with wrong disulfide bonds
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Proteins
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Substrates: implicated in the biosynthesis of secretory proteins
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Proteins
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Substrates: may play a role in the formation of disulfide bonds in extracellular and periplasmic proteins
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Proteins
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Substrates: native, reduced or with wrong disulfide bonds
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Proteins
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Substrates: involved in the assembly of wheat storage proteins within the endoplasmic reticulum
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Proteins
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Substrates: plays a role in the formation of disulfide bonds during biosynthesis of wheat storage proteins
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Proteins
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Substrates: native, reduced or with wrong disulfide bonds
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tissue factor
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Substrates: PDI switches tissue factor from coagulation to signaling by targeting the allosteric Cys186-Cys209 disulfide, the tissue factor coagulant function is enhanced by protein-disulfide isomerase independent of oxidoreductase activity, the chaperone activity is sufficient, PDI enhances factor VIIa-dependent substrate factor X activation 5-10fold in the presence of wild-type, oxidized soluble TF but not TF mutants that contain an unpaired Cys186 or Cys209, PDI has no effect on fully active TF on either negatively charged phospholipids or in activating detergent, indicating that PDI selectively acts upon cryptic TF to facilitate ternary complex formation and macromolecular substrate turnover, overview
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additional information
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Substrates: PDI has an important function in the correct folding of nascent polypeptides, which is a crucial step in the mechanism which delivers tick proteins to the secretion pathway important for blood feeding
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additional information
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Substrates: PDI has an important function in the correct folding of nascent polypeptides, which is a crucial step in the mechanism which delivers tick proteins to the secretion pathway important for blood feeding
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additional information
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Substrates: the cotyledon-specific chloroplast biogenesis factor CYO1 is a protein disulfide isomerase and has a chaperone-like activity required for thylakoid biogenesis in cotyledons, mutation of Cyo1 affects the photosynthesis in cotyledons, overview
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additional information
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Substrates: the cotyledon-specific chloroplast biogenesis factor CYO1 is a protein disulfide isomerase and has a chaperone-like activity required for thylakoid biogenesis in cotyledons, mutation of Cyo1 affects the photosynthesis in cotyledons, overview
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additional information
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Substrates: structure and mechanism of PDI in disulfide formation and oxidative protein folding, overview
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additional information
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Substrates: the enzyme may be significant in the action of triiodothyronine towards the target cells
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additional information
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Substrates: modeling of disulfide formation, the enzyme catalyzes disulfide formation and isomerization and acts as a chaperone inhibiting aggregation, enzyme assists in the system of chaperones and folding catalysts to ensure proper connection of disulfides and protein folding without improper interactions, mechanism of incorrect disulfide recognition
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additional information
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Substrates: PDI is able to renature reduced-denatured RNase. Plasma transglutaminase-coagulation factor XIII, FXIII, also shows PDI activity with reduced-denatured RNase, its PDI activity is located on the A subunit
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additional information
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Substrates: PDI is a multifunctional protein required for many aspects of protein folding and transit through the endoplasmic reticulum, the PDI activity is essential for viability, collagen biogenesis and extracellular matrix formation, PDI-2 is required for the normal function of prolyl 4-hydroxylase, a key collagen-modifying enzyme, overview, PDI-2 is required for normal post-embryonic development, all isozymes are synergistically essential for embryonic development in this nematode
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additional information
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Substrates: PDI is a multifunctional protein required for many aspects of protein folding and transit through the endoplasmic reticulum, the PDI activity is essential for viability, collagen biogenesis and extracellular matrix formation, overview, all isozymes are synergistically essential for embryonic development in this nematode
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additional information
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Substrates: RB60 is an atypical PDI that functions as a member of a redox regulatory protein complex controlling translation in the chloroplast, the enzyme is essential in the endoplasmic reticulum
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additional information
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Substrates: RB60 is involved in the light-regulated translation of the psbA mRNA in the chloroplast of the unicellular alga Chlamydomonas reinhardtii, light controls the redox regulation of RB47 function via the coupling of RB47 and RB60 redox states, overview
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additional information
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Substrates: structure and mechanism of PDI in disulfide formation and oxidative protein folding, overview
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additional information
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Substrates: RB60 is an atypical PDI that functions as a member of a redox regulatory protein complex controlling translation in the chloroplast, the enzyme is essential in the endoplasmic reticulum
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additional information
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Substrates: in vivo, disulfide bond formation is mainly catalyzed by protein disulfide isomerase
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additional information
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Substrates: in vivo, disulfide bond formation is mainly catalyzed by protein disulfide isomerase
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additional information
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Substrates: the enzyme is involved in diphtheria toxin sensitivity and is required for toxin entry, Chlamydia trachomatis or Chlamydia psittaci, intracellular pathogens of humans, require the enzyme for attachment to mammalian CHO6 cells, host cell invasion is obligatory for survival, growth and pathogenesis, overview
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additional information
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Substrates: the PDI protein is necessary for Chlamydia attachment, but the bacteria apparently do not bind directly to cell-associated PDI, suggesting that Chlamydia attaches to a host protein(s) associated with PDI. PDI enzymatic activity is necessary for bacterial entry but not for attachment, cell surface PDI-mediated reduction triggers Chlamydia entry into cells, molecular mechanism, overview
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additional information
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Substrates: the enzyme plays a crucial role in folding periplasmatically excreted proteins
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additional information
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Substrates: DsbC resolves incorrect disulfides whose formation has been catalyzed by redox-active copper
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additional information
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Substrates: the enzyme catalyzes disulfide formation and isomerization and acts as a chaperone inhibiting aggregation, enzyme assists in the system of chaperones and folding catalysts to ensure proper connection of disulfides and protein folding without improper interactions
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additional information
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Substrates: DsbB is an integral membrane protein responsible for the de novo synthesis of disulfide bonds in the Escherichia coli periplasm, disulfide bond formation is catalyzed by the DsbA/DsbB system, DsbA is critical for catalyzing disulfide bond formation in proteins in the bacterial periplasm, which it accomplishes by directly oxidizing substrate proteins via dithiol-disulfide exchange, DsbA donates its disulfide bond directly to substrate proteins, in the process of transferring electrons from DsbA to a tightly bound ubiquinone cofactor, DsbB undergoes an unusual spectral transition, DsbA must be reoxidized by an electron acceptor, mechanism, overview
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additional information
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Substrates: PDI oxidizes pairs of cysteines to form disulfide bonds and can also shuffle incorrect disulfides into their correct pairings, function and mechanism of PDI, bacterial machinery for disulfide formation and oxidative protein folding, overview
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additional information
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Substrates: PDI is a subunit of the enzyme prolyl-4-hydroxylase, which catalyzes the formation of 4-hydroxyprolyl residues in nascent collagen-like polypeptides. PDI is also a subunit of a triacylglycerol transfer protein, which facilitates the incorporation of lipids into newly synthesized core lipoproteins within the endoplasmic reticulum. The function of PDI is to maintain the alpha-subunit of this enzyme in an active form
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additional information
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Substrates: the enzyme acts as a thyroid-hormone binding protein
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additional information
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Substrates: the enzyme plays important roles in the folding of nascent polypeptides and the formation of disulfide bonds in the endoplasmic reticulum, PDIS-1 associates with proglycinin, a precursor of the seed storage protein glycinin, in the cotyledon, seed-dependent aggregation of amyloid beta-peptide (1-40) monomers is inhibited by both PDIS-1 and PDIS-2, both are involved in seed development, overview
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additional information
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Substrates: enzyme is involved in the proper folding or quality control of storage proteins
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additional information
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Substrates: GmPDIL-1 and GmPDIL-2 function as molecular chaperones, and prevent the aggregation of unfolded rhodanese, while GmPDIL-3a and GmPDIL-3b do not
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additional information
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Substrates: HlPDI-1 might be involved in tick blood feeding and Babesia parasite infection in ticks
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additional information
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Substrates: HlPDI-1 might be involved in tick blood feeding and Babesia parasite infection in ticks
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additional information
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Substrates: HlPDI-1 might be involved in tick blood feeding and Babesia parasite infection in ticks
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additional information
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Substrates: HlPDI-1 might be involved in tick blood feeding and Babesia parasite infection in ticks
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additional information
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Substrates: HlPDI-3 might be involved in tick blood feeding and Babesia parasite infection in ticks
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additional information
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Substrates: HlPDI-3 might be involved in tick blood feeding and Babesia parasite infection in ticks
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additional information
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Substrates: HlPDI-3 might be involved in tick blood feeding and Babesia parasite infection in ticks
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additional information
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Substrates: HlPDI-3 might be involved in tick blood feeding and Babesia parasite infection in ticks
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additional information
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Substrates: protein disulfide isomerases are involved in blood feeding, viability and oocyte development, probably by mediating the formation of disulfide bond-containing proteins of the ticks and the formation of basement membrane and cuticle components such as extracellular matrix
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additional information
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Substrates: protein disulfide isomerases are involved in blood feeding, viability and oocyte development, probably by mediating the formation of disulfide bond-containing proteins of the ticks and the formation of basement membrane and cuticle components such as extracellular matrix
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additional information
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Substrates: protein disulfide isomerases are involved in blood feeding, viability and oocyte development, probably by mediating the formation of disulfide bond-containing proteins of the ticks and the formation of basement membrane and cuticle components such as extracellular matrix
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additional information
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Substrates: protein disulfide isomerases are involved in blood feeding, viability and oocyte development, probably by mediating the formation of disulfide bond-containing proteins of the ticks and the formation of basement membrane and cuticle components such as extracellular matrix
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additional information
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Substrates: modeling of disulfide formation, the enzyme catalyzes disulfide formation and isomerization and acts as a chaperone inhibiting aggregation, enzyme assists in the system of chaperones and folding catalysts to ensure proper connection of disulfides and protein folding without improper interactions, the pancreatic enzyme is responsible for folding of a subset of secreted pancreatic zymogens
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additional information
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Substrates: the enzyme is involved in correct disulfide bond formation in secretory proteins as a key step in endoplasmic reticulum quality control, ERp57 works in conjunction with the endoplasmic reticulum lectin-like chaperones calnexin and calreticulin via the noncatalytic b' domain of the enzyme, the b' domains of ERp57 and PDI are very different, overview
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additional information
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Substrates: the enzyme is involved in correct disulfide bond formation in secretory proteins as a key step in endoplasmic reticulum quality control, ERp57 works in conjunction with the endoplasmic reticulum lectin-like chaperones calnexin and calreticulin via the noncatalytic b' domain of the enzyme, the b' domains of ERp57 and PDI are very different, overview
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additional information
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Substrates: the enzyme is involved in correct disulfide bond formation in secretory proteins as a key step in endoplasmic reticulum quality control, ERp57 works in conjunction with the endoplasmic reticulum lectin-like chaperones calnexin and calreticulin via the noncatalytic b' domain of the enzyme, the b' domains of ERp57 and PDI are very different, overview
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additional information
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Substrates: the enzyme is involved in correct disulfide bond formation in secretory proteins as a key step in endoplasmic reticulum quality control, ERp57 works in conjunction with the endoplasmic reticulum lectin-like chaperones calnexin and calreticulin via the noncatalytic b' domain of the enzyme, the b' domains of ERp57 and PDI are very different, overview
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additional information
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Substrates: the enzyme mediates rapid delivery of NO signalling into human platelets from the S-nitrosothiol compound S-nitrosoglutathione, NO delivery is blocked by inhibition of PDI, overview
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additional information
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Substrates: PDI has two distinct functions: acting as a molecular chaperone to maintain properly folded proteins and regulating the redox state of proteins by catalyzing the thiol-disulfide exchange reaction through two thioredoxin-like domains
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additional information
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Substrates: PDIis responsible for correct disulfide bond formation of proteins in the endoplasmic reticulum, it recognize unfolded proteins and can be selective for specific proteins or classes
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additional information
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Substrates: structure and mechanism of PDI in disulfide formation and oxidative protein folding, overview
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additional information
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Substrates: PDI can function as a high-capacity intracellular 17beta-estradiol-binding protein that increases the concentration and accumulation of 17beta-estradiol in live cells. The intracellular PDI-bound 17beta-estradiol can be released from PDI upon a drop in 17beta-estradiol levels and the released 17beta-estradiol can augment estrogen receptor-mediated transcriptional activity and mitogenic actions in cultured cells. The binding of 17beta-estradiol by PDI also reduces the rate of metabolic disposition of this hormone
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additional information
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Substrates: protein disulfide isomerase contributes to the activation of cryptic initiator protein tissue factoron microvesicles in vitro
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additional information
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Substrates: protein disulfide isomerase PDI directly interacts with thiol-containing fibrinogen receptor alphaIIbbeta3. PDI has greater ability to isomerize disulfide bonds than the alphaIIbbeta3 integrin
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additional information
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Substrates: the PDI protein is necessary for Chlamydia attachment, but the bacteria apparently do not bind directly to cell-associated PDI, suggesting that Chlamydia attaches to a host protein(s) associated with PDI. PDI enzymatic activity is necessary for bacterial entry but not for attachment, cell surface PDI-mediated reduction triggers Chlamydia entry into cells, molecular mechanism, overview
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additional information
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Substrates: ER protein 57, ERP-57, also known as PDIA3, has disulfide oxidoreductase and isomerase activity. ERP-57 interacts with calnexin, CANX, a chaperone protein and a lectin that binds glycoproteins through a transient oligosaccharide intermediate, thought to prevent a rapid degradation, as well as endoplasmic reticulum retention, of misfolded proteins, overview
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additional information
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Substrates: PDI catalyzes disulfide bond formation in the endoplasmic reticulum
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additional information
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Substrates: PDI catalyzes disulfide bond formation in the endoplasmic reticulum
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additional information
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Substrates: PDI specifically binds 3,3',5-triiodo-L-thyronine
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additional information
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Substrates: PDIp also shows chaperone activity in preventing the aggregation of reduced insulin B chain and denatured D-glyceraldehyde-3-phosphate dehydrogenase, PDIp can form stable complexes with thermal-denatured substrate proteins, e.g. MCF-7 cellular proteins, independently of their enzymatic activity. The b-b' fragment of PDIp, which does not contain the active sites and is devoid of enzymatic activity, still has chaperone activity
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additional information
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Substrates: PDIp also shows chaperone activity in preventing the aggregation of reduced insulin B chain and denatured D-glyceraldehyde-3-phosphate dehydrogenase, PDIp can form stable complexes with thermal-denatured substrate proteins, e.g. MCF-7 cellular proteins, independently of their enzymatic activity. The b-b' fragment of PDIp, which does not contain the active sites and is devoid of enzymatic activity, still has chaperone activity
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additional information
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Substrates: PDI specifically associates with signal peptide peptidase, SPP, independently of human cytomegalovirus glycoprotein US2, but not with Derlin-1
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additional information
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Substrates: the enzyme has a single E2-binding site
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additional information
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Substrates: the enzyme has three catalytic activities including thiol-disulfide oxireductase, disulfide isomerase, and redox-dependent chaperone
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additional information
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Substrates: TXNDC5 directly interacts with Srx through its thioredoxin-like domains, binding and in vivo complexing analysis. The Srx-TXNDC5 interaction is not affected by the treatment of cells with exogenous H2O2
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additional information
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Substrates: TXNDC5 directly interacts with Srx through its thioredoxin-like domains, binding and in vivo complexing analysis. The Srx-TXNDC5 interaction is not affected by the treatment of cells with exogenous H2O2
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additional information
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Substrates: the enzyme has a single E2-binding site
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additional information
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Substrates: protein disulfide isomerase serves as a subunit of at least two enzymes, the beta-subunit of the enzyme prolyl hydroxylase and an ER triglyceride transferase
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additional information
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Substrates: PDILT forms intermolecular disulfide bonds in testis
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additional information
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Substrates: sperm surface protein disulfide isomerase activity plays a role in gamete fusion and sperm-egg interaction, the enzyme mediates conformational changes by thiol-disulfide exchange in fusion-active proteins, participation of ERp57, overview
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additional information
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Substrates: PDI is required in vivo for both fibrin generation and platelet thrombus formation
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additional information
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Substrates: protein disulfide isomerase directly promotes initiator protein tissue factor-dependent fibrin production during thrombus formation in vivo
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additional information
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Substrates: PDIA1, and probably also PDIA3, shows cytotoxic regulatory protein 2, CxRP2, activity in T-cells, acting as perforin inhibitor associated with cytotoxic T cell granules, overview. Perforin is a membrane-permeabilizing protein important to T cell cytotoxic action
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additional information
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Substrates: AGR2 is essential for production of intestinal mucin MUC2, but is not required for establishment of intestinal secretory epithelial cell lineages
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additional information
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Substrates: PDI specifically binds 3,3',5-triiodo-L-thyronine
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additional information
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Substrates: PDIA1, and probably also PDIA3, shows cytotoxic regulatory protein 2, CxRP2, activity in T-cells, acting as perforin inhibitor associated with cytotoxic T cell granules, overview. Perforin is a membrane-permeabilizing protein important to T cell cytotoxic action
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additional information
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Substrates: PDI is a major protein in the endoplasmic reticulum, operating as an essential folding catalyst and molecular chaperone for disulfide-containing proteins by catalyzing the formation, rearrangement, and breakage of their disulfide bridges
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additional information
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Substrates: the enzyme is involved in the oxidative folding of cystine knot defense proteins and in in the biosynthesis of insecticidal cyclotides, overview, the Oldenlandia affinis plant accumulates knotted circular proteins called cyclotides
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additional information
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Substrates: the enzyme assists protein folding in malaria parasites
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additional information
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Substrates: the enzyme assists protein folding in malaria parasites
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additional information
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Substrates: the enzyme assists protein folding in malaria parasites
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additional information
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Substrates: the enzyme assists protein folding in malaria parasites
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additional information
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Substrates: the enzyme assists protein folding in malaria parasites
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additional information
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Substrates: the enzyme assists protein folding in malaria parasites
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additional information
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Substrates: the enzyme assists protein folding in malaria parasites
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additional information
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Substrates: the enzyme assists protein folding in malaria parasites
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additional information
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Substrates: the enzyme assists protein folding in malaria parasites
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additional information
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Substrates: the enzyme assists protein folding in malaria parasites
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additional information
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Substrates: the enzyme assists protein folding in malaria parasites
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additional information
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Substrates: DsbA and DsbC are involved in disulfide bond formation and play an important role in the formation of extracellular enzymes, DsbA is important in lipase stability and excretion
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additional information
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Substrates: PDI has dehydroascorbate reductase activity, PDI may play a role in the intraluminal dehydroascorbate reduction
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additional information
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Substrates: modeling of disulfide formation, the enzyme catalyzes disulfide formation and isomerization and acts as a chaperone inhibiting aggregation, enzyme assists in the system of chaperones and folding catalysts to ensure proper connection of disulfides and protein folding without improper interactions
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additional information
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Substrates: PDI is a multifunctional protein that is critically involved in the folding, assembly, and shedding of many cellular proteins via its isomerase activity in addition to being considered to function as an intracellular hormone reservoir
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additional information
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Substrates: cell-surface PDI is required for transnitrosation of metallothionein by S-nitroso-albumin in intact pulmonary vascular endothelial cells, overview
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additional information
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Substrates: PDI possesses an anomalously low thiol pKa and is fine-tuned to catalyze oxidative folding in the lumen of the endoplasmic reticulum where the ambient pH of about 7 would otherwise retard thioldisulfide exchange reactions and hinder acquisition of the native fold
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additional information
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Substrates: PDIA1, and probably also PDIA3, shows cytotoxic regulatory protein 2, CxRP2, activity in T-cells, acting as perforin inhibitor associated with cytotoxic T cell granules, overview. Perforin is a membrane-permeabilizing protein important to T cell cytotoxic action
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additional information
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Substrates: PDI is a catalyst of isomerization of substrate protein intra- and extramolecular disulfide bridges and also has 3,3',5-triiodo-L-thyronine-binding activity and molecular chaperone-like activity
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additional information
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Substrates: the oxidoreductase chaperone PDI has an effect on the critical structure-forming step during the oxidative maturation of model disulfide-bond-containing proteins, it inhibits the conformational folding step of oxidative fold maturation and, therefore, has limited overall catalytic efficiency as an oxidoreductase chaperone, impact of rat PDI, null PDI and enzyme domains on the structure-forming step, overview. Detrimental impact of the oxidoreductase activity PDI during conformational folding include peptidyl prolyl isomerase which facilitates cis-trans isomerization of prolines
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additional information
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Substrates: PDI specifically binds 3,3',5-triiodo-L-thyronine
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additional information
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Substrates: the enzyme has an essential role that is distinct from its function in formation of native disulphides
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additional information
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Substrates: the enzyme is an essential catalyst of disulfide formation with two cysteines in the active site facilitating thiol-disulfide exchange
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additional information
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Substrates: essential enzyme for yeast cell growth, both oxidase and isomerase activities are required
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additional information
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Substrates: PDI plays a key role in catalyzing the folding of secretory proteins
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additional information
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Substrates: the organism is completely dependent on PDI activity for growth
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additional information
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Substrates: regulation of PDI and PDI homologues activities, in vivo isomerase activity depends only on full-length PDI, not on PDI-homologues, modeling of disulfide formation, the enzyme catalyzes disulfide formation and isomerization and acts as a chaperone inhibiting aggregation, enzyme assists in the system of chaperones and folding catalysts to ensure proper connection of disulfides and protein folding without improper interactions
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additional information
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Substrates: structure and mechanism of PDI in disulfide formation and oxidative protein folding, overview
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additional information
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Substrates: structure and mechanism of PDI in disulfide formation and oxidative protein folding, overview
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additional information
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Substrates: interactions between the C-terminal domain of Mnl1p and PDI, which include an intermolecular disulfide bond, are essential for subsequent introduction of a disulfide bond into the mannosidase homology domain of Mnl1p by PDI. This disulfide bond is essential for the ER-associated degradation activity of Mnl1p and in turn stabilizes the prolonged association of PDI with Mnl1p
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additional information
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Substrates: the organism is completely dependent on PDI activity for growth
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additional information
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Substrates: interactions between the C-terminal domain of Mnl1p and PDI, which include an intermolecular disulfide bond, are essential for subsequent introduction of a disulfide bond into the mannosidase homology domain of Mnl1p by PDI. This disulfide bond is essential for the ER-associated degradation activity of Mnl1p and in turn stabilizes the prolonged association of PDI with Mnl1p
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additional information
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Substrates: PDI is involved in the cellular growth and response to nutritional and oxidative stress, regulation, overview
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additional information
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Substrates: PDI is involved in the cellular growth and response to nutritional and oxidative stress, regulation, overview
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additional information
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Substrates: PDI is involved in the cellular growth and response to nutritional and oxidative stress, regulation, overview
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additional information
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Substrates: both chaperone and isomerase functions of PDI are essential for acceleration of the oxidative refolding and reactivation of dimeric alkaline protease inhibitor API, PDI acts as isomerase/chaperone for a few monomeric proteins assisting in disulfide bond formation and rearrangement of secreted proteins
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Substrates: both chaperone and isomerase functions of PDI are essential for acceleration of the oxidative refolding and reactivation of dimeric alkaline protease inhibitor API, PDI acts as isomerase/chaperone for a few monomeric proteins assisting in disulfide bond formation and rearrangement of secreted proteins
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Substrates: PDIA3 shows chaperone activity to promote oxidative refolding of reduced denatured lysozyme, meanwhile PDI-P5 exhibits anti-chaperone activity to inhibit oxidative refolding of lysozyme at an equimolar ratio
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Substrates: PDIA3 shows chaperone activity to promote oxidative refolding of reduced denatured lysozyme, meanwhile PDI-P5 exhibits anti-chaperone activity to inhibit oxidative refolding of lysozyme at an equimolar ratio
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Substrates: the single domain PDI-1 and the class 1 PDI-2 are not essential for the organism
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additional information
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Substrates: the single domain PDI-1 and the class 1 PDI-2 are not essential for the organism
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ATP
-
for the ATPase activity, binding of ATP does not alter the enzyme's conformation, binding structure
ubiquinone
-
tightly bound ubiquinone cofactor, which becomes oxidized to hydroquinone and is regenerated by the electron transport chain and O2PDI contains four transmembrane helices that surround the bound ubiquinone cofactor, overview
additional information
-
glutathione is used in vitro as redox system
-
glutathione
-
at physiological concentrations of GSSG, the rate-limiting step for the oxidation of the active site of PDI by GSSG is the nucleophilic attack by the C-terminal active-site cysteine on the reduced glutathione (GSH)-PDI mixed disulfide
thioredoxin
-
the enzymes PDI, P5, ERp72, ERp46 and ERp18 contains a thioredoxin binding site and the CGHC active site
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Cu2+
Mg2+
Mn2+
Zn2+
additional information
Ca2+
-
recombinant ECaST/PDI binds 26 mol of Ca2+/mol of protein with a Kd of 2.8 mM, 1-5 mM Ca2+ augments the reactivation of rBPTI
Ca2+
-
the enzyme is a major calcium binding protein of the endoplasmic reticulum via acidic residues
Ca2+
-
enzyme binds 19 mol Ca2+ per mol of protein with low affinity, which is reduced by increasing the ionic strength. Ca2+ induces conformational changes
Ca2+
-
1-5 mM Ca2+ augments the reactivation of reduced bovine pancreatic trypsin inhibitor
Cu2+
-
PDI binds a maximum of 4 mol Cu2+ and is able to reduce it to Cu+, the bound Cu+ is surface-exposed
Mn2+
-
modulates the thiol isomerase activity of protein disulfide isomerase that is bound to integrin alphaVbeta3 and induces its transition to the ligand-competent state
additional information
-
enzyme requires divalent cations for ATPase activity, with descending specificity for Mg2+, Co2+, Ca2+, Cu2+, and Mn2+
additional information
-
Ca2+ and Mg2+ have no effect on the enzyme and do not influence Zn2+ effects
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(2E)-1-(2,4-dimethoxyphenyl)-3-(4-methoxyphenyl)prop-2-en-1-one
-
i.e. metochalcone
(2E)-1-(4-[[(diethylamino)oxy]sulfinyl]phenyl)-3-(3-hydroxyphenyl)prop-2-en-1-one
-
-
(2E)-1-(4-[[(dipentylamino)oxy]sulfinyl]phenyl)-3-(3-hydroxyphenyl)prop-2-en-1-one
-
-
(2E)-1-phenyl-3-[4-(4,4,5,5-tetramethyl-1,3,2-dioxaborolan-2-yl)phenyl]prop-2-en-1-one
-
-
(2E)-3-[4-hydroxy-2-methoxy-5-(2-methylbut-3-en-2-yl)phenyl]-1-(4-hydroxyphenyl)prop-2-en-1-one
-
i.e. licochalcone A
(5Z)-3-(4-methoxyphenyl)-5-[(5-nitrothiophen-2-yl)methylidene]-2-thioxo-1,3-thiazolidin-4-one
i.e. CCF642
1,1-bis(4-hydroxyphenyl)ethane
-
i.e.bisphenol E, 15% inhibition at 0.0125 mM
1,6-dimethyl-3-(4-nitrophenyl)pyrimido[5,4-e][1,2,4]triazine-5,7(1H,6H)-dione
-
-
1-(6-((4-fluorophenyl)(piperidin-1-yl)methyl)-7-hydroxybenzofuran-2-yl)ethanone
-
1-[(3-chloro-4-hydroxyphenyl)methyl]-N-ethyl-N-methyl-4-(2-phenoxyethyl)piperidine-4-carboxamide
i.e. bepristat
1-[(4-fluorophenyl)(6-hydroxy-1,3-benzodioxol-5-yl)methyl]-3-methylurea
-
1-[(6-hydroxy-1,3-benzodioxol-5-yl)(3,4,5-trimethoxyphenyl)methyl]-3-methylurea
-
1-[1,3,5-benzotrioxepin-7-yl(6-hydroxy-1,3-benzodioxol-5-yl)methyl]-3-methylurea
-
2',3,3',4',5'-pentachlorobiphenyl
-
strong inhibition of PDI 3,3',5-triiodo-L-thyronine-binding activity
2',3,3',5,5',6'-hexachlorobiphenyl
-
strong inhibition of PDI 3,3',5-triiodo-L-thyronine-binding activity
2,2-bis(4-hydroxyphenyl)propane
-
i.e. bisphenol A, 30% inhibition at 0.0125 mM
2-(2,6-dimethyl-4-[(1E)-3-[4-(methylsulfanyl)phenyl]-3-oxoprop-1-en-1-yl]phenoxy)-2-methylpropanoic acid
-
i.e. elafibranor
2-(2-carboxy-4-nitro-phenyl) disulfonyl-5-nitrobenzoic acid
i.e. NSC517871. Molecular docking simulation into the redox-active site, residues C37, G38, H39, C40. Inhibitor binds to hydrophobic amino acidsA34, W36, C37, C40, H39, T68 and F80. The redox inhibitory conformations are energetically and statistically favored
2-chloro-N-(2-([4-(octylamino)-6-(2-propyn-1-ylamino)-1,3,5-triazin-2-yl]amino)ethyl)acetamide
i.e. RB-11-ca
-
2-chloro-N-[2-([4-[methyl(4-phenylbutyl)amino]-6-[(prop-2-yn-1-yl)amino]-1,3,5-triazin-2-yl]amino)ethyl]acetamide
i.e. KSC-34
2-nitro-5-sulfo-sulfonyl-benzoic acid
molecular docking simulation into the redox-active site, residues C37, G38, H39, C40. Inhibitor binds to hydrophobic amino acidsA34, W36, C37, C40, H39, T68 and F80. The redox inhibitory conformations are energetically and statistically favored
2-Nitro-5-thiocyanobenzoic acid
molecular docking simulation into the redox-active site, residues C37, G38, H39, C40. Inhibitor binds to hydrophobic amino acidsA34, W36, C37, C40, H39, T68 and F80. The redox inhibitory conformations are energetically and statistically favored
2-[[4-(cyclopropanecarbonyl)piperazin-1-yl]methyl]-1,2-benzothiazol-3(2H)-one
-
potent, reversible inhibition
3-((4-fluorophenyl)(piperidin-1-yl)methyl)-5,6,7,8-tetrahydronaphthalen-2-ol
-
3-(3-methoxyphenyl)-1,6-dimethylpyrimido[5,4-e][1,2,4]triazine-5,7(1H,6H)-dione
-
-
3-(4-methoxyphenyl)-1,6-dimethylpyrimido[5,4-e][1,2,4]triazine-5,7(1H,6H)-dione
-
-
3-[(1E)-3-(4-[[(dibutylamino)oxy]sulfinyl]phenyl)-3-oxoprop-1-en-1-yl]benzonitrile
-
-
3-[(1E)-3-(4-[[(diethylamino)oxy]sulfinyl]phenyl)-3-oxoprop-1-en-1-yl]benzonitrile
-
-
3-[(1E)-3-(4-[[(dimethylamino)oxy]sulfinyl]phenyl)-3-oxoprop-1-en-1-yl]benzonitrile
-
-
3-[(1E)-3-(4-[[(dipentylamino)oxy]sulfinyl]phenyl)-3-oxoprop-1-en-1-yl]benzonitrile
-
-
3-[(1E)-3-(4-[[imino(phenyl)methoxy]sulfinyl]phenyl)-3-oxoprop-1-en-1-yl]benzonitrile
-
-
3-[(1E)-3-[4-hydroxy-3-(trifluoromethyl)phenyl]-3-oxoprop-1-en-1-yl]benzoic acid
-
-
3-[(1E)-3-[4-hydroxy-3-(trifluoromethyl)phenyl]-3-oxoprop-1-en-1-yl]benzonitrile
-
-
3-[(1E)-3-[4-[(4-nitrobenzene-1-sulfonyl)amino]phenyl]-3-oxoprop-1-en-1-yl]benzoic acid
-
-
4,4'-diisothiocyano-2,2'-stilbene disulfonic acid
-
considerably more effective after preincubation with DTT
4-amino-phenylarsine oxide
-
0.0058 mM, 50% inhibition of tyramine-S-S-poly(D-lysine) reduction
4-[(1E)-3-[4-hydroxy-3-(trifluoromethyl)phenyl]-3-oxoprop-1-en-1-yl]benzonitrile
-
-
5,5'-dithiobis(2-nitrobenzoic acid)
-
0.0049 mM, 50% inhibition of tyramine-S-S-poly(D-lysine) reduction
5-(3-carboxy-4-nitro-phenyl) sulfonyl-2-nitrobenzoic acid
i.e. NSC695265. Molecular docking simulation into the redox-active site, residues C37, G38, H39, C40. Inhibitor binds to hydrophobic amino acidsA34, W36, C37, C40, H39, T68 and F80. The redox inhibitory conformations are energetically and statistically favored
6-((2,2-difluorobenzo[d][1,3]dioxol-5-yl)(piperidin-1-yl)methyl)benzofuran-7-ol
-
6-((2,3-dimethoxyphenyl)(morpholino)methyl)-2,2-difluorobenzo[d][1,3]dioxol-5-ol
-
6-((4-fluorophenyl)(piperidin-1-yl)methyl)-2,3-dihydrobenzo[b][1,4]dioxin-5-ol
-
6-[(2,4-dimethoxyphenyl)(piperidin-1-yl)methyl]-2H-1,3-benzodioxol-5-ol
-
6-[(2-hydroxy-3-methoxyphenyl)(pyrimidin-2-ylamino)methyl]-1,3-benzodioxol-5-ol
-
6-[(2-hydroxy-3-methoxyphenyl)(pyrrolidin-1-yl)methyl]-1,3-benzodioxol-5-ol
-
6-[(2H,4H-1,3,5-benzotrioxepin-7-yl)(piperidin-1-yl)methyl]-2H-1,3-benzodioxol-5-ol
-
6-[(3,4-dimethoxyphenyl)(morpholin-4-yl)methyl]-1,3-benzodioxol-5-ol
covalent nanomolar inhibitor
6-[(3,4-dimethoxyphenyl)(piperidin-1-yl)methyl]-2H-1,3-benzodioxol-5-ol
-
6-[(3-hydroperoxy-2-hydroxyphenyl)(morpholin-4-yl)methyl]-1,3-benzodioxol-5-ol
-
6-[(4-hydroxy-3,5-dimethoxyphenyl)(pyridin-2-ylamino)methyl]-1,3-benzodioxol-5-ol
-
6-[(4-hydroxy-3,5-dimethoxyphenyl)(pyrimidin-2-ylamino)methyl]-1,3-benzodioxol-5-ol
-
6-[(4-hydroxy-3-methoxyphenyl)(morpholin-4-yl)methyl]-1,3-benzodioxol-5-ol
-
6-[(morpholin-4-yl)(2,4,6-trimethoxyphenyl)methyl]-2H-1,3-benzodioxol-5-ol
-
6-[(morpholin-4-yl)(3,4,5-trimethoxyphenyl)methyl]-2H-1,3-benzodioxol-5-ol
-
6-[(piperidin-1-yl)(3,4,5-trimethoxyphenyl)methyl]-2H-1,3-benzodioxol-5-ol
-
6-[(pyrrolidin-1-yl)(3,4,5-trimethoxyphenyl)methyl]-2H-1,3-benzodioxol-5-ol
-
6-[1,3,5-benzotrioxepin-7-yl(morpholin-4-yl)methyl]-1,3-benzodioxol-5-ol
-
6-[1,3,5-benzotrioxepin-7-yl(pyridin-2-ylamino)methyl]-1,3-benzodioxol-5-ol
-
6-[1,3,5-benzotrioxepin-7-yl(pyrimidin-2-ylamino)methyl]-1,3-benzodioxol-5-ol
-
6-[1,3,5-benzotrioxepin-7-yl(pyrrolidin-1-yl)methyl]-1,3-benzodioxol-5-ol
-
6-[[4-(dimethylamino)phenyl](piperidin-1-yl)methyl]-2H-1,3-benzodioxol-5-ol
-
6-[[4-(dimethylamino)phenyl](pyrrolidin-1-yl)methyl]-1,3-benzodioxol-5-ol
-
7-((4-fluorophenyl)(piperidin-1-yl)methyl)-2,3-dihydrobenzo[b][1,4]dioxin-6-ol
-
7-[(2,5-dimethylcyclohexa-1,3-dien-1-yl)[(4-methylpyridin-2-yl)amino]methyl]quinolin-8-ol
-
7-[(2,6-dichlorophenyl)[(4-methylpyridin-2-yl)amino]methyl]quinolin-8-ol
-
7-[(2-chloro-3-hydroxycyclohexa-1,3-dien-1-yl)(pyridin-2-ylamino)methyl]quinolin-8-ol
-
7-[(2-chloro-6-fluorophenyl)[(4-methylpyridin-2-yl)amino]methyl]quinolin-8-ol
-
7-[(2-fluorocyclohexa-1,3-dien-1-yl)(pyridin-2-ylamino)methyl]quinolin-8-ol
-
7-[(2-methylcyclohexa-1,3-dien-1-yl)[(4-methylpyridin-2-yl)amino]methyl]quinolin-8-ol
-
7-[(3-hydroxy-4-methoxyphenyl)[(4-methylpyridin-2-yl)amino]methyl]quinolin-8-ol
-
7-[(3-methoxycyclohexa-1,3-dien-1-yl)(pyridin-2-ylamino)methyl]quinolin-8-ol
-
7-[(4-hydroxy-3,5-dimethoxyphenyl)[(5-methylpyridin-2-yl)amino]methyl]quinolin-8-ol
-
7-[cyclohexa-1,3-dien-1-yl[(4-methylpyridin-2-yl)amino]methyl]quinolin-8-ol
-
7-[[(4-methylpyridin-2-yl)amino][4-(trifluoromethyl)phenyl]methyl]quinolin-8-ol
-
7-[[(pyridin-2-yl)amino](2,4,6-trimethylcyclohexa-1,3-dien-1-yl)methyl]quinolin-8-ol
-
Diazobenzene sulfonic acid
-
considerably more effective after preincubation with DTT
Dithionitrobenzoic acid
molecular docking simulation into the redox-active site, residues C37, G38, H39, C40. Inhibitor binds to hydrophobic amino acidsA34, W36, C37, C40, H39, T68 and F80. The redox inhibitory conformations are energetically and statistically favored
dithiothreitol
-
treatment decreases the content of 52 kDa isoform by half
E-64
-
0.01 mM, 11% inhibition after treatment with 0.01 mM DTT. No inhibition without DTT
ethyl N-[[[(cyanocarbonyl)(2,4-dimethoxyphenyl)amino]thiophen-2-yl]acetyl]glycinate
-
-
genistein
-
suppresses binding of proinsulin to PDI, inhibits 66% of PDIs chaperone activity
gentamycin
-
analysis of binding and dissociation constants with PDI and PDI domain deletion mutants
kanamycin
-
analysis of binding and dissociation constants with PDI and PDI domain deletion mutants
MA3 018
-
inhibition of protein disulfide isomerase. Treatment of Mn2+-treated endothelial cells abolishes the conversion of integrin alphaVbeta to the ligand-competent high-affinity state
-
MA3 019
-
inhibition of protein disulfide isomerase. Treatment of Mn2+-treated endothelial cells abolishes the conversion of integrin alphaVbeta to the ligand-competent high-affinity state
-
methyl 3-[(1E)-3-(4-[[(dibutylamino)oxy]sulfinyl]phenyl)-3-oxoprop-1-en-1-yl]benzoate
-
-
methyl 3-[(1E)-3-(4-[[(dipropylamino)oxy]sulfinyl]phenyl)-3-oxoprop-1-en-1-yl]benzoate
-
-
methyl 3-[(1E)-3-[3-bromo-4-(hydroxymethyl)phenyl]-3-oxoprop-1-en-1-yl]benzoate
-
-
methyl 3-[(1E)-3-[4-hydroxy-3-(trifluoromethyl)phenyl]-3-oxoprop-1-en-1-yl]benzoate
-
-
methyl 3-[(1E)-3-[4-[(4-nitrobenzene-1-sulfonyl)amino]phenyl]-3-oxoprop-1-en-1-yl]benzoate
-
-
methyl-methanethiosulfonate
-
abolishes PDI oxidoreductase but not chaperone activity
N-(4-(5,5-difluoro-1,3,7,9-tetramethyl-5H-4lambda4,5lambda4-dipyrrolo[1,2-c:2',1'-f][1,3,2]diazaborinin-10-yl)-N(2-(4-((6-hydroxybenzo[d][1,3]dioxol-5-yl)(piperidin-1-yl)methyl)benzamido)ethyl)benzamide
-
N-([4-[(2E)-3-(3-cyanophenyl)prop-2-enoyl]phenyl]methyl)-4-nitrobenzene-1-sulfonamide
-
-
N-([4-[(2E)-3-(3-hydroxyphenyl)prop-2-enoyl]phenyl]methyl)thiophene-2-carboxamide
-
-
N-([4-[(2E)-3-(3-hydroxyphenyl)prop-2-enoyl]phenyl]methyl)thiophene-2-sulfonamide
-
-
N-([4-[(2E)-3-(4-methoxyphenyl)prop-2-enoyl]phenyl]methyl)thiophene-2-carboxamide
-
-
N-([4-[(2E)-3-(4-methoxyphenyl)prop-2-enoyl]phenyl]methyl)thiophene-2-sulfonamide
-
-
N-acetylated-triiodothyronine
-
0.07 mM, 50% inhibition of tyramine-S-S-poly(D-lysine) reduction
N-Iodoacetyl-N'-(5-sulfo)-1-naphthyl-diaminoethane
-
incubation after pretreatment with DTT or GSH
neomycin
-
analysis of binding and dissociation constants with PDI and PDI domain deletion mutants
nitazoxanide thiazolide derivatives
-
PDI is inhibited by those thiazolides that also affected parasite proliferation
-
paromomycin
-
analysis of binding and dissociation constants with PDI and PDI domain deletion mutants
peptides
-
study of the inhibition of enzyme catalyzed reduction of insulin by GSH by peptides of various length and amino acid composition
prop-2-yn-1-yl 1-methyl-2-[[nitroso(phenyl)amino]acetyl]-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-1-carboxylate
reversible inhibitor. The compound is capable to moderately inhibit activity of the enzyme and S-nitrosylate the protein
S-nitrosocysteine
-
S-nitrosates endogenous or overexpressed PDI in HEK-293T cells
sisomycin
-
analysis of binding and dissociation constants with PDI and PDI domain deletion mutants
sodium (2Z)-2-(2H-1,3-benzodioxol-5-yl)-4-(4-methoxyphenyl)-4-oxo-3-[(3,4,5-trimethoxyphenyl)methyl]but-2-enoate
-
i.e. PD-156707
streptomycin
-
analysis of binding and dissociation constants with PDI and PDI domain deletion mutants
T8 inhibitors
-
class of weak enzyme inhibitors at moderately high concentrations, sensitize several cancer cell lines to etoposide treatments
-
thionitrobenzoic acid
molecular docking simulation into the redox-active site, residues C37, G38, H39, C40. Inhibitor binds to hydrophobic amino acidsA34, W36, C37, C40, H39, T68 and F80. The redox inhibitory conformations are energetically and statistically favored
Vancomycin
-
analysis of binding and dissociation constants with PDI and PDI domain deletion mutants
vincristine
-
inhibits chaperone activity but not isomerase activity of both isoforms PDI and P5 in vitro. A 100:1 molar ratio of vincristine to enzyme is sufficient to almost completely inhibit chaperone activity
zinc bacitracin
specific inhibition; specific inhibition; specific inhibition
[4-[(2E)-3-(3-hydroxyphenyl)prop-2-enoyl]phenyl]methyl thiophene-2-carboxylate
-
-
[4-[(2E)-3-(4-methoxyphenyl)prop-2-enoyl]phenyl]methyl thiophene-2-carboxylate
-
-
[5-[(3-methylbut-2-en-1-yl)oxy]-2-[(2E)-3-[4-[(3-methylbut-2-en-1-yl)oxy]phenyl]prop-2-enoyl]phenoxy]acetic acid
-
i.e. sofalcone
1,3,6-trimethylpyrimido[5,4-e] [1,2,4] triazine-5,7(1H,6H)-dione
-
i.e. 35G8, potent nanomolar inhibitor
1,3,6-trimethylpyrimido[5,4-e] [1,2,4] triazine-5,7(1H,6H)-dione
i.e. 35G8
1,3,6-trimethylpyrimido[5,4-e][1,2,4]triazine-5,7(1H,6H)-dione
-
i.e. NSC280172; potent nanomolar inhibitor
3,4-dichlorophenol
-
inhibits PDI 3,3',5-triiodo-L-thyronine binding activity
bacitracin
-
inhibition of protein disulfide isomerase results in enhanced stress response and apoptosis
bacitracin
-
inhibition of protein disulfide isomerase. Treatment of Mn2+-treated endothelial cells abolishes the conversion of integrin alphaVbeta to the ligand-competent high-affinity state
bacitracin
-
infusion of blood vessels inhibits platelet thrombus formation and fibrin generation
bisphenol A
-
i.e. 2,2-bis(4-hydroxyphenyl)propane, an endocrine disrupting chemical, inhibiting the enzyme's 3,3',5-triiodo-L-thyronine binding activity, its chaperone activity, and its isomerase activity, structural requirements, overview. Inhibits also PDI family members ERp57 and ERp72
bisphenol A
-
i.e. 2,2-bis(4-hydroxyphenyl)propane, an endocrine disrupting chemical, inhibiting the enzyme's 3,3',5-triiodo-L-thyronine binding activity, its chaperone activity, and its isomerase activity, structural requirements, overview
bisphenol A
-
i.e. 2,2-bis-(4-hydroxyphenyl) propane, BPA, binds to the enzyme and inhibits its enzymatic and hormone-binding activities
bisphenol A
-
halogenated derivatives of bisphenol A as well as bisphenol A itself bind to PDI and thereby suppress the oxidative refolding of reduced RNaseA by PDI
bisphenol A
-
i.e. 2,2-bis(4-hydroxyphenyl)propane, an endocrine disrupting chemical, inhibiting the enzyme's 3,3',5-triiodo-L-thyronine binding activity, its chaperone activity, and its isomerase activity, structural requirements, overview
ethyl N-[[(2,4-dimethoxyphenyl)(prop-2-ynoyl)amino](thiophen-2-yl)acetyl]glycinate
-
i.e. PACMA31
ethyl N-[[(2,4-dimethoxyphenyl)(prop-2-ynoyl)amino](thiophen-2-yl)acetyl]glycinate
i.e. PACMA31, irreversible inhibitor
iodoacetamide
alkylation of PDIp by iodoacetamide fully abolishes its enzymatic activity while it still retains most of its chaperone activity
iodoacetate
-
1 mM, almost complete inhibition after reduction with 0.01 mM DTT. No inhibition in absence of DTT
Pentachlorophenol
-
inhibits PDI 3,3',5-triiodo-L-thyronine binding activity
ribostamycin
-
aminoglycoside antibiotic, inhibits the chaperone activity of PDI, isomerase activity is not inhibited
ribostamycin
-
analysis of binding and dissociation constants with PDI and PDI domain deletion mutants
tetrabromobisphenyl A
-
TBBPA, inhibits PDI 3,3',5-triiodo-L-thyronine binding activity
tetrabromobisphenyl A
-
TBBPA, inhibits PDI 3,3',5-triiodo-L-thyronine binding activity
tetrabromobisphenyl A
-
TBBPA, inhibits PDI 3,3',5-triiodo-L-thyronine binding activity
tetrachlorobisphenyl A
-
TCBPA, inhibits PDI 3,3',5-triiodo-L-thyronine binding activity
tetrachlorobisphenyl A
-
TCBPA, inhibits PDI 3,3',5-triiodo-L-thyronine binding activity
tetrachlorobisphenyl A
-
TCBPA, inhibits PDI 3,3',5-triiodo-L-thyronine binding activity
additional information
-
in presence of light, the level of protein disulfide isomerase protein decreases by 80%
-
additional information
-
malonaldehyde bis(diethyl acetal) is a poor inhibitor, pH-dependency of inhibition by alkylating inhibitors and SH-reagents
-
additional information
-
pressure conditions at 400 MPa decrease the enzyme isomerase activity
-
additional information
-
both GmPDIL-3a and GmPDIL-3b are resistant to protease treatment in the absence of detergent, and are degraded when detergent is added
-
additional information
-
in absence of DTT, the enzyme, at a concentration above 0.001 mM, inhibits reactivation of creatinine kinase involving Cys36 and Cys295 of PDI
-
additional information
-
functional inhibition of protein disulfide isomerase by S-nitrosylation
-
additional information
no inhibition of PDI oxido-reductase activity with di(o-aminobenzyl)-labeled oxidized glutathione by DELTA-somatostatin
-
additional information
-
no inhibition of PDI oxido-reductase activity with di(o-aminobenzyl)-labeled oxidized glutathione by DELTA-somatostatin
-
additional information
-
although PDI can be protective against mutant SOD1 aggregation and toxicity, aberrant S-nitrosylation of critical active site cysteine residues likely inactivates the normal protective function of PDI in amyotrophic lateral sclerosis spinal cords
-
additional information
-
ribostamycin has very slight inhibitory effect on protein disulfide isomerase chaperone activity and no effect on both reductase and isomerase activities
-
additional information
no inhibition of CxPR2 activity by treatment with cysteine and serine protease inhibitors E-64 and DCI
-
additional information
-
although PDI can be protective against mutant SOD1 aggregation and toxicity, aberrant S-nitrosylation of critical active site cysteine residues likely inactivates the normal protective function of PDI in amyotrophic lateral sclerosis spinal cords
-
additional information
-
CxRP2 activity is partially depleted by immobilized RNK-16 granule proteins, no inhibition of CxPR2 activity by treatment with cysteine and serine protease inhibitors E-64 and DCI
-
additional information
-
no effects of nonhydroxylated biphenyls on 3,3',5-triiodo-L-thyronine binding
-
additional information
-
although PDI can be protective against mutant SOD1 aggregation and toxicity, aberrant S-nitrosylation of critical active site cysteine residues likely inactivates the normal protective function of PDI in amyotrophic lateral sclerosis spinal cords
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
calnexin
interacts with the enzyme via the b and b' domains, binding site and structure, overview
-
dichlorophenyl-1,1-dimethylurea
-
blocks the reduction of plastoquinone, resulting in 1.5- to 2fold increase in PDI content
DsbA
-
disulfide bond formation is catalyzed by the DsbA/DsbB system, DsbA is critical for catalyzing disulfide bond formation in proteins in the bacterial periplasm, which it accomplishes by directly oxidizing substrate proteins via dithiol-disulfide exchange, DsbA donates its disulfide bond directly to substrate proteins, in the process of transferring electrons from DsbA to a tightly bound ubiquinone cofactor, DsbA must be reoxidized by an electron acceptor, overview
-
phosphate
-
treatment of plants results in 1.5- to 2fold increase in PDI content
additional information
-
thioredoxin reductase activates PDI at pH 7.4, 37°C involving glutathione reduction and NADPH, the disulfide reduction activity of PDI-thioredoxin reductase is reduced
-
additional information
-
light controls the redox regulation of RB47 function via the coupling of RB47 and RB60 redox states
-
additional information
-
PDIS-1, but not PDIS-2, is induced under endoplasmic reticulum-stress conditions
-
additional information
blood feeding induces the expression of HlPDI-1 in both partially fed nymphs and adults, overview
-
additional information
blood feeding induces the expression of HlPDI-1 in both partially fed nymphs and adults, overview
-
additional information
blood feeding induces the expression of HlPDI-1 in both partially fed nymphs and adults, overview
-
additional information
-
blood feeding induces the expression of HlPDI-1 in both partially fed nymphs and adults, overview
-
additional information
blood feeding induces the expression of HlPDI-3 in both partially fed nymphs and adults, overview
-
additional information
blood feeding induces the expression of HlPDI-3 in both partially fed nymphs and adults, overview
-
additional information
blood feeding induces the expression of HlPDI-3 in both partially fed nymphs and adults, overview
-
additional information
-
blood feeding induces the expression of HlPDI-3 in both partially fed nymphs and adults, overview
-
additional information
-
the enzyme is present in untreated cells in an inactive S-nitrosylated form, which becomes activated following glutathione depletion via S-denitrosylation
-
additional information
-
PDI1 gene expression is stress-induced by over 2.5fold in response to e.g. reducing agents such as DTT, or to thiol-specific oxidizing agents such as diamide, other PDI gene homologues are also stress-induced
-
additional information
oxidaive stress by H2O2, and glucose deprivation or nitrogen starvation induce PDI enzyme expression
-
additional information
-
oxidaive stress by H2O2, and glucose deprivation or nitrogen starvation induce PDI enzyme expression
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0253
denatured-reduced lysozyme
-
pH 7.0, temperature not specified in the publication
-
0.0116
scrambled reoxidized lysozyme
-
pH 7.0, temperature not specified in the publication
-
0.46
mycothiol-coupled hydroxyethyl disulfide
recombinant mutant C24S, pH 7.6, 30°C
-
0.51
mycothiol-coupled hydroxyethyl disulfide
recombinant wild-type enzyme, pH 7.6, 30°C
-
33.69
mycothiol-coupled hydroxyethyl disulfide
recombinant mutant C21S, pH 7.6, 30°C
-
0.002
ribonuclease
-
dithiothreitol, with scrambled ribonuclease as substrate
-
additional information
additional information
-
Km for scrambled ribonuclease: 0.023 mg/ml
-
additional information
additional information
-
light scattering and fluorescence measurement kinetics of wild-type PDI and mutant abb'a' lacking the C-terminal domain c, overview
-
additional information
additional information
-
redox equilibrium measurements of wild-type and mutant C90A/C97A enzymes, determination of oxidase and isomerase activities
-
additional information
additional information
-
kinetics and kinetic mechanism of DsbB, overview
-
additional information
additional information
-
folding kinetics of linear and cyclic kalata B1
-
additional information
additional information
-
refolding reaction obeys almost first-order kinetics with respect to PDI concentration
-
additional information
additional information
-
kinetic analysis of the RB60-RB47 complex, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0009
mycothiol-coupled hydroxyethyl disulfide
recombinant mutant C21S, pH 7.6, 30°C
-
8.55
mycothiol-coupled hydroxyethyl disulfide
recombinant wild-type enzyme, pH 7.6, 30°C
-
11.37
mycothiol-coupled hydroxyethyl disulfide
recombinant mutant C24S, pH 7.6, 30°C
-
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000027
mycothiol-coupled hydroxyethyl disulfide
recombinant mutant C21S, pH 7.6, 30°C
-
16.77
mycothiol-coupled hydroxyethyl disulfide
recombinant wild-type enzyme, pH 7.6, 30°C
-
24.72
mycothiol-coupled hydroxyethyl disulfide
recombinant mutant C24S, pH 7.6, 30°C
-
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
pseudo-first-order and second-order kinetics
-
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00021
(2E)-1-(3-hydroxyphenyl)-3-[3-(pyridin-4-yl)phenyl]prop-2-en-1-one
Homo sapiens
-
at pH 7.0 and 37°C
0.00035
(2E)-1-(3-hydroxyphenyl)-3-[4-(pyridin-3-yl)phenyl]prop-2-en-1-one
Homo sapiens
-
at pH 7.0 and 37°C
0.00174
(2E)-1-(4-hydroxyphenyl)-3-(4-methoxyphenyl)prop-2-en-1-one
Homo sapiens
-
at pH 7.0 and 37°C
0.00167
(2E)-1-(4-hydroxyphenyl)-3-[2-(trifluoromethyl)phenyl]prop-2-en-1-one
Homo sapiens
-
at pH 7.0 and 37°C
0.00156
(2E)-1-(4-hydroxyphenyl)-3-[3-(trifluoromethyl)phenyl]prop-2-en-1-one
Homo sapiens
-
at pH 7.0 and 37°C
0.00256
(2E)-1-(4-hydroxyphenyl)-3-[4-(trifluoromethyl)phenyl]prop-2-en-1-one
Homo sapiens
-
at pH 7.0 and 37°C
0.00129
(2E)-1-(4-[[(diethylamino)oxy]sulfinyl]phenyl)-3-(3-hydroxyphenyl)prop-2-en-1-one
Homo sapiens
-
at pH 7.0 and 37°C
0.00081
(2E)-1-(4-[[(dipentylamino)oxy]sulfinyl]phenyl)-3-(3-hydroxyphenyl)prop-2-en-1-one
Homo sapiens
-
at pH 7.0 and 37°C
0.00957
(2E)-1-(pyrazin-2-yl)-3-[3-(trifluoromethyl)phenyl]prop-2-en-1-one
Homo sapiens
-
at pH 7.0 and 37°C
0.0022
(2E)-1-phenyl-3-[4-(4,4,5,5-tetramethyl-1,3,2-dioxaborolan-2-yl)phenyl]prop-2-en-1-one
Homo sapiens
-
at pH 7.0 and 37°C
0.0004
(2E)-3-(4-bromophenyl)-1-(3-hydroxyphenyl)prop-2-en-1-one
Homo sapiens
-
at pH 7.0 and 37°C
0.00023
(2E)-3-[4-(1H-benzimidazol-1-yl)phenyl]-1-(3-hydroxyphenyl)prop-2-en-1-one
Homo sapiens
-
at pH 7.0 and 37°C
0.00093
(E)-3-(3-(4-hydroxyphenyl)-3-oxoprop-1-en-1-yl)benzonitrile
Homo sapiens
-
at pH 7.0 and 37°C
-
0.000105
1,6-dimethylpyrimido[5,4-e][1,2,4]triazine-5,7(1H,6H)-dione
Homo sapiens
-
at pH 7.0 and 37°C
0.1
1-((4-fluorophenyl)(7-methoxybenzofuran-6-yl)methyl)piperidine
Homo sapiens
IC50 above 0.1 mM, at pH 7.0 and 37°C
0.00123
1-(6-((4-fluorophenyl)(piperidin-1-yl)methyl)-7-hydroxybenzofuran-2-yl)ethanone
Homo sapiens
at pH 7.0 and 37°C
0.03
1-[(4-fluorophenyl)(6-hydroxy-1,3-benzodioxol-5-yl)methyl]-3-methylurea
Homo sapiens
IC50 above 0.03 mM, at pH 7.0 and 37°C
0.04
1-[(6-hydroxy-1,3-benzodioxol-5-yl)(3,4,5-trimethoxyphenyl)methyl]-3-methylurea
Homo sapiens
IC50 above 0.04 mM, at pH 7.0 and 37°C
0.04
1-[(6-hydroxy-1,3-benzodioxol-5-yl)(4-hydroxyphenyl)methyl]urea
Homo sapiens
IC50 above 0.04 mM, at pH 7.0 and 37°C
0.04
1-[1,3,5-benzotrioxepin-7-yl(6-hydroxy-1,3-benzodioxol-5-yl)methyl]-3-methylurea
Homo sapiens
IC50 above 0.04 mM, at pH 7.0 and 37°C
0.03
2-(dimethylamino)-6-((4-fluorophenyl)(piperidin-1-yl)methyl)phenol
Homo sapiens
IC50 above 0.03 mM, at pH 7.0 and 37°C
0.1
3-((4-fluorophenyl)(piperidin-1-yl)methyl)-5,6,7,8-tetrahydronaphthalen-2-ol
Homo sapiens
IC50 above 0.1 mM, at pH 7.0 and 37°C
0.1
3-[(1E)-3-(3,4-dimethoxyphenyl)-3-oxoprop-1-en-1-yl]benzonitrile
Homo sapiens
-
at pH 7.0 and 37°C
0.0091
3-[(1E)-3-(3-fluoro-4-hydroxyphenyl)-3-oxoprop-1-en-1-yl]benzoic acid
Homo sapiens
-
at pH 7.0 and 37°C
0.00114
3-[(1E)-3-(3-fluoro-4-hydroxyphenyl)-3-oxoprop-1-en-1-yl]benzonitrile
Homo sapiens
-
at pH 7.0 and 37°C
0.1
3-[(1E)-3-(3-hydroxy-4-methoxyphenyl)-3-oxoprop-1-en-1-yl]benzoic acid
Homo sapiens
-
at pH 7.0 and 37°C
0.01093
3-[(1E)-3-(3-hydroxy-4-methoxyphenyl)-3-oxoprop-1-en-1-yl]benzonitrile
Homo sapiens
-
at pH 7.0 and 37°C
0.01019
3-[(1E)-3-(3-hydroxyphenyl)-3-oxoprop-1-en-1-yl]benzoic acid
Homo sapiens
-
at pH 7.0 and 37°C
0.00187
3-[(1E)-3-(3-hydroxyphenyl)-3-oxoprop-1-en-1-yl]benzonitrile
Homo sapiens
-
at pH 7.0 and 37°C
0.00813
3-[(1E)-3-(3-methoxyphenyl)-3-oxoprop-1-en-1-yl]benzonitrile
Homo sapiens
-
at pH 7.0 and 37°C
0.1
3-[(1E)-3-(4-aminophenyl)-3-oxoprop-1-en-1-yl]benzoic acid
Homo sapiens
-
at pH 7.0 and 37°C
0.5
3-[(1E)-3-(4-aminophenyl)-3-oxoprop-1-en-1-yl]benzonitrile
Homo sapiens
-
at pH 7.0 and 37°C
0.00166
3-[(1E)-3-(4-bromophenyl)-3-oxoprop-1-en-1-yl]benzonitrile
Homo sapiens
-
at pH 7.0 and 37°C
0.5
3-[(1E)-3-(4-chloro-3-fluorophenyl)-3-oxoprop-1-en-1-yl]benzonitrile
Homo sapiens
-
at pH 7.0 and 37°C
0.00237
3-[(1E)-3-(4-fluoro-2-hydroxyphenyl)-3-oxoprop-1-en-1-yl]benzonitrile
Homo sapiens
-
at pH 7.0 and 37°C
0.00115
3-[(1E)-3-(4-fluoro-3-hydroxyphenyl)-3-oxoprop-1-en-1-yl]benzonitrile
Homo sapiens
-
at pH 7.0 and 37°C
0.00272
3-[(1E)-3-(4-hydroxy-3-methoxyphenyl)-3-oxoprop-1-en-1-yl]benzonitrile
Homo sapiens
-
at pH 7.0 and 37°C
0.00085
3-[(1E)-3-(4-hydroxyphenyl)-3-oxoprop-1-en-1-yl]benzonitrile
Homo sapiens
-
at pH 7.0 and 37°C
0.5
3-[(1E)-3-(4-methoxyphenyl)-3-oxoprop-1-en-1-yl]benzonitrile
Homo sapiens
-
at pH 7.0 and 37°C
0.04 - 0.5
3-[(1E)-3-(4-nitrophenyl)-3-oxoprop-1-en-1-yl]benzoic acid
Homo sapiens
-
at pH 7.0 and 37°C
0.00134
3-[(1E)-3-(4-[[(dibutylamino)oxy]sulfinyl]phenyl)-3-oxoprop-1-en-1-yl]benzonitrile
Homo sapiens
-
at pH 7.0 and 37°C
0.00123
3-[(1E)-3-(4-[[(diethylamino)oxy]sulfinyl]phenyl)-3-oxoprop-1-en-1-yl]benzonitrile
Homo sapiens
-
at pH 7.0 and 37°C
0.00623
3-[(1E)-3-(4-[[(dimethylamino)oxy]sulfinyl]phenyl)-3-oxoprop-1-en-1-yl]benzonitrile
Homo sapiens
-
at pH 7.0 and 37°C
0.00016
3-[(1E)-3-(4-[[(dipentylamino)oxy]sulfinyl]phenyl)-3-oxoprop-1-en-1-yl]benzonitrile
Homo sapiens
-
at pH 7.0 and 37°C
0.00105
3-[(1E)-3-(4-[[imino(phenyl)methoxy]sulfinyl]phenyl)-3-oxoprop-1-en-1-yl]benzonitrile
Homo sapiens
-
at pH 7.0 and 37°C
0.5
3-[(1E)-3-oxo-3-(pyrazin-2-yl)prop-1-en-1-yl]benzonitrile
Homo sapiens
-
at pH 7.0 and 37°C
0.04 - 0.5
3-[(1E)-3-oxo-3-[4-(piperidin-4-yl)phenyl]prop-1-en-1-yl]benzoic acid
Homo sapiens
-
at pH 7.0 and 37°C
0.1
3-[(1E)-3-[4-(morpholin-4-yl)phenyl]-3-oxoprop-1-en-1-yl]benzoic acid
Homo sapiens
-
at pH 7.0 and 37°C
0.5
3-[(1E)-3-[4-(morpholin-4-yl)phenyl]-3-oxoprop-1-en-1-yl]benzonitrile
Homo sapiens
-
at pH 7.0 and 37°C
0.00409
3-[(1E)-3-[4-hydroxy-3-(trifluoromethyl)phenyl]-3-oxoprop-1-en-1-yl]benzoic acid
Homo sapiens
-
at pH 7.0 and 37°C
0.002
3-[(1E)-3-[4-hydroxy-3-(trifluoromethyl)phenyl]-3-oxoprop-1-en-1-yl]benzonitrile
Homo sapiens
-
at pH 7.0 and 37°C
0.004
3-[(1E)-3-[4-[(4-nitrobenzene-1-sulfonyl)amino]phenyl]-3-oxoprop-1-en-1-yl]benzoic acid
Homo sapiens
-
at pH 7.0 and 37°C
0.00664
3-[(1E)-3-[4-[(aminooxy)sulfinyl]phenyl]-3-oxoprop-1-en-1-yl]benzonitrile
Homo sapiens
-
at pH 7.0 and 37°C
0.00111
3-[(1E)-3-[4-[(anilinooxy)sulfinyl]phenyl]-3-oxoprop-1-en-1-yl]benzonitrile
Homo sapiens
-
at pH 7.0 and 37°C
0.00148
3-[[(8-hydroxyquinolin-7-yl)(phenyl)methyl]amino]benzoic acid
Homo sapiens
at pH 7.0 and 37°C
0.00029
4-((4-(1H-pyrrol-1-yl)phenyl)(piperidin-1-yl)methyl)-1H-indazol-5-ol
Homo sapiens
at pH 7.0 and 37°C
0.00035
4-((4-fluorophenyl)(piperidin-1-yl)methyl)-1H-indazol-5-ol
Homo sapiens
at pH 7.0 and 37°C
0.00181
4-((4-fluorophenyl)(piperidin-1-yl)methyl)-1H-indol-5-ol
Homo sapiens
at pH 7.0 and 37°C
0.1
4-((4-fluorophenyl)(piperidin-1-yl)methyl)benzo[d]thiazol-5-ol
Homo sapiens
IC50 above 0.1 mM, at pH 7.0 and 37°C
0.00052
4-((4-nitrophenyl)(piperidin-1-yl)methyl)-1H-indazol-5-ol
Homo sapiens
at pH 7.0 and 37°C
0.00083
4-(piperidin-1-yl(4-(pyrimidin-5-yl)phenyl)methyl)-1H-indazol-5-ol
Homo sapiens
at pH 7.0 and 37°C
0.00034
4-(piperidin-1-yl(4-(thiazol-2-yl)phenyl)methyl)-1H-indazol-5-ol
Homo sapiens
at pH 7.0 and 37°C
0.00071
4-(piperidin-1-yl(4-(trifluoromethyl)phenyl)methyl)-1H-indazol-5-ol
Homo sapiens
at pH 7.0 and 37°C
0.00021
4-[(1E)-3-(3-fluoro-4-hydroxyphenyl)-3-oxoprop-1-en-1-yl]benzonitrile
Homo sapiens
-
at pH 7.0 and 37°C
0.0018
4-[(1E)-3-(4-fluoro-2-hydroxyphenyl)-3-oxoprop-1-en-1-yl]benzonitrile
Homo sapiens
-
at pH 7.0 and 37°C
0.00183
4-[(1E)-3-(4-fluoro-3-hydroxyphenyl)-3-oxoprop-1-en-1-yl]benzonitrile
Homo sapiens
-
at pH 7.0 and 37°C
0.00074
4-[(1E)-3-(4-hydroxyphenyl)-3-oxoprop-1-en-1-yl]benzonitrile
Homo sapiens
-
at pH 7.0 and 37°C
0.00111
4-[(1E)-3-[4-hydroxy-3-(trifluoromethyl)phenyl]-3-oxoprop-1-en-1-yl]benzonitrile
Homo sapiens
-
at pH 7.0 and 37°C
0.0003
4-[[(8-hydroxyquinolin-7-yl)(phenyl)methyl]amino]benzoic acid
Homo sapiens
at pH 7.0 and 37°C
0.01
5-((4-fluorophenyl)(piperidin-1-yl)methyl)-2,3-dihydro-1H-inden-4-ol
Homo sapiens
IC50 above 0.01 mM, at pH 7.0 and 37°C
0.00057
5-((4-fluorophenyl)(piperidin-1-yl)methyl)benzo[d]thiazol-4-ol
Homo sapiens
at pH 7.0 and 37°C
0.00283
5-((4-fluorophenyl)(piperidin-1-yl)methyl)benzo[d][1,3]dioxol-4-ol
Homo sapiens
at pH 7.0 and 37°C
0.1
5-((4-fluorophenyl)(piperidin-1-yl)methyl)isoquinolin-6-ol
Homo sapiens
IC50 above 0.1 mM, at pH 7.0 and 37°C
0.03
5-((4-fluorophenyl)(piperidin-1-yl)methyl)quinolin-6-ol
Homo sapiens
IC50 above 0.03 mM, at pH 7.0 and 37°C
0.1
5-((4-fluorophenyl)(piperidin-1-yl)methyl)quinoxalin-6-ol
Homo sapiens
IC50 above 0.1 mM, at pH 7.0 and 37°C
0.0002
6-((2,2-difluorobenzo[d][1,3]dioxol-5-yl)(piperidin-1-yl)methyl)benzofuran-7-ol
Homo sapiens
IC50 above 0.0002 mM, at pH 7.0 and 37°C
0.00041
6-((2,3-dihydro-1H-inden-5-yl)(piperidin-1-yl)methyl)benzofuran-7-ol
Homo sapiens
at pH 7.0 and 37°C
0.00051
6-((2,3-dimethoxyphenyl)(morpholino)methyl)-2,2-difluorobenzo[d][1,3]dioxol-5-ol
Homo sapiens
at pH 7.0 and 37°C
0.00106
6-((2,3-dimethoxyphenyl)(morpholino)methyl)benzo[d][1,3]dioxol-5-ol
Homo sapiens
at pH 7.0 and 37°C
0.00107
6-((4-fluoro-2-hydroxyphenyl)(piperidin-1-yl)methyl)benzofuran-7-ol
Homo sapiens
at pH 7.0 and 37°C
0.03
6-((4-fluorophenyl)(piperidin-1-yl)methyl)-2,3-dihydro-1H-inden-5-ol
Homo sapiens
IC50 above 0.03 mM, at pH 7.0 and 37°C
0.00029
6-((4-fluorophenyl)(piperidin-1-yl)methyl)-2,3-dihydrobenzo[b][1,4]dioxin-5-ol
Homo sapiens
at pH 7.0 and 37°C
0.00056
6-((4-fluorophenyl)(piperidin-1-yl)methyl)benzofuran-7-ol
Homo sapiens
at pH 7.0 and 37°C
0.00701
6-((4-fluorophenyl)(piperidin-1-yl)methyl)indolin-5-ol
Homo sapiens
at pH 7.0 and 37°C
0.00061
6-((4-fluorophenyl)(piperidin-1-yl)methyl)isoquinolin-5-ol
Homo sapiens
at pH 7.0 and 37°C
0.00066
6-((4-fluorophenyl)(piperidin-1-yl)methyl)quinoxalin-5-ol
Homo sapiens
at pH 7.0 and 37°C
0.0029
6-(phenyl(piperidin-1-yl)methyl)benzo[d][1,3]dioxol-5-ol
Homo sapiens
at pH 7.0 and 37°C
0.0003
6-(piperidin-1-yl(4-(trifluoromethyl)phenyl)methyl)benzofuran-7-ol
Homo sapiens
at pH 7.0 and 37°C
0.0002
6-(piperidin-1-yl(pyridin-4-yl)methyl)benzofuran-7-ol
Homo sapiens
IC50 above 0.0002 mM, at pH 7.0 and 37°C
0.12
6-methylpyrimido[5,4-e][1,2,4]triazine-5,7(1H,6H)-dione
Homo sapiens
-
at pH 7.0 and 37°C
0.00259
6-[(2,4-dimethoxyphenyl)(piperidin-1-yl)methyl]-2H-1,3-benzodioxol-5-ol
Homo sapiens
at pH 7.0 and 37°C
0.00036
6-[(2,4-dimethoxyphenyl)(pyrrolidin-1-yl)methyl]-1,3-benzodioxol-5-ol
Homo sapiens
at pH 7.0 and 37°C
0.00902
6-[(2-hydroxy-3-methoxyphenyl)(pyrimidin-2-ylamino)methyl]-1,3-benzodioxol-5-ol
Homo sapiens
at pH 7.0 and 37°C
0.00165
6-[(2-hydroxy-3-methoxyphenyl)(pyrrolidin-1-yl)methyl]-1,3-benzodioxol-5-ol
Homo sapiens
at pH 7.0 and 37°C
0.00034
6-[(2-hydroxyphenyl)(morpholin-4-yl)methyl]-1,3-benzodioxol-5-ol
Homo sapiens
at pH 7.0 and 37°C
0.00033
6-[(2-methoxyphenyl)(morpholin-4-yl)methyl]-1,3-benzodioxol-5-ol
Homo sapiens
at pH 7.0 and 37°C
0.00035
6-[(2H,4H-1,3,5-benzotrioxepin-7-yl)(piperidin-1-yl)methyl]-2H-1,3-benzodioxol-5-ol
Homo sapiens
at pH 7.0 and 37°C
0.0003
6-[(3,4-dimethoxyphenyl)(morpholin-4-yl)methyl]-1,3-benzodioxol-5-ol
Homo sapiens
at pH 7.0 and 37°C
0.00096
6-[(3,4-dimethoxyphenyl)(piperidin-1-yl)methyl]-2H-1,3-benzodioxol-5-ol
Homo sapiens
at pH 7.0 and 37°C
0.0009
6-[(3-hydroperoxy-2-hydroxyphenyl)(morpholin-4-yl)methyl]-1,3-benzodioxol-5-ol
Homo sapiens
at pH 7.0 and 37°C
0.000092
6-[(4-chlorophenyl)(morpholin-4-yl)methyl]-1,3-benzodioxol-5-ol
Homo sapiens
at pH 7.0 and 37°C
0.00067
6-[(4-fluorophenyl)(1H-imidazol-1-yl)methyl]-1,3-benzodioxol-5-ol
Homo sapiens
at pH 7.0 and 37°C
0.00023
6-[(4-fluorophenyl)(morpholin-4-yl)methyl]-1,3-benzodioxol-5-ol
Homo sapiens
at pH 7.0 and 37°C
0.00027
6-[(4-fluorophenyl)(piperidin-1-yl)methyl]-2H-1,3-benzodioxol-5-ol
Homo sapiens
at pH 7.0 and 37°C
0.01272
6-[(4-fluorophenyl)(pyrimidin-2-ylamino)methyl]-1,3-benzodioxol-5-ol
Homo sapiens
at pH 7.0 and 37°C
0.0002
6-[(4-fluorophenyl)(pyrrolidin-1-yl)methyl]-1,3-benzodioxol-5-ol
Homo sapiens
IC50 above 0.0002 mM, at pH 7.0 and 37°C
0.00017
6-[(4-hydroxy-3,5-dimethoxyphenyl)(pyridin-2-ylamino)methyl]-1,3-benzodioxol-5-ol
Homo sapiens
at pH 7.0 and 37°C
0.0022
6-[(4-hydroxy-3,5-dimethoxyphenyl)(pyrimidin-2-ylamino)methyl]-1,3-benzodioxol-5-ol
Homo sapiens
at pH 7.0 and 37°C
0.0023
6-[(4-hydroxy-3-methoxyphenyl)(morpholin-4-yl)methyl]-1,3-benzodioxol-5-ol
Homo sapiens
at pH 7.0 and 37°C
0.00068
6-[(4-hydroxyphenyl)(piperazin-1-yl)methyl]-1,3-benzodioxol-5-ol
Homo sapiens
at pH 7.0 and 37°C
0.00013
6-[(4-methoxyphenyl)(morpholin-4-yl)methyl]-1,3-benzodioxol-5-ol
Homo sapiens
at pH 7.0 and 37°C
0.00088
6-[(4-methoxyphenyl)(piperidin-1-yl)methyl]-2H-1,3-benzodioxol-5-ol
Homo sapiens
at pH 7.0 and 37°C
0.0013
6-[(4-methoxyphenyl)(pyrimidin-2-ylamino)methyl]-1,3-benzodioxol-5-ol
Homo sapiens
at pH 7.0 and 37°C
0.00152
6-[(4-methoxyphenyl)(pyrrolidin-1-yl)methyl]-1,3-benzodioxol-5-ol
Homo sapiens
at pH 7.0 and 37°C
0.00098
6-[(morpholin-4-yl)(2,4,6-trimethoxyphenyl)methyl]-2H-1,3-benzodioxol-5-ol
Homo sapiens
at pH 7.0 and 37°C
0.00064
6-[(morpholin-4-yl)(3,4,5-trimethoxyphenyl)methyl]-2H-1,3-benzodioxol-5-ol
Homo sapiens
at pH 7.0 and 37°C
0.0007
6-[(piperidin-1-yl)(3,4,5-trimethoxyphenyl)methyl]-2H-1,3-benzodioxol-5-ol
Homo sapiens
at pH 7.0 and 37°C
0.00018
6-[(pyrrolidin-1-yl)(3,4,5-trimethoxyphenyl)methyl]-2H-1,3-benzodioxol-5-ol
Homo sapiens
at pH 7.0 and 37°C
0.0002
6-[1,3,5-benzotrioxepin-7-yl(morpholin-4-yl)methyl]-1,3-benzodioxol-5-ol
Homo sapiens
IC50 above 0.0002, at pH 7.0 and 37°C
0.000072
6-[1,3,5-benzotrioxepin-7-yl(pyridin-2-ylamino)methyl]-1,3-benzodioxol-5-ol
Homo sapiens
at pH 7.0 and 37°C
0.00118
6-[1,3,5-benzotrioxepin-7-yl(pyrimidin-2-ylamino)methyl]-1,3-benzodioxol-5-ol
Homo sapiens
at pH 7.0 and 37°C
0.000023
6-[1,3,5-benzotrioxepin-7-yl(pyrrolidin-1-yl)methyl]-1,3-benzodioxol-5-ol
Homo sapiens
at pH 7.0 and 37°C
0.00062
6-[1H-imidazol-1-yl(4-methoxyphenyl)methyl]-1,3-benzodioxol-5-ol
Homo sapiens
at pH 7.0 and 37°C
0.04
6-[cyclohexyl(phenyl)methyl]-1,3-benzodioxol-5-ol
Homo sapiens
IC50 above 0.04 mM, at pH 7.0 and 37°C
0.00127
6-[[4-(dimethylamino)phenyl](piperidin-1-yl)methyl]-2H-1,3-benzodioxol-5-ol
Homo sapiens
at pH 7.0 and 37°C
0.0002
6-[[4-(dimethylamino)phenyl](pyrrolidin-1-yl)methyl]-1,3-benzodioxol-5-ol
Homo sapiens
IC50 above 0.0002 mM, at pH 7.0 and 37°C
0.00039
7-((2,3-dimethoxyphenyl)(morpholino)methyl)quinolin-8-ol
Homo sapiens
at pH 7.0 and 37°C
0.0012
7-((4-fluorophenyl)(piperazin-1-yl)methyl)quinazolin-8-ol
Homo sapiens
at pH 7.0 and 37°C
0.00067
7-((4-fluorophenyl)(piperidin-1-yl)methyl)-2,3-dihydrobenzo[b][1,4]dioxin-6-ol
Homo sapiens
at pH 7.0 and 37°C
0.00486
7-((4-fluorophenyl)(piperidin-1-yl)methyl)quinazolin-8-ol
Homo sapiens
at pH 7.0 and 37°C
0.00069
7-((4-fluorophenyl)(piperidin-1-yl)methyl)quinolin-8-ol
Homo sapiens
at pH 7.0 and 37°C
0.04
7-[(2,5-dimethylcyclohexa-1,3-dien-1-yl)[(4-methylpyridin-2-yl)amino]methyl]quinolin-8-ol
Homo sapiens
IC50 above 0.04 mM, at pH 7.0 and 37°C
0.00073
7-[(2,5-dimethylphenyl)(pyridin-2-ylamino)methyl]quinolin-8-ol
Homo sapiens
at pH 7.0 and 37°C
0.00189
7-[(2,6-dichlorophenyl)(pyridin-2-ylamino)methyl]quinolin-8-ol
Homo sapiens
at pH 7.0 and 37°C
0.04
7-[(2,6-dichlorophenyl)[(4-methylpyridin-2-yl)amino]methyl]quinolin-8-ol
Homo sapiens
IC50 above 0.04 mM, at pH 7.0 and 37°C
0.00037
7-[(2-chloro-3-hydroxycyclohexa-1,3-dien-1-yl)(pyridin-2-ylamino)methyl]quinolin-8-ol
Homo sapiens
at pH 7.0 and 37°C
0.04
7-[(2-chloro-6-fluorophenyl)[(4-methylpyridin-2-yl)amino]methyl]quinolin-8-ol
Homo sapiens
IC50 above 0.04 mM, at pH 7.0 and 37°C
0.0005
7-[(2-chlorophenyl)(pyridin-2-ylamino)methyl]quinolin-8-ol
Homo sapiens
at pH 7.0 and 37°C
0.04
7-[(2-chlorophenyl)[(4-methylpyridin-2-yl)amino]methyl]quinolin-8-ol
Homo sapiens
IC50 above 0.04 mM, at pH 7.0 and 37°C
0.00047
7-[(2-fluorocyclohexa-1,3-dien-1-yl)(pyridin-2-ylamino)methyl]quinolin-8-ol
Homo sapiens
at pH 7.0 and 37°C
0.00088
7-[(2-fluorophenyl)[(4-methylpyridin-2-yl)amino]methyl]quinolin-8-ol
Homo sapiens
at pH 7.0 and 37°C
0.04
7-[(2-methylcyclohexa-1,3-dien-1-yl)[(4-methylpyridin-2-yl)amino]methyl]quinolin-8-ol
Homo sapiens
IC50 above 0.04 mM, at pH 7.0 and 37°C
0.00035
7-[(3-fluorophenyl)[(4-methylpyridin-2-yl)amino]methyl]quinolin-8-ol
Homo sapiens
at pH 7.0 and 37°C
0.00015
7-[(3-hydroxy-4-methoxyphenyl)[(4-methylpyridin-2-yl)amino]methyl]quinolin-8-ol
Homo sapiens
at pH 7.0 and 37°C
0.00286
7-[(3-methoxycyclohexa-1,3-dien-1-yl)(pyridin-2-ylamino)methyl]quinolin-8-ol
Homo sapiens
at pH 7.0 and 37°C
0.00017
7-[(4-chlorophenyl)(pyridin-2-ylamino)methyl]quinolin-8-ol
Homo sapiens
at pH 7.0 and 37°C
0.00017
7-[(4-ethylphenyl)(pyridin-2-ylamino)methyl]quinolin-8-ol
Homo sapiens
at pH 7.0 and 37°C
0.00539
7-[(4-ethylphenyl)[(4-methylpyridin-2-yl)amino]methyl]quinolin-8-ol
Homo sapiens
at pH 7.0 and 37°C
0.00014
7-[(4-fluorophenyl)[(4-methylpyridin-2-yl)amino]methyl]quinolin-8-ol
Homo sapiens
at pH 7.0 and 37°C
0.00018
7-[(4-hydroxy-3,5-dimethoxyphenyl)[(5-methylpyridin-2-yl)amino]methyl]quinolin-8-ol
Homo sapiens
at pH 7.0 and 37°C
0.00046
7-[(4-methylphenyl)(pyridin-2-ylamino)methyl]quinolin-8-ol
Homo sapiens
at pH 7.0 and 37°C
0.0002
7-[cyclohexa-1,3-dien-1-yl[(4-methylpyridin-2-yl)amino]methyl]quinolin-8-ol
Homo sapiens
IC50 above 0.0002 mM, at pH 7.0 and 37°C
0.00039
7-[[(3-methoxyphenyl)amino](phenyl)methyl]quinolin-8-ol
Homo sapiens
at pH 7.0 and 37°C
0.00053
7-[[(4-methylpyridin-2-yl)amino](4-nitrophenyl)methyl]quinolin-8-ol
Homo sapiens
at pH 7.0 and 37°C
0.00062
7-[[(4-methylpyridin-2-yl)amino](4-phenoxyphenyl)methyl]quinolin-8-ol
Homo sapiens
at pH 7.0 and 37°C
0.0265
7-[[(4-methylpyridin-2-yl)amino][4-(trifluoromethyl)phenyl]methyl]quinolin-8-ol
Homo sapiens
at pH 7.0 and 37°C
0.00015
7-[[(4-nitrophenyl)amino](phenyl)methyl]quinolin-8-ol
Homo sapiens
at pH 7.0 and 37°C
0.00019
7-[[(pyridin-2-yl)amino](2,4,6-trimethylcyclohexa-1,3-dien-1-yl)methyl]quinolin-8-ol
Homo sapiens
at pH 7.0 and 37°C
0.0102
8-((4-fluorophenyl)(piperidin-1-yl)methyl)isoquinolin-7-ol
Homo sapiens
at pH 7.0 and 37°C
0.0002
ethyl 3-[[(8-hydroxyquinolin-7-yl)(phenyl)methyl]amino]benzoate
Homo sapiens
IC50 above 0.0002 mM, at pH 7.0 and 37°C
0.00581 - 0.01079
ethyl N-[[(2,4-dimethoxyphenyl)(prop-2-ynoyl)amino](thiophen-2-yl)acetyl]glycinate
0.0478
methyl 3-[(1E)-3-(3-hydroxy-4-methoxyphenyl)-3-oxoprop-1-en-1-yl]benzoate
Homo sapiens
-
at pH 7.0 and 37°C
0.00012
methyl 3-[(1E)-3-(3-hydroxyphenyl)-3-oxoprop-1-en-1-yl]benzoate
Homo sapiens
-
at pH 7.0 and 37°C
0.0004
methyl 3-[(1E)-3-(4-hydroxyphenyl)-3-oxoprop-1-en-1-yl]benzoate
Homo sapiens
-
at pH 7.0 and 37°C
0.1
methyl 3-[(1E)-3-(4-[[(dibutylamino)oxy]sulfinyl]phenyl)-3-oxoprop-1-en-1-yl]benzoate
Homo sapiens
-
at pH 7.0 and 37°C
0.1
methyl 3-[(1E)-3-(4-[[(dipropylamino)oxy]sulfinyl]phenyl)-3-oxoprop-1-en-1-yl]benzoate
Homo sapiens
-
at pH 7.0 and 37°C
0.00013
methyl 3-[(1E)-3-[3-bromo-4-(hydroxymethyl)phenyl]-3-oxoprop-1-en-1-yl]benzoate
Homo sapiens
-
at pH 7.0 and 37°C
0.00049
methyl 3-[(1E)-3-[4-hydroxy-3-(trifluoromethyl)phenyl]-3-oxoprop-1-en-1-yl]benzoate
Homo sapiens
-
at pH 7.0 and 37°C
0.1
methyl 3-[(1E)-3-[4-[(4-nitrobenzene-1-sulfonyl)amino]phenyl]-3-oxoprop-1-en-1-yl]benzoate
Homo sapiens
-
at pH 7.0 and 37°C
0.00137
N-(4-(5,5-difluoro-1,3,7,9-tetramethyl-5H-4lambda4,5lambda4-dipyrrolo[1,2-c:2',1'-f][1,3,2]diazaborinin-10-yl)-N(2-(4-((6-hydroxybenzo[d][1,3]dioxol-5-yl)(piperidin-1-yl)methyl)benzamido)ethyl)benzamide
Homo sapiens
at pH 7.0 and 37°C
0.00851
N-([4-[(2E)-3-(3-cyanophenyl)prop-2-enoyl]phenyl]methyl)-4-nitrobenzene-1-sulfonamide
Homo sapiens
-
at pH 7.0 and 37°C
0.00574
N-([4-[(2E)-3-(3-hydroxyphenyl)prop-2-enoyl]phenyl]methyl)thiophene-2-carboxamide
Homo sapiens
-
at pH 7.0 and 37°C
0.01113
N-([4-[(2E)-3-(3-hydroxyphenyl)prop-2-enoyl]phenyl]methyl)thiophene-2-sulfonamide
Homo sapiens
-
at pH 7.0 and 37°C
0.5
N-([4-[(2E)-3-(4-methoxyphenyl)prop-2-enoyl]phenyl]methyl)thiophene-2-carboxamide
Homo sapiens
-
at pH 7.0 and 37°C
0.04 - 0.5
N-([4-[(2E)-3-(4-methoxyphenyl)prop-2-enoyl]phenyl]methyl)thiophene-2-sulfonamide
Homo sapiens
-
at pH 7.0 and 37°C
0.05
prop-2-yn-1-yl 1-methyl-2-[[nitroso(phenyl)amino]acetyl]-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-1-carboxylate
Homo sapiens
at pH 7.0 and 37°C
0.00125
[4-[(1E)-3-oxo-3-phenylprop-1-en-1-yl]phenyl]boronic acid
Homo sapiens
-
at pH 7.0 and 37°C
0.00083
[4-[(2E)-3-(3-cyanophenyl)prop-2-enoyl]phenyl]boronic acid
Homo sapiens
-
at pH 7.0 and 37°C
0.00175
[4-[(2E)-3-(3-hydroxyphenyl)prop-2-enoyl]phenyl]methyl thiophene-2-carboxylate
Homo sapiens
-
at pH 7.0 and 37°C
0.04 - 0.5
[4-[(2E)-3-(4-methoxyphenyl)prop-2-enoyl]phenyl]methyl thiophene-2-carboxylate
Homo sapiens
-
at pH 7.0 and 37°C
0.00017
1,3,6-trimethylpyrimido[5,4-e][1,2,4]triazine-5,7(1H,6H)-dione
Homo sapiens
-
at pH 7.0 and 37°C
0.00655
1,3,6-trimethylpyrimido[5,4-e][1,2,4]triazine-5,7(1H,6H)-dione
Homo sapiens
-
at pH 7.0 and 37°C
0.00082
3-[(1E)-3-oxo-3-[4-(piperidin-4-yl)phenyl]prop-1-en-1-yl]benzonitrile
Homo sapiens
-
at pH 7.0 and 37°C
0.5
3-[(1E)-3-oxo-3-[4-(piperidin-4-yl)phenyl]prop-1-en-1-yl]benzonitrile
Homo sapiens
-
at pH 7.0 and 37°C
0.07
bacitracin
Bos taurus
-
commercial bacitracin, in 100 mM potassium phosphate and 1 mm EDTA (pH 7.4), at 22°C
0.172
bacitracin
Entamoeba histolytica
-
using denatured-reduced lysozyme as substrate, at pH 7.0, temperature not specified in the publication
0.334
bacitracin
Entamoeba histolytica
-
using scrambled reoxidized lysozyme as substrate, at pH 7.0, temperature not specified in the publication
1.137
bacitracin
Entamoeba histolytica
-
using insulin as substrate, at pH 7.0, temperature not specified in the publication
0.00581
ethyl N-[[(2,4-dimethoxyphenyl)(prop-2-ynoyl)amino](thiophen-2-yl)acetyl]glycinate
Homo sapiens
-
at pH 7.0 and 37°C
0.01079
ethyl N-[[(2,4-dimethoxyphenyl)(prop-2-ynoyl)amino](thiophen-2-yl)acetyl]glycinate
Homo sapiens
-
at pH 7.0 and 37°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.175
isoform PDIL5A, at pH 7.5 and 25°C
0.179
isoform PDIL4D, at pH 7.5 and 25°C
0.287
isoform PDIL2, at pH 7.5 and 25°C
0.665
isoform PDIL1B, at pH 7.5 and 25°C
0.736
isoform PDIL1Aalpha, at pH 7.5 and 25°C
additional information
additional information
-
ATPase activity, Holmgren's turbimetric method for reductive activity measurement utilizing bovine insulin
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5
7.4
7.5
additional information
-
PDI has a greater relative impact on isomerization reactions and consequently the structure-forming step in oxidative folding at pH 7, as opposed to pHs 8 and 9
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.5 - 7.5
-
approx. 50% of maximal activity at pH 5.5, approx. 75% of maximal activity at pH 7.5
5 - 7
-
approx. 50% of maximal activity at pH 5.5, approx. 80% of maximal activity at pH 7.0, oxidation of NRCSQGSCWN
7.5 - 9
-
pH 7.5: about 20% of maximal activity, pH 9.0: about 80% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
30
37
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.7
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
a tick cultured on rabbit hosts, constitutive gene
SwissProt
brenda
12 genes coding for protein disulfide isomerase. Expression of six PDI genes is significantly up-regulated by unfolded protein response and sharply attenuated by the transcription inhibitor, actinomycin D. PDI and binding protein BIP2 expression is not affected in the unfolded protein response signaling mediator Atire1-2 mutant. The expression of four PDI genes is decreased in the unfolded protein response signaling mediator Atbzip60 mutant
-
-
brenda
-
3034, 3042, 3046, 3048, 3051, 3061, 3066, 3077, 3080, 3081, 3083, 3090, 3093, 3097, 649583, 651787, 651796, 652343, 652825, 661029, 661243, 661292, 678408, 692913, 695185, 706820, 713901, 714977, 715615
-
-
brenda
protein disulfide isomerase activity and glutathione-insulin transhydrogenase activity, EC 1.8.4.2, are catalyzed by a single enzyme protein
-
-
brenda
thyroid hormone binding protein is apparently identical to protein disulfide isomerase
-
-
brenda
isozyme PDI-2; wild-type strain N2 and diverse mutant strains, overview, isozymes PDI-1, PDI-2 and PDI-3 encoded by genes pdi-1, pdi-2 and pdi-3
-
-
brenda
wild-type strain N2 and diverse mutant strains, overview, isozymes PDI-1 and PDI-3 encoded by genes pdi-1 and pdi-3
-
-
brenda
-
-
-
brenda
proteins with protein disulfide isomerase activity: DsbA, DsbC and DsbD
-
-
brenda
protein disulfide-isomerase is identical with the beta-subunit of the prolyl 4-hydroxylase tetramer, alpha2beta2
-
-
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isozyme HlPDI-1; a tick cultured on rabbit hosts, gene HlPDI-1
SwissProt
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isozyme HlPDI-2; a tick cultured on rabbit hosts, gene HlPDI-2
SwissProt
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isozyme HlPDI-3; a tick cultured on rabbit hosts, gene HlPDI-3
SwissProt
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3034, 3038, 3039, 3040, 3055, 3057, 3068, 3070, 3076, 3092, 3093, 3097, 439186, 649103, 649415, 649629, 649853, 650065, 650318, 650485
-
-
brenda
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650995, 651254, 651915, 651957, 651977, 651990, 652289, 652425, 652434, 652503, 652514, 652576, 652604, 652930, 653808, 660877, 661243, 662298, 662348
-
-
brenda
-
726956, 727242, 727573, 728220, 728627, 728758, 728766, 746919, 746998, 747197, 747829, 747833, 747835, 747836
-
-
brenda
isoform procollagen-proline, 2-oxoglutarate-4-dioxygenase beta subunit
-
-
brenda
protein disulfide isomerase is identical to the beta-subunit of prolyl-4-hydroxylase
-
-
brenda
thyroid hormone binding protein is apparently identical to protein disulfide isomerase
-
-
brenda
protein disulfide isomerase is identical to the beta-subunit of prolyl-4-hydroxylase
-
-
brenda
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3053, 3076, 679424, 691923, 693350, 693351, 702795, 704927, 705216, 705291, 706539, 727242, 727990, 746977, 748196
-
-
brenda
chimeric PDI mutant containing Pichia pastoris signal sequence and ER retention sequence
AY919669
GenBank
brenda
-
3034, 3038, 3039, 3041, 3043, 3047, 3054, 3059, 3066, 3075, 3077, 3079, 3080, 3087, 3093, 3094, 3095, 3097, 649922, 652217, 661243, 663327
-
-
brenda
glutathione-insulin transhydrogenase and protein disulfide-isomerase are both not catalyzed by a single enzyme species
-
-
brenda
-
-
-
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PDI-2; two PDI enzyme forms, which contain one or two double-cysteine redox-active sites and correspond to a single domain PDI and a class 1 PDI, i.e. PDI-1 and PDI-2
SwissProt
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
brenda
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time-dependent decrease in in PDI expression in thrombi following injury. Infusion of monoclonal antibodies against PDI into the circulation of mice lacking the G protein-coupled platelet receptor Par4 prior to vessel wall injury inhibits fibrin generation
brenda
-
activities in adult tissues are only 10-40% of those found in newborn
brenda
cells of the acini type II and III of salivary gland
brenda
TXNDC5 is highly expressed in patient-derived lung cancer specimens, immunohistochemic analysis
brenda
-
activities in adult tissues are only 10-40% of those found in newborn
brenda
female tick, high expression of HlPDI-1
brenda
epididymal caput, corpus, and cauda sperm, isozymes PDIA3 and PDI-P5. PDI-P5 is downregulated from the epididymal corpus to cauda sperm, while PDIA3 is constitutively expressed
brenda
additional information
-
the thiol-containing form of PDI increases in the platelet surface with platelet activition
brenda
-
activities in adult tissues are only 10-40% of those found in newborn
brenda
-
distribution to the endoplasmic reticulum and protein storage vacuoles, PDIS-1 levels, but not PDIS-2 levels, are increased in cotyledons
brenda
-
expression of GmPDIL-3a and GmPDIL-3b in soybean cotyledons during maturation, overview
brenda
-
transcription is more than 7fold enriched in L1 state compared to eggs
brenda
female tick, highest expression level of HlPDI-1
brenda
-
brenda
-
activities in adult tissues are only 10-40% of those found in newborn
brenda
-
transiently transfected with human wild-type US2, wild-type US11, or different cysteine mutants of US2 and US11
brenda
-
activities in adult tissues are only 10-40% of those found in newborn
brenda
-
-
3042, 3046, 3048, 3051, 3052, 3061, 3069, 3077, 3089, 3093, 661292, 661029, 678408, 692913, 695185, 706820, 713901, 714977, 715615
brenda
-
activities in adult tissues are only 10-40% of those found in newborn
brenda
-
activities in adult tissues are only 10-40% of those found in newborn
brenda
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enzyme activity increases in response to polyclonal activation by bacterial lipopolysaccharide. Induction of the enzyme is closely coupled to the final stages of differentiation to plasma cells
brenda
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pancreas-specific protein disulfide isomerase, PDIp, specific expression in pancreatic acinar cells, high expression level of PDIp
brenda
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on the extracellular surface of both nonactivated and thrombin-activated platelets. Enzyme is released by vesiculation from activated platelets
brenda
female tick, high expression of HlPDI-1
brenda
female tick, high expression of HlPDI-2
brenda
female tick, high expression of HlPDI-3
brenda
-
changes in the levels of PDIS-1 and PDIS-2 during seed development, overview
brenda
-
activities in adult tissues are only 10-40% of those found in newborn
brenda
-
activities in adult tissues are only 10-40% of those found in newborn
brenda
-
specific expression of PDIp in gastric chief cells, high expression level of PDIp
brenda
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activities in adult tissues are only 10-40% of those found in newborn
brenda
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localized in the hypodermis and uterus wall of female adults
brenda
additional information
the PDI expression levels in salivary gland is uniform in unfed ticks and ticks fed for different time intervals, no differences in enzyme expression between female and male ticks, PDI tissue distribution analysis, overview
brenda
additional information
-
the PDI expression levels in salivary gland is uniform in unfed ticks and ticks fed for different time intervals, no differences in enzyme expression between female and male ticks, PDI tissue distribution analysis, overview
brenda
additional information
-
no detection of protein of the 52 kDa isoform in root
brenda
additional information
-
PDI-2 is required for normal post-embryonic development
brenda
additional information
-
transcription is more than 7fold enriched in L1 state compared to eggs, and displays a dramatic decrease in L3. Following an increase in the L5 stage, there is again a decrease in the adult worm
brenda
additional information
-
GmPDIL-3a and GmPDIL-3b are ubiquitously expressed in the plant body
brenda
additional information
the isozymes are present in all the developmental stages of the tick, immunihistochemic and quantitative expression analysis, overview
brenda
additional information
the isozymes are present in all the developmental stages of the tick, immunihistochemic and quantitative expression analysis, overview
brenda
additional information
the isozymes are present in all the developmental stages of the tick, immunihistochemic and quantitative expression analysis, overview
brenda
additional information
-
the isozymes are present in all the developmental stages of the tick, immunihistochemic and quantitative expression analysis, overview
brenda
additional information
the isozymes are present in all the developmental stages of the tick, immunohistochemic and quantitative expression analysis, overview
brenda
additional information
the isozymes are present in all the developmental stages of the tick, immunohistochemic and quantitative expression analysis, overview
brenda
additional information
the isozymes are present in all the developmental stages of the tick, immunohistochemic and quantitative expression analysis, overview
brenda
additional information
-
the isozymes are present in all the developmental stages of the tick, immunohistochemic and quantitative expression analysis, overview
brenda
additional information
-
no activity of PDIp in pancreatic adenocarcinoma cells
brenda
additional information
TXNDC5 cannot be detected in human normal organs, including bone marrow, prostate, cardiac muscle, and cervix. In contrast, strong positive TXNDC5 staining is consistently observed in tissues from human normal cerebral gray matter, small intestine, colon, stomach, kidney, and salivary gland. No significant numbers of TXNDC5 are positively stained cells in normal lung tissue while strongly positive staining of TXNDC5 is found in lung tumor cells, as evidenced by the dark brown color in examples of lung squamous cell carcinoma, bronchioloalveolar carcinoma, adenocarcinoma, and small cell carcinoma. Differential expression pattern of TXNDC5 in human lung normal and cancer specimens
brenda
additional information
-
TXNDC5 cannot be detected in human normal organs, including bone marrow, prostate, cardiac muscle, and cervix. In contrast, strong positive TXNDC5 staining is consistently observed in tissues from human normal cerebral gray matter, small intestine, colon, stomach, kidney, and salivary gland. No significant numbers of TXNDC5 are positively stained cells in normal lung tissue while strongly positive staining of TXNDC5 is found in lung tumor cells, as evidenced by the dark brown color in examples of lung squamous cell carcinoma, bronchioloalveolar carcinoma, adenocarcinoma, and small cell carcinoma. Differential expression pattern of TXNDC5 in human lung normal and cancer specimens
brenda
additional information
-
no or poor expression of PDIp in colon, cecum, and duodenum. PDIp shows a cell-type specific expression in various mouse tissues, in the digestive organs, such as the stomach and pancreas, very high levels of PDIp are selectively expressed in the digestive enzyme-secreting cells
brenda
additional information
-
stage-specific expression and cellular localization of isozymes, overview, isozyme PDI-8 is expressed during all stages of parasite life cycle
brenda
additional information
-
PDI expression during parasite development, overview
brenda
additional information
differential expression of PDIA3 mRNA in salmon tissues
brenda
additional information
-
differential expression of PDIA3 mRNA in salmon tissues
brenda
additional information
developmentally regulated expression of both PDI enzyme forms, the enzymes are not essential for growth of trypanosomes
brenda
additional information
-
developmentally regulated expression of both PDI enzyme forms, the enzymes are not essential for growth of trypanosomes
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
in endothelial cells. On activation of endothelial cells, PDI remains confined to the intracellular stores of the dense tubular system and is neither released nor targeted to the cell surface
-
brenda
additional information
-
in presence of light, level of protein disulfide isomerase protein decreases by 80%. The effect of chemical treatments coincides with the effect of the light/dark cycle
brenda
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RB60 contains an N-terminal sequence of 50 amino acids that are sufficient for chloroplast and enodplasmic reticulum targeting, after translocation to the ER the leader sequence is cleaved while it remains intact after import into chloroplasts
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RB60 contains an N-terminal sequence of 50 amino acids that are sufficient for chloroplast and enodplasmic reticulum targeting, after translocation to the ER the leader sequence is cleaved while it remains intact after import into chloroplasts
-
brenda
PDI contains an endoplasmic reticulum-retention KEEL signal
brenda
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the enzyme contains a C-terminal endoplasmic reticulum retention signal, RB60 contains an N-terminal leader sequence of 50 amino acids that are sufficient for chloroplast and enodplasmic reticulum targeting, after translocation to the ER the leader sequence is cleaved while it remains intact after import into chloroplasts
brenda
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the enzyme contains a C-terminal endoplasmic reticulum retention signal, RB60 contains an N-terminal leader sequence of 50 amino acids that are sufficient for chloroplast and enodplasmic reticulum targeting, after translocation to the ER the leader sequence is cleaved while it remains intact after import into chloroplasts
-
brenda
the enzyme contains an N-terminal ER retention signal sequence
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ER retention/retrieval signal KQRL
brenda
gPDI-3 has a ER retention/retrieval signal KQRL, gPDI-2 has a KRKK motif
brenda
-
PDIS-1 and PDIS-2 lack the C-terminal, endoplasmic reticulum-retrieval signal, KDEL
brenda
-
expression is up-regulated in ER-stress conditions
brenda
PDI contains an endoplasmic reticulum-retention VEL signal
brenda
PDI contains an endoplasmic reticulum-retention DEL signal
brenda
PDI contains an endoplasmic reticulum-retention EEL signal
brenda
ERp27 contains a putative secretory pathway signal sequence and a putative endoplasmic reticulum-retention signal, overview
brenda
-
exclusively in human umbilical vein endothelial cells. In endothelium, PDI remains exclusively localized in the endoplasmic reticulum, both at steady state and after thrombin stimulation
brenda
-
-
704927, 705291, 702970, 704784, 714600, 715531, 728766, 727573, 747829, 747833, 746919, 747835, 747836
brenda
mainly localized in the endoplasmic reticulum lumen
brenda
-
the enzyme contains a C-terminal endoplasmic reticulum retrieval signal, SEEL
brenda
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loosely associated with the luminal surface
brenda
-
PDI possesses an anomalously low thiol pKa and is fine-tuned to catalyze oxidative folding in the lumen of the endoplasmic reticulum where the ambient pH of about 7 would otherwise retard thioldisulfide exchange reactions and hinder acquisition of the native fold
brenda
-
-
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lumen, high concentration in the ER
brenda
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enzyme exists as an interconvertible mixture of monomers and dimers
brenda
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the enzyme is among the most abundant proteins within the endoplasmic reticulum of developing grains
brenda
-
brenda
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GmPDIL-3a and GmPDIL-3b form protein complexes in the endoplasmic reticulum
brenda
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integral, the catalytic reaction takes place on the periplasmic side, PDI contains four transmembrane helices that surround the bound ubiquinone cofactor, overview
brenda
-
rough. The enzyme associates with the membrane via electrostatic interactions between the acidic enzyme and the basic groups on the membrane
-
brenda
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located on both sides of the membrane. The inside-located enzyme is immunochemically different from the outside-located enzyme
-
brenda
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presence of isoforms P5 and Erp57. P5 localizes to the inner side of the inner membrane
brenda
-
-
-
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PDIL2-3 is localized mainly on the surface of the endoplasmic reticulum
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PDIL1-1 is uniformly distributed in the lumen
brenda
additional information
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dual localization of RB60 via two different conserved transport mechanisms, overview
-
brenda
additional information
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dual localization of RB60 via two different conserved transport mechanisms, overview
-
-
brenda
additional information
-
PDIS-1 and PDIS-2 both possess a putative N-terminal secretory signal sequence and two tandem thioredoxin-like motifs, with a CGHC active site
-
brenda
additional information
subcellular localization study with wild-type and mutant enzyme, overview
-
brenda
additional information
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subcellular localization study with wild-type and mutant enzyme, overview
-
brenda
additional information
-
presence of protein disulfide isomerase on the surface of platelet-derived microparticles. Enzyme is catalytically active and capable of both promoting platelet aggregation and disrupting insulin signaling. Platelet-derived microparticles increase the initial rates of aggregation by 4fold and the pro-aggregatory activity of micrparticles can be attenuated with an anti-PDI antibody. Anti-PDI antibodies are able to block the degradation of insulin, thereby restoring insulin signaling
-
brenda
additional information
-
semiquantitative analysis of the endogenous PDI distribution, overview
-
brenda
additional information
-
stage-specific expression and cellular localization of isozymes, overview
-
brenda
additional information
cullular enzyme distribution, immunohistochemic detection, overview
-
brenda
additional information
both enzyme forms co-localized with markers of the endocytic pathway and concentrate at the posterior end of the cell between the nucleus and the kinetoplast
-
brenda
additional information
-
both enzyme forms co-localized with markers of the endocytic pathway and concentrate at the posterior end of the cell between the nucleus and the kinetoplast
-
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
additional information
malfunction
-
mice lacking AGR2 are viable but are highly susceptible to colitis, indicating a critical role for AGR2 in protection from disease
malfunction
-
PDI inhibition or silencing increases apoptosis and inhibits migration and adhesion of endothelial cells, overview
malfunction
-
the anomalous behavior of PDI during a key step in oxidative regeneration may contribute to misfolding in the endoplasmic reticulum, aggregation, and neurodegenerative disease
malfunction
-
functional inhibition of protein disulfide isomerase by S-nitrosylation may contribute to pathophysiology in both mutant superoxide dismutase 1-linked disease and sporadic amyotrophic lateral sclerosis
malfunction
PDIL2-3 knockdown causes aberrant accumulation of prolamins in endoplasmic reticulum-derived type-I protein bodies whereas the oxidative folding of vacuole-targeted proteins, such as proglutelins and alpha-globulin, is hardly affected. PDIL2-3 knockdown inhibits the accumulation of Cys-rich 10-kD prolamin in the core of type-I protein bodies
malfunction
-
inhibition of cell surface PDI induces a marked increase in tissue factor procoagulant function
malfunction
-
enzyme silencing prevents Nox responses to angiotensin II and inhibits Akt phosphorylation in vascular cells and parasite phagocytosis in macrophages
malfunction
-
enzyme silencing decreases Nox1 expression and reactive oxygen species production as well as platelet-derived growth factor-induced Rac1 and RhoA activities
malfunction
PDIA6-deficient cells hyperrespond to endoplasmic reticulum stress with sustained autophosphorylation of inositol-requiring enzyme 1alpha and splicing of XBP1 mRNA, resulting in exaggerated upregulation of UPR target genes and increased apoptosis. In vivo, PDIA6-deficient Caenorhabditis elegans exhibits constitutive unfolded protein response and fails to complete larval development
malfunction
-
enzyme inhibition results ina 25% loss of vessel caliber post-injury. This is accompanied by decreased hydrogen peroxide formation and changes in collagen organization, resulting in increased arterial stiffness
malfunction
deletion of the ncgl2478 gene increases the size of growth inhibition zones. Site-directed mutagenesis confirms Cys24 as the resolving Cys residue, while Cys21 is the nucleophilic cysteine that is oxidized to a sulfenic acid and then forms an intramolecular disulfide bond with Cys24 or a mixed disulfide with MSH under oxidative stress
malfunction
TXNDC5 knockdown in lung cancer cells inhibits cell proliferation and represses anchorage-independent colony formation and migration, but increases cell invasion and activation of mitogen-activated protein kinases. Knockdown of TXNDC5 sensitizes human lung cancer cells to endoplasmic reticulum (ER) stress-induced cell death. Knockdown of TXNDC5 enhances EGF-induced MAPK activation in human lung cancer cells, which may contribute to the increased invasiveness of these cells
malfunction
-
enzyme inhibition or knockdown reduces CRC cell viability and induced apoptosis
metabolism
-
the close interdependence between Mnl1p and PDI suggests that these two proteins form a functional unit in the ER-associated degradation, ERAD, pathway
metabolism
-
isoform PDI2 interacts with proteins in both the endoplasmic reticulum (ER) and nucleus, including ER-resident protein folding chaperone, BiP1, and nuclear embryo transcription factor, MEE8
metabolism
isoform PDIL1;1 plays primary roles in both disulfide bond formation and disulfide bond reduction, which allow for redox control of protein quality and packaging
metabolism
-
the enzyme participates in many important cellular events including the oxidative protein folding, the endoplasmic reticulum associated degradation, the retrieval of unassembled proteins in the early secretory pathway, and the regulation of unfolded protein response pathways
metabolism
-
the enzyme is responsible for the oxidation (formation), reduction (break down) and isomerization (rearrangement) of protein disulfide bonds via disulfide interchange activity. The enzyme also has general chaperone activity
metabolism
-
enzyme-mediated disulfide bond exchange plays a pivotal role in the post-ligation phase of integrin alphaIIbbeta3-mediated adhesion to fibrinogen
metabolism
the enzyme receives electrons preferentially from the mycothiol (MSH)/mycothione reductase (Mtr)/NADPH pathway
metabolism
protein disulfide isomerase is both an enzyme and a molecular chaperone
metabolism
-
the close interdependence between Mnl1p and PDI suggests that these two proteins form a functional unit in the ER-associated degradation, ERAD, pathway
-
physiological function
-
the enzyme is required for infection by Chlamydia species
physiological function
physiological roles of PDIA3 and PDI-P5 in sperm maturation and fertilization, overview
physiological function
-
the enzyme plays a role in the formation of disulfide bonds in immunoglobulins, it is also involved in disulfide bond formation of the IgG4 subclass of antibody, but catalysis of disulfide bond formation is not rate limiting for IgG4 production
physiological function
-
the enzyme plays a role in the formation of disulfide bonds in immunoglobulins, it is also involved in disulfide bond formation of the IgG4 subclass of antibody, but catalysis of disulfide bond formation is not rate limiting for IgG4 production
physiological function
-
the enzyme is involved in myocardial angiogenesis. Protein disulfide isomerase is highly upregulated in hypoxic myocardial capillary endothelial cells, chronic hypoxia increases the survival rate and reduces the infarct size in myocardial ischemia, overview
physiological function
PDIA3 is an endoplasmic reticulum stress protein. It is induced by oxidative stress and plays a role in relation to stress regulation
physiological function
-
PDI and other PDI family proteins are thought to play important roles in disulfide bond formation and isomerization in the endoplasmic reticulum
physiological function
-
PDIp may function as a protein-folding catalyst for secretory digestive enzymes
physiological function
-
the protein disulfide isomerase AGR2 is essential for production of intestinal mucin MUC2, a large, cysteine-rich glycoprotein that forms the protective mucus gel lining the intestine
physiological function
-
the enzyme is involved in myocardial angiogenesis, overview
physiological function
-
PDI is a key enzyme involved in formation of correct pattern of disulfide bonds in proteins. PDI also plays an important role in the hypothalamic-pituitary-thyroid axis, mechanism, overview
physiological function
-
PDI is a key enzyme involved in formation of correct pattern of disulfide bonds in proteins. PDI also plays an important role in the hypothalamic-pituitary-thyroid axis, mechanism, overview
physiological function
-
PDI is a key enzyme involved in formation of correct pattern of disulfide bonds in proteins. PDI also plays an important role in the hypothalamic-pituitary-thyroid axis, mechanism, overview
physiological function
-
PDI is an abundant enzyme that forms, breaks, and isomerizes disulfide bonds and is therefore an important cellular defense against protein misfolding. PDI can be protective against mutant SOD1 aggregation and toxicity
physiological function
-
PDI is an abundant enzyme that forms, breaks, and isomerizes disulfide bonds and is therefore an important cellular defense against protein misfolding. PDI can be protective against mutant SOD1 aggregation and toxicity
physiological function
-
PDI is an abundant enzyme that forms, breaks, and isomerizes disulfide bonds and is therefore an important cellular defense against protein misfolding. PDI can be protective against mutant SOD1 aggregation and toxicity
physiological function
PDI is a multifunctional protein for catalyzing the formation, isomerization, and reduction of disulfide bonds
physiological function
-
endoplasmic reticulum stress is important in the formation of mutant superoxide dismutase 1 inclusions, and protein disulfide isomerase has an important function in ameliorating mutant superoxide dismutase 1 aggregation and toxicity
physiological function
-
the substrate binding, but not catalytic, activity of PDI is essential for the degradation of MHC class I HC by human cytomegalovirus glycoprotein US2, but not by US11, since oxidative folding of US2 is required for US2 function in inducing degradation of MHC class I molecules, PDI catalyses the release of MHC class I molecules from US2, function for PDI in SPP-mediated ERAD pathway, overview
physiological function
PDIL2-3 does not facilitate the oxidative folding of proglutelins
physiological function
the a and a' domains of PDIL1-1 are both functional in the oxidative folding of proglutelins
physiological function
-
the DsbA coexpressed as whole cell bioconversion system can more efficiently detoxify high concentration of organophosphates than cells expressing methyl parathion hydrolase only. Overexpression of protein disulfide isomerase DsbA enhances detectability in the environment following degradation of pesticide residues
physiological function
-
protein disulfide isomerase blocks transcription factor C/EBP-alpha translation but not transcription
physiological function
-
extracellular protein disulfide isomerase negatively regulates coagulation on endothelial cells through modulation of phosphatidylserine exposure
physiological function
-
PDI is required for cholera toxin intoxication but not for cholera toxin subunit A1 translocation
physiological function
-
the enzyme isoform PDI2 is involved in circadian rhythm regulation. Isoform PDI2 is a redox-active protein and has refolding activity. Overexpression of the ioform PDI2 causes a shift in acrophase of the circadian rhythm of phototaxis
physiological function
-
the enzyme plays a key role in assisting Leishmania protein folding via its capacity to catalyze formation, breakage, and rearrangement of disulfide bonds in nascent polypeptides. The enzyme displays a chaperone-like activity
physiological function
-
the enzyme is associated with the reproductive development and enriched in adult females
physiological function
-
protein disulfide isomerase regulates endoplasmic reticulum stress and the apoptotic process during prion infection and prion protein mutant-induced cytotoxicity. The enzyme functions as a pleiotropic regulator in the processes of different misfolded prion proteins and at different stages during prion infection. The enzyme is involved in mitochondrial dysfunction induced by misfolded prion
physiological function
-
protein disulfide isomerase interacts with tau protein and physiologically inhibits its fibrillization mainly through ist thioredoxin-like catalytic domain a, forming a 1:1 complex and preventing Tau misfolding. Protein disulfide isomerase is both an enzyme and a chaperone, and implicated in neuroprotection against Alzheimer disease
physiological function
-
the enzyme is responsible for catalyzing the proper oxidation and isomerization of disulfide bonds of newly synthesized proteins in the endoplasmic reticulum
physiological function
-
extracellular protein disulfide isomerase (PDI) regulates ligand-binding activity of alphaMbeta2 integrin and neutrophil recruitment during vascular inflammation. Neutrophil PDI is required for neutrophil adhesion and crawling during tumor necrosis factor-alpha-induced vascular inflammation in vivo
physiological function
-
extracellular protein disulfide isomerase (PDI) regulates ligand-binding activity of alphaMbeta2 integrin and neutrophil recruitment during vascular inflammation. Neutrophil PDI is required for neutrophil adhesion and crawling during tumor necrosis factor-alpha-induced vascular inflammation in vivo
physiological function
-
enzyme overexpression spontaneously enhances Nox activation and expression. In neutrophils, enzyme redox-dependently associates with p47phox and supports the respiratory burst
physiological function
-
protein disulfide isomerase is required for platelet-derived growth factor-induced vascular smooth muscle cell migration, Nox1 NADPH oxidase expression, and Rho-GTPase activation
physiological function
-
protein disulfide isomerase directly interacts with beta-actin Cys374 during cell adhesion and spreading and regulates cytoskeleton reorganization
physiological function
-
the surface-associated enzyme is an important regulator of coagulation factor ligation to thrombin-stimulated platelets and of subsequent feedback activation of platelet thrombin generation. Extracellular enzyme regulates thrombin generation on thrombin-stimulated platelets
physiological function
isoform PDIA6 limits the duration of inositol-requiring enzyme 1alpha (IRE1alpha) activity by direct binding to cysteine 148 in the lumenal domain of the sensor, which is oxidized when IRE1 is activated
physiological function
-
isoform PDI8 functions in the oxidation of cysteines to produce disulfide bonds. It likely plays a role in folding newly-synthesized secretory proteins as they translocate across the endoplasmic reticulum membrane into the lumen
physiological function
-
enzyme overexpression has a negative impact on the initiation of chlorophyll degradation and proteolysis within chloroplasts. Enzyme overexpression in leaves induces a stay-green phenotype during darkness, where oxidative conditions favor catabolism
physiological function
-
isoform PDIA1 is required for agonist-triggered Nox NADPH oxidase activation and cell migration in vascular cells and macrophages. The enzyme also plays role in cytoskeleton organization
physiological function
-
the enzyme affects the redox homeostasis and unfolded protein response-related genes. The enzyme is involved in all major developmental processes, such as the formation of sclerotia, conidial anastomosis tubes and infection cushions, is involved in oxidative and osmotic stress resistance, and needed for full virulence
physiological function
-
PDI1 is a virulence factor of Phytophthora parasitica and contributes to plant infection
physiological function
-
the enzyme is a regulatorof vessel architecture and circumference that prevents inward remodeling without effects on wall thickness or neointima formation
physiological function
-
the enzyme is required for plants to survive under reducing conditions. Isoform PDI11 is involved in protein oxidative refolding
physiological function
enzyme NCgl2478 plays an important role in stress resistance. The enzyme receives electrons preferentially from the mycothiol (MSH)/mycothione reductase (Mtr)/NADPH pathway. NCgl2478 protects against various stresses by acting as an MSH-dependent thiol-disulfide reductase, belonging to a DsbA-Mrx1 cluster
physiological function
the redox regulator sulfiredoxin (Srx) forms a complex with thioredoxin domain-containing 5 protein in response to endoplasmic reticulum (ER) stress, but not to oxidative stress, in lung cancer cells. Increased association of Srx with TXNDC5 facilitates the retention of normally cytosolic Srx in the ER. TXNDC5 directly interacts with Srx through its thioredoxin-like domains
physiological function
the enzyme contributes to vascular inflammation and venous thrombosis. Endothelial enzyme protects against diabetic vascular complication. The enzyme reduces disulfides on the viral glycoprotein gp120 causing the internalization of HIV-1. The enzyme reduces beta1 and beta3 integrins allowing for the entry of dengue virus
physiological function
-
enzyme overexpression of wild type enzyme augments the viability of colorectal cancer cells and inhibits endoplasmic reticulum stress response and apoptosis through its oxidoreductase activity, thereby promoting the malignancy of colorectal cancer
physiological function
-
the enzyme plays a key role in assisting Leishmania protein folding via its capacity to catalyze formation, breakage, and rearrangement of disulfide bonds in nascent polypeptides. The enzyme displays a chaperone-like activity
-
additional information
the enzyme preserves a Cys-Pro-Phe-Cys active-site motif, which is presumed to be an exclusive characteristic of the DsbA-mycoredoxin 1 (Mrx1) cluster. Cys24 is the resolving Cys residue, while Cys21 is the nucleophilic cysteine that is oxidized to a sulfenic acid and then forms an intramolecular disulfide bond with Cys24 or a mixed disulfide with MSH under oxidative stress
additional information
-
the enzyme preserves a Cys-Pro-Phe-Cys active-site motif, which is presumed to be an exclusive characteristic of the DsbA-mycoredoxin 1 (Mrx1) cluster. Cys24 is the resolving Cys residue, while Cys21 is the nucleophilic cysteine that is oxidized to a sulfenic acid and then forms an intramolecular disulfide bond with Cys24 or a mixed disulfide with MSH under oxidative stress
additional information
-
the enzyme preserves a Cys-Pro-Phe-Cys active-site motif, which is presumed to be an exclusive characteristic of the DsbA-mycoredoxin 1 (Mrx1) cluster. Cys24 is the resolving Cys residue, while Cys21 is the nucleophilic cysteine that is oxidized to a sulfenic acid and then forms an intramolecular disulfide bond with Cys24 or a mixed disulfide with MSH under oxidative stress
-
additional information
-
the enzyme preserves a Cys-Pro-Phe-Cys active-site motif, which is presumed to be an exclusive characteristic of the DsbA-mycoredoxin 1 (Mrx1) cluster. Cys24 is the resolving Cys residue, while Cys21 is the nucleophilic cysteine that is oxidized to a sulfenic acid and then forms an intramolecular disulfide bond with Cys24 or a mixed disulfide with MSH under oxidative stress
-
additional information
-
the enzyme preserves a Cys-Pro-Phe-Cys active-site motif, which is presumed to be an exclusive characteristic of the DsbA-mycoredoxin 1 (Mrx1) cluster. Cys24 is the resolving Cys residue, while Cys21 is the nucleophilic cysteine that is oxidized to a sulfenic acid and then forms an intramolecular disulfide bond with Cys24 or a mixed disulfide with MSH under oxidative stress
-
additional information
-
the enzyme preserves a Cys-Pro-Phe-Cys active-site motif, which is presumed to be an exclusive characteristic of the DsbA-mycoredoxin 1 (Mrx1) cluster. Cys24 is the resolving Cys residue, while Cys21 is the nucleophilic cysteine that is oxidized to a sulfenic acid and then forms an intramolecular disulfide bond with Cys24 or a mixed disulfide with MSH under oxidative stress
-
additional information
-
the enzyme preserves a Cys-Pro-Phe-Cys active-site motif, which is presumed to be an exclusive characteristic of the DsbA-mycoredoxin 1 (Mrx1) cluster. Cys24 is the resolving Cys residue, while Cys21 is the nucleophilic cysteine that is oxidized to a sulfenic acid and then forms an intramolecular disulfide bond with Cys24 or a mixed disulfide with MSH under oxidative stress
-
additional information
-
the enzyme preserves a Cys-Pro-Phe-Cys active-site motif, which is presumed to be an exclusive characteristic of the DsbA-mycoredoxin 1 (Mrx1) cluster. Cys24 is the resolving Cys residue, while Cys21 is the nucleophilic cysteine that is oxidized to a sulfenic acid and then forms an intramolecular disulfide bond with Cys24 or a mixed disulfide with MSH under oxidative stress
-
Show AA Sequence and Transmembrane Helices (25742 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
107000
108000
110000
116000
gel filtration, the C-terminal fragment comprising residues 441-491 contributes to the anomalous molecular mass determination by gel filtration
120000
140000
15000
x * 15000, isozyme pdi-15, SDS-PAGE
21100
40000
x * 40000, isozyme pdi-40, SDS-PAGE
45000
x * 45000, recombinant PDI-1, SDS-PAGE, x * 80000, recombinant PDI-2, SDS-PAGE
47000
x * 47000, isozyme pdi-47, SDS-PAGE
48074
x * 48074, PDI-P5, sequence calculation, x * 56859, PDIA3, sequence calculation
50430
52000
53100
-
x * 53100, oxidized enzyme, calculated from amino acid sequence
55000
56000
56859
x * 48074, PDI-P5, sequence calculation, x * 56859, PDIA3, sequence calculation
57000
58000
58900
-
x * 58900, SDS-PAGE under reducing conditions, other bands with MW 53800 and 55200 represent proteolytic degradation products of the 58900 MW protein
60000
62000
63000
65000
80000
x * 45000, recombinant PDI-1, SDS-PAGE, x * 80000, recombinant PDI-2, SDS-PAGE
85000
x * 55000, recombinant PDI, SDS-PAGE, x * 85000, recombinant GST-tagged PDI, SDS-PAGE
additional information
-
Zn2+ induces formation of larger enzyme aggregates with MW up to 600 kDa and above
52000
-
2 * 55000, about, sequence calculation, 2 * 52000, analytical ultrafiltration
52000
x * 52000, isozyme pdi-52, SDS-PAGE
52000
-
x * 52000, native enzyme, SDS-PAGE, x * 55000, recombinant His-tagged enzyme, SDS-PAGE
55000
-
x * 55000, SDS-PAGE, another band with MW 45000 represents a proteolytic degradation product
55000
-
2 * 55000, about, sequence calculation, 2 * 52000, analytical ultrafiltration
55000
-
x * 52000, native enzyme, SDS-PAGE, x * 55000, recombinant His-tagged enzyme, SDS-PAGE
55000
x * 55000, recombinant PDI, SDS-PAGE, x * 85000, recombinant GST-tagged PDI, SDS-PAGE
57000
-
2 * 57000, SDS-PAGE under reducing and nonreducing conditions, association between subunits is noncovalent
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homotetramer
4 * 72397, PDIL2-3, calculated from amino acid sequence
monomer
trimer
additional information
?
-
x * 55000, SDS-PAGE, another band with MW 45000 represents a proteolytic degradation product
?
-
x * 52000, native enzyme, SDS-PAGE, x * 55000, recombinant His-tagged enzyme, SDS-PAGE
?
x * 55000, recombinant PDI, SDS-PAGE, x * 85000, recombinant GST-tagged PDI, SDS-PAGE
?
-
x * 58900, SDS-PAGE under reducing conditions, other bands with MW 53800 and 55200 represent proteolytic degradation products of the 58900 MW protein
?
x * 48074, PDI-P5, sequence calculation, x * 56859, PDIA3, sequence calculation
?
x * 70000, isoform PDIL2, SDS-PAGE
?
x * 69000, isoform PDIL3A, SDS-PAGE
?
x * 40000, isoform PDIL4D, SDS-PAGE
?
x * 47000, isoform PDIL5A, SDS-PAGE
?
x * 60000, isoform PDIL1Aalpha, SDS-PAGE
?
x * 60000, isoform PDIL1B, SDS-PAGE
?
x * 45000, recombinant PDI-1, SDS-PAGE, x * 80000, recombinant PDI-2, SDS-PAGE
dimer
-
2 * 57000, SDS-PAGE under reducing and nonreducing conditions, association between subunits is noncovalent
dimer
-
DsbC contains an N-terminal dimerization domain followed by a linker helix both involved in protein dimerization, the linker helix helps separate the C-terminal catalytic domains
dimer
-
DsbG is a homodimer with an N-terminal dimerization domain on each subunit, crystal structure
dimer
-
DsbC dimerizes to form a protein binding site flanked by two catalytic thioredoxin domains
dimer
-
V-shaped homodimeric modular structures of the dimerization domains and dimer interface of DsbC and DsbG, the dimerization domains fold independently of the catalytic portions of the full-length molecules, overview, each dimeric molecule contains two separate C-terminal thioredoxin-fold domains, joined by hinged helical stalks to a single N-terminal dimerization domain formed from the N-terminal 67 residues of each monomer
dimer
-
2 * 55000, about, sequence calculation, 2 * 52000, analytical ultrafiltration
additional information
CYO1 has a C4-type zinc finger domain, putative enzyme topology, overview
additional information
-
CYO1 has a C4-type zinc finger domain, putative enzyme topology, overview
additional information
-
a multidomain protein, tertiary structure and function analysis under pressure conditions above 100 MPa, overview
additional information
-
tryptic peptide preparation and analysis by MALDI-MS/MS and LC-ESI-MS/MS methods, peptide mapping and amino acid sequence determination, sequence comparison, overview
additional information
formation of an intramolecular disulfide bond Cys21-Cys24 in the enzyme structure under oxidative stress
additional information
-
formation of an intramolecular disulfide bond Cys21-Cys24 in the enzyme structure under oxidative stress
additional information
-
formation of an intramolecular disulfide bond Cys21-Cys24 in the enzyme structure under oxidative stress
-
additional information
-
formation of an intramolecular disulfide bond Cys21-Cys24 in the enzyme structure under oxidative stress
-
additional information
-
formation of an intramolecular disulfide bond Cys21-Cys24 in the enzyme structure under oxidative stress
-
additional information
-
formation of an intramolecular disulfide bond Cys21-Cys24 in the enzyme structure under oxidative stress
-
additional information
-
formation of an intramolecular disulfide bond Cys21-Cys24 in the enzyme structure under oxidative stress
-
additional information
-
formation of an intramolecular disulfide bond Cys21-Cys24 in the enzyme structure under oxidative stress
-
additional information
-
protein disulfide isomerase-related chaperone Wind contains a thioredoxin fold domain and a C-terminal D-domain unique in PDI-D proteins
additional information
-
the catalytic domain, residues 88-231, shows a thioredoxin fold with a helical insert
additional information
-
the enzyme structure contains two thioredoxin-like domains, a and a', and an ERp29c domain, determination by peptide mapping with either trypsin or V8 protease, domain structures, overview
additional information
-
isoform PDIL-1 associates with the precursor of a seed storage protein, proglycinin, and with the alpha' subunit of the seed storage protein beta-conglycinin
additional information
-
isoform PDIL-2 associates with the precursor of a seed storage protein, proglycinin, and with the alpha' subunit of the seed storage protein beta-conglycinin
additional information
-
GmPDIL-3a and GmPDIL-3b are plant endoplasmic reticulum PDI family proteins containing the nonclassic redox center motif CXXS? C
additional information
PDI is a multifunctional enzyme that acts as beta subunit in prolyl 4-hydroxylases and as a subunit in the microsomal triglyceride transfer protein
additional information
-
PDI consist of 2 catalytically active domains, a and a', and two inactive ones b and b', all four domains have a thioredoxin fold, domain b' contains he primary peptide binding site
additional information
-
PDI domain organization, domains a, b, b', a', PDI and P5 contain both two thioredoxin-like domains, domains a and a', at the N-terminus and the C-terminus, respectively, are homologous to thioredoxin and both have an independent active site, each active site contains 2 cysteine residues within the sequence WCGHCK, overview
additional information
-
PDI domain organization, 5 domains a, b, b', a', and c, the acidic C-terminal domain c, residues 463-491, stabilizes the chaperone function of the enzyme
additional information
the four domains a, b, b', and a' are arranged in an annular manner
additional information
domain structure of isozymes, comparison, overview
additional information
domain structure of isozymes, comparison, overview
additional information
domain structure of isozymes, comparison, overview
additional information
domain structure of isozymes, comparison, overview
additional information
ERp27 is a two-domain protein homologous to the non-catalytic b and b' domains of protein disulfide isomerase, domain structure, thioredoxin site structure and involved residues, overview
additional information
-
ERp27 is a two-domain protein homologous to the non-catalytic b and b' domains of protein disulfide isomerase, domain structure, thioredoxin site structure and involved residues, overview
additional information
determination and analysis of the crystal structure of the bb domains of ERp57, overview
additional information
-
reconstitution of the Ero1-Lalpha/protein disulfide isomerase oxidative folding system in vitro. The a' domain of protein disulfide isomerase is much more active than the a domain in Ero1-Lalpha-mediated folding. The minimal element for binding to Ero1-Lalpha are core element b, linker x and the a domain
additional information
-
PDI can directly interact with estrogen receptor alpha, but it does not interact with estrogen receptor beta
additional information
-
PDIp exists predominantly as monomer under reducing conditions, but the dimeric form is significantly increased following the removal of the reducing agent, due to the formation of an inter-subunit disulfide bond. The oxidized PDIp exposes more hydrophobic patches and is more sensitive to protease digestion. The formation of the inter-subunit disulfide bond is mainly contributed by its non-active cysteine residue C4. The formation of the inter-subunit disulfide bond is redox-dependent and is favored under oxidizing conditions. PDIp can function as a chaperone to form stable complexes with various non-native cellular proteins, particularly under oxidizing conditions
additional information
the protein disulfide isomerase exhibits a saturable, substrate binding site. NMR structural analysis of peptide binding pocket of b and b' domains, and interaction analysis of b and b' domains of PDI, the b' domain tends to form dimers, while the b domain moderates the tendency of the b' domain to dimerize and significantly slows interconversion, overview
additional information
-
the protein disulfide isomerase exhibits a saturable, substrate binding site. NMR structural analysis of peptide binding pocket of b and b' domains, and interaction analysis of b and b' domains of PDI, the b' domain tends to form dimers, while the b domain moderates the tendency of the b' domain to dimerize and significantly slows interconversion, overview
additional information
-
the enzyme molecule has four domains a,a', b, and b', each possessing a thioredoxin fold, the domain a and a' show catalytic sites with the Cys-Gly-His-Cys motif, the b and b' domains possess substrate binding sites, domains b' and a' are linked via linker x, and the enbzyme also posseses a C-terminal acidic alpha-helix containing the endoplasmic reticulum retention signal, domain structure, overview
additional information
the two catalytic domains of PDIp, a and a', which contain the WCGHC and WCTHC motifs, respectively, may be responsible for its enzymatic activity, whereas the two non-catalytic domains, b and b', may be involved in substrate-binding
additional information
-
the two catalytic domains of PDIp, a and a', which contain the WCGHC and WCTHC motifs, respectively, may be responsible for its enzymatic activity, whereas the two non-catalytic domains, b and b', may be involved in substrate-binding
additional information
-
the enzyme molecule has four domains a,a', b, and b', each possessing a thioredoxin fold, the domain a and a' show catalytic sites with the Cys-Gly-His-Cys motif, the b and b' domains possess substrate binding sites, domains b' and a' are linked via linker x, and the enbzyme also posseses a C-terminal acidic alpha-helix containing the endoplasmic reticulum retention signal, domain structure, overview
additional information
the enzyme has a modular structure with four thioredoxin-like domains, a, b, b', and a', along with a C-terminal extension. The homologous a and a' domains contain one cysteine pair in their active site directly involved in thiol-disulfide exchange reactions, while the b' domain putatively provides a primary binding site for unstructured regions of the substrate polypeptides, structure determination and analysis by NMR and small-angle X-ray scattering methods, domain arrangements and redox behaviour, overview
additional information
-
primary and secondary PDi structure analysis, overview
additional information
-
in solution at low concentration, enzyme comprises mainly monomers. At increasing concentrations, fractions of dimers and higher order oligomers are observed. Oligomerization is not driven by formation of intermolecular disulfide bonds, but by non-covalent interactions
additional information
-
structural analysis and comparison of PDIs from different Plasmodium species
additional information
-
structural analysis and comparison of PDIs from different Plasmodium species
-
additional information
structure determination and molecular modeling, overview
additional information
-
structure determination and molecular modeling, overview
additional information
-
structural analysis and comparison of PDIs from different Plasmodium species
additional information
structural analysis and comparison of PDIs from different Plasmodium species
additional information
-
structural analysis and comparison of PDIs from different Plasmodium species
additional information
-
structural analysis and comparison of PDIs from different Plasmodium species
-
additional information
structural analysis and comparison of PDIs from different Plasmodium species
additional information
-
structural analysis and comparison of PDIs from different Plasmodium species
additional information
-
structural analysis and comparison of PDIs from different Plasmodium species
-
additional information
structural analysis and comparison of PDIs from different Plasmodium species
additional information
-
structural analysis and comparison of PDIs from different Plasmodium species
additional information
-
PDI domain organization, 5 domains a, b, b', a', and c, domains a and a' are homologous to thioredoxin and both have an independent active site, each active site contains 2 cysteine residues within the sequence WCGHCK, domain structure and electrostatic surface, overview
additional information
comparison of structures of b and b' domains and the bb' fragments of ERp57 and ERp72, modelling, overview
additional information
-
comparison of structures of b and b' domains and the bb' fragments of ERp57 and ERp72, modelling, overview
additional information
-
the enzyme molecule has four domains a,a', b, and b', each possessing a thioredoxin fold, the domain a and a' show catalytic sites with the Cys-Gly-His-Cys motif, the b and b' domains possess substrate binding sites, domains b' and a' are linked via linker x, and the enzyme also posseses a C-terminal acidic alpha-helix containing the endoplasmic reticulum retention signal, domain structure, overview
additional information
-
non-active site cysteines form a disulfide bridge that is stable even under very reducing environment destabilizing the N-terminal active site disulfide which becomes a 18fold better oxidant by this way
additional information
-
the catalytic domains a and a' are responsible for the oxidase and the isomerase activity, respectively
additional information
-
domain arrangement: two catalytically inactive thioredoxin domains inserted between two catalytically active thioredoxin domains and an acidic C-terminal tail, the four thioredoxin domains form the shape of a twisted U with the active sites facing each other across the long sides, the inside surface is enriched in hydrophobic residues facilitating interactions with misfolded proteins, all 5 domains of PDI are required for full catalytic activity
additional information
-
PDI domain organization, Eug1p, Mpd1p, Mpd2p, and Eps1p have only one catalytic domain with 2 cysteines, overview
additional information
the PDIA3 sequence contains two PDI-typical thioredoxin active sites of WCGHC
additional information
-
the PDIA3 sequence contains two PDI-typical thioredoxin active sites of WCGHC
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
acetylation
glutathionylation
glycoprotein
no glycoprotein
phosphoprotein
S-nitrosylation
additional information
acetylation
acetylation of the active site-flanking lysine residues can act to reversibly modulate enzyme activity
glycoprotein
-
the enzyme has 5 N-glycosylation sites all modified in vivo
glycoprotein
-
expression in Bombyx mori results in production of mostly non-N-glycosylated and some N-glycosylated recombinant protein
glycoprotein
-
the enzyme has 5 N-glycosylation sites all modified in vivo
-
glycoprotein
both enzyme forms are N-glycosylated, PDI-1 contains 2 N-glycosylation sites, PDI-2 contains 12 sites
S-nitrosylation
-
the enzyme is primarily S-nitrosylated at Cys-343. S-nitrosylation of Cys-343 is slowly reversible by glutathione. Reduced enzyme is converted to S-nitrosylated species and oxidized enzyme by S-nitrosocysteine or S-nitrosoglutathione
additional information
-
PDIp exists predominantly as monomer under reducing conditions, but the dimeric form is significantly increased following the removal of the reducing agent, due to the formation of an inter-subunit disulfide bond. The oxidized PDIp exposes more hydrophobic patches and is more sensitive to protease digestion. The formation of the inter-subunit disulfide bond is mainly contributed by its non-active cysteine residue C4. The formation of the inter-subunit disulfide bond is redox-dependent and is favored under oxidizing conditions. PDIp can function as a chaperone to form stable complexes with various non-native cellular proteins, particularly under oxidizing conditions
additional information
-
in vivo, protein disulfide isomerase is present in two semi-oxidized forms in which either the first active site in the a domain or the second active site in the a' domain is oxidized. In HEK-293 cells, about 50% of enzyme is fully reduced, in 18% a domain is oxidized, a' reduced, in 15%, the a domain is reduced, a' oxidized, and 16% of enzyme are fully oxidized
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified native and selenomethionine-labeled DsbG in oxidized and in redox-mixed state, DsbG is oxidized by 1.7 mM (1,10-phenanthroline)Cu(II), crystallization in 20% PEG 4000, 0.1 M sodium citrate, pH 3.8-4.2, and 0.2 M ammonium sulfate, X-ray diffraction structure determination and analysis at 1.7-2.0 A resolution
-
purified recombinant His6-tagged DsbC and DsbG dimerization domains, sitting drop vapour-diffusion method, 4-6 mg/ml protein in 25 mM HEPES, pH 7.5, 150 mM NaCl, 0.001 ml of protein and of reservoir solution, containing 2.0 M Li2SO4, 0.1 M MgSO4 and 5% 2-propanol, pH 4.5, are mixed, for crystallization of DsbG also addition of 0.2 M CdCl2 and 33% MPD, X-ray diffraction structure determination and analysis at 2.0 and 1.9 A, respectively
-
purified recombinant reduced DsbC, hanging drop vapour diffusion method, the reservoir solution contains 0.2 M Li2SO4, o.1 M Tris, pH8.4, and 20% PEG 4000, 0.0015 ml of protein and of reservoir solution are mixed, X-ray diffraction reduced structure determination and analysis at 2.5 A resolution
-
ERp57 and its isolated bb' and b' domains in complex with the lectin chaperone calnexin, hanging drop vapour diffusion method, equilibration of 14 mg/ml protein in 50 mM Tris-HCl, 0.15 M NaCl, 1 mM DTT, pH 7.5, against 30% w/v PEG 3350, 0.1 M (NH4)2SO4, 0.1 M HEPES buffer, pH 7.5, for 1-3 days at 20°C, X-ray diffraction structure determination and analysis at 2.0 A resoution
hanging drop vapor diffusion method, using 0.01 M zinc chloride, 20% (w/v) polyethylene glycol 6000, and 0.1 M Tris-HCl (pH 8.0)
hanging drop vapor diffusion method, using 0.2 M ammonium sulfate, 0.1 M bis-Tris pH 5.5, 25% (w/v) PEG 3350
hanging-drop vapour-diffusion, mixing of 0.003 ml protein solution i.e. 15 mg/ml protein, 25 mM HEPES, pH 7.5 with 0.003 mL reservoir solution containing 20-23% polyethylene glycol 5000, 200 mM ammonium acetate, 100 mM HEPES, pH 7.5 and 5% glycerol
-
molecular modeling offers a role for the conserved residue R103 in coordinating the oxidative transition-state complex
small angle X-ray scattering analysis of purified recombinant wild-type and deletion mutant PDIs, structure modeling, the enzyme forms an approximately flat elliptical cylinder
in complex with alpha-synuclein, using 0.1 M HEPES buffer (pH 7.5) containing 25% (w/v) PEG3350
sitting drop vapor diffusion method, using 30% (w/v) PEG 8000, 0.1 M MES buffer, pH 6.0, 80 mM calcium acetate
N-terminally truncated form of the protomer with two helices of the trimerization stem removed, generating a protein with dithiol oxidase rather than disulfide isomerase activity, hanging drop vapor diffusion method, using 0.1 M HEPES pH 7, 32%(v/v) Jeffamine M-600
purified recombinant b and b' domains and the bb' fragments of ERp57 and ERp72, hanging drop vapor diffusion method, 0.002 ml protein solution containing 10 mg/ml protein in 50 mM Tris-HCl, pH 7.5, 0.15 M NaCl, and 1 mM DTT, are mixed with 0.002 ml reservoir solution containing 18% w/v PEG MME 2000, 25% glycerol, and 0.1 M Tris, pH 8.0, suspended over 1 ml reservoir solution, 1-3 days, 20°C, X-ray diffraction structure determination and analysis at 1.9 A resolution, overview
hanging drop vapor diffusion method, using 24% (w/v) PEG 4000, 100 mM sodium acetate, pH 6.4, 25 mM sodium citrate, pH 6.4, and 17% (v/v) glycerol
purified recombinant residues 23-522 of PDI1, X-ray diffraction structure determination and analysis at 2.4 A resolution, modeling
-
to 3.7 A resolution. PDI is a highly flexible molecule with its catalytic domains, a and a', representing two mobile arms connected to a more rigid core composed of the b and b' domains. The linker between the a domain and the core is more susceptible to degradation than that connecting the a' domain to the core. Molecular flexibility is essential for the enzymatic activity in vitro and in vivo
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C51S
-
the mutant shows reduced reductase and oxidase activities compared to the recombinant wild type enzyme PDI-A
C55S
-
the mutant shows reduced reductase and oxidase activities compared to the recombinant wild type enzyme PDI-A
C85S/C92S
-
the mutant shows reduced reductase and oxidase activities compared to the recombinant wild type enzyme PDI-A
C92S
-
the mutant shows reduced reductase and oxidase activities compared to the recombinant wild type enzyme PDI-A
K56G
-
the mutant shows reduced reductase and oxidase activities compared to the recombinant wild type enzyme PDI-A
C24S
C27S
-
site-directed mutagenesis, unaltered Pipe processing efficiency compared to the wild-type enzyme
D29N
-
site-directed mutagenesis, unaltered Pipe processing efficiency compared to the wild-type enzyme
D31N
-
site-directed mutagenesis, unstable protein that still dimerizes but then aggregates, unaltered Pipe processing efficiency compared to the wild-type enzyme
D31N/R41S
-
site-directed mutagenesis, monomeric mutant, slightly decreased Pipe processing efficiency compared to the wild-type enzyme
D50A
-
site-directed mutagenesis, inactive mutant, normal dimerization
D50N
-
site-directed mutagenesis, decreased Pipe processing efficiency compared to the wild-type enzyme
D50S
-
site-directed mutagenesis, altered Pipe targeting compared to the wild-type enzyme, normal dimerization
D85N
-
site-directed mutagenesis, unaltered Pipe processing efficiency compared to the wild-type enzyme
E32K
-
site-directed mutagenesis, unaltered Pipe processing efficiency compared to the wild-type enzyme
E60A
-
site-directed mutagenesis, unaltered Pipe processing and targeting efficiency compared to the wild-type enzyme
E60Q
-
site-directed mutagenesis, decreased Pipe processing efficiency compared to the wild-type enzyme
E60Y
-
site-directed mutagenesis, unaltered Pipe processing and targeting efficiency compared to the wild-type enzyme
E88K
-
site-directed mutagenesis, unaltered Pipe processing efficiency compared to the wild-type enzyme
E88Q
-
site-directed mutagenesis, unaltered Pipe processing efficiency compared to the wild-type enzyme
E90R
-
site-directed mutagenesis, unaltered Pipe processing efficiency compared to the wild-type enzyme
E90R/D29N
-
site-directed mutagenesis, unaltered Pipe processing efficiency compared to the wild-type enzyme
E90R/E60A
-
site-directed mutagenesis, unaltered Pipe processing efficiency compared to the wild-type enzyme
G87S
-
site-directed mutagenesis, unaltered Pipe processing efficiency compared to the wild-type enzyme
H59Y
-
site-directed mutagenesis, unaltered Pipe processing efficiency compared to the wild-type enzyme
K58S
-
site-directed mutagenesis, unaltered Pipe processing efficiency compared to the wild-type enzyme
K84D
-
site-directed mutagenesis, decreased Pipe processing efficiency compared to the wild-type enzyme
K84N
-
site-directed mutagenesis, unaltered Pipe processing efficiency compared to the wild-type enzyme
K84S
-
site-directed mutagenesis, unaltered Pipe processing efficiency compared to the wild-type enzyme
L219S/E212Q
-
site-directed mutagenesis, decreased Pipe processing efficiency compared to the wild-type enzyme
L232K
-
site-directed mutagenesis, increased Pipe processing efficiency compared to the wild-type enzyme
P106D
-
site-directed mutagenesis, similar to the wild-type enzyme, altered conformation
R215A
-
site-directed mutagenesis, unaltered Pipe processing efficiency but eliminated Pipe targeting compared to the wild-type enzyme
R218D
-
site-directed mutagenesis, increased Pipe processing efficiency compared to the wild-type enzyme
R41S
-
site-directed mutagenesis, sligtly reduced dimerization of the mutant and processing of Pipe
T25K
-
site-directed mutagenesis, unaltered Pipe processing efficiency compared to the wild-type enzyme
T63K
-
site-directed mutagenesis, unaltered Pipe processing efficiency compared to the wild-type enzyme
V28D
-
site-directed mutagenesis, monomeric mutant, no dimerization, mutant aggregates
V28Y
-
site-directed mutagenesis, monomeric mutant, no dimerization, mutant aggregates
Y53S
-
site-directed mutagenesis, decreased Pipe processing efficiency compared to the wild-type enzyme
Y55K
-
site-directed mutagenesis, mutant shows increased affinity for substrate Pipe but decreased processing efficiency compared to the wild-type enzyme
Y55K/D31N/R41S
-
site-directed mutagenesis, slightly decreased Pipe processing efficiency compared to the wild-type enzyme
Y55S
-
site-directed mutagenesis, decreased Pipe processing efficiency compared to the wild-type enzyme
Y86F
-
site-directed mutagenesis, unaltered Pipe processing efficiency compared to the wild-type enzyme
Y86L
-
site-directed mutagenesis, highly decreased Pipe processing efficiency compared to the wild-type enzyme
Y86Q
-
site-directed mutagenesis, highly decreased Pipe processing efficiency compared to the wild-type enzyme
Y86S
-
site-directed mutagenesis, unaltered Pipe processing efficiency compared to the wild-type enzyme
C312A
-
the level of S-nitrosylation of the mutant in over-expressed cells is similar to that of the wild type enzyme
C312A/C343A
-
the level of S-nitrosylation of the mutant in over-expressed cells is substantially lower than that of the wild type enzyme
C343A
-
the level of S-nitrosylation of the mutant in over-expressed cells is substantially lower than that of the wild type enzyme
C343S
-
the level of S-nitrosylation of the mutant in over-expressed cells is substantially lower than that of the wild type enzyme
D292N
the mutation is associated with amyotrophic lateral sclerosis, causing motor neuron dysfunction
E231A/W232A/D233G
site-directed mutagenesis, the ERp27 mutant shows a similar structure as wild-type ERp57, but highly reduced binding to ERp57 compared to the wild-type enzyme
E231K
site-directed mutagenesis, the ERp27 mutant shows a similar structure as wild-type ERp57, but highly reduced binding to ERp57 compared to the wild-type enzyme
F258W/I272A
-
the mutant shows stronger binding of signal peptide peptidase, SPP, than the wild-type enzyme. PDI F258W/I272A-myc competes with endogenous PDI for SPP and remains attached to SPP, leading to a reduced pool of SPP available for US2-mediated degradation of MHC class I
F299W
-
site-directed mutagenesis, the mutation reduces the interaction between the two chaperones ERP-57 and CANX, but no difference between wild-type and mutant ERP-57 chaperone is observed, even when CANX is additionally transfected, in plasma membrane expression of the enzyme, overview
F449R
F449W
F449Y
G448R
I196W
site-directed mutagenesis, the ERp27 mutant shows a structure and ERp57 binding similar to the wild-type enzyme
I272A
K274A
site-directed mutagenesis, the mutant shows affected interaction with calnexin
K332A
site-directed mutagenesis, the mutant shows binding affinity with calnexin identical to wild-type enzyme
K401Q
the mutant shows about 1.5fold less activity than the wild type enzyme
K450A
K57A/K401A
the mutant shows about 4fold less activity than the wild type enzyme
K57E/K401E
the mutant shows about 7fold less activity than the wild type enzyme
K57Q
the mutant shows about 1.5fold less activity than the wild type enzyme
K57Q/K401Q
the mutant shows about 2.5fold less activity than the wild type enzyme
L343A
-
the mutant is more sensitive to proteinase K than wild type enzyme. The mutant shows the same chaperone activity as that of wild type PDI
L453E
Q265L
-
the mutant displays similar E2-binding activity as the corresponding wild type proteins
R280A
site-directed mutagenesis, the mutant shows a structure reduced binding of ERp27, wild-type and mutants, as compared to the wild-type ERp57
R282A
site-directed mutagenesis, the mutant shows affected interaction with calnexin
R300H
the mutation is associated with amyotrophic lateral sclerosis, causing motor neuron dysfunction
R444A
H278L
-
the mutant protein does not have an appreciable E2-binding activity
-
Q265L
-
the mutant displays similar E2-binding activity as the corresponding wild type proteins
-
Cys59/62/195/198Ala
the PDIL2-3 active site mutant is evenly dispersed within the endoplasmic reticulum lumen
C34S
-
site-directed mutagenesis, the mutant shows impaired lipase activity, the defect cannot be rescued by constitutive expression of lipA gene encoding lipase A
C146S
-
site-directed mutagenesis, very highly reduced reduction activity compared to the wild-type enzyme
C35A
-
site-directed mutagenesis, reduced reduction activity compared to the wild-type enzyme
C35A/C146S
-
site-directed mutagenesis, very highly reduced reduction activity compared to the wild-type enzyme
C294S/C325S
-
site-directed mutagenesis, exchange of the enzyme's cysteine residues involved in rearrangement of disulfide bonds by function in thiol/disulfide exchange
C55S/C379S
-
The double active site mutant Cys55Ser, Cys379Ser is not capable of catalyzing protein folding
G36A
-
Mutagenesis of Trp34 to Ser and Gly36 to Ala has little effect on activity. Mutagenesis of amino acid residues within the active site sequence, Trp34 to a Ser and Gly36 to an Ala has little effect on activity
L39R
-
Mutagenesis of Lys39 to an Arg results in only a modest loss of activity
W34S
-
Mutagenesis of Trp34 to Ser and Gly36 to Ala has little effect on activity. Mutagenesis of amino acid residues within the active site sequence, Trp34 to a Ser and Gly36 to an Ala has little effect on activity
C409A
-
site-directed mutagenesis, mutation of the second cysteine of the active site, the mutant shows similar activity to the wild-type enzyme
C64A
-
site-directed mutagenesis, mutation of the second cysteine of the active site, the mutant shows similar activity to the wild-type enzyme
C90A
-
site-directed mutagenesis, mutation of a non-active site cysteine residue, reduced oxidase and isomerase activities compared to the wild-type enzyme
C90A/C97A
-
site-directed mutagenesis, mutation of both non-active site cysteine residues, 60% and 80% reduced oxidase and isomerase activities, respectively, compared to the wild-type enzyme
C97A
-
site-directed mutagenesis, mutation of a non-active site cysteine residue, reduced oxidase and isomerase activities compared to the wild-type enzyme
additional information
C24S
site-directed mutagenesis, the mutant shows increased activity compared to wild-type enzyme with a mixed disulfide substrate
C24S
-
site-directed mutagenesis, the mutant shows increased activity compared to wild-type enzyme with a mixed disulfide substrate
-
C24S
-
site-directed mutagenesis, the mutant shows increased activity compared to wild-type enzyme with a mixed disulfide substrate
-
C24S
-
site-directed mutagenesis, the mutant shows increased activity compared to wild-type enzyme with a mixed disulfide substrate
-
C24S
-
site-directed mutagenesis, the mutant shows increased activity compared to wild-type enzyme with a mixed disulfide substrate
-
C24S
-
site-directed mutagenesis, the mutant shows increased activity compared to wild-type enzyme with a mixed disulfide substrate
-
C24S
-
site-directed mutagenesis, the mutant shows increased activity compared to wild-type enzyme with a mixed disulfide substrate
-
C24S
-
site-directed mutagenesis, unaltered Pipe processing efficiency compared to the wild-type enzyme
F449R
no 4-hydroxylase activity, 85% and 93% of wild-type isomerase and reductase activity, respectively
F449R
-
mutation in the last alpha helix of domain a', 7.5-8fold reduced appearance rate of folding product RNase A
F449W
59%, 133% and 94% of wild-type 4-hydroxylase, isomerase and reductase activity, respectively
F449Y
79%, 42% and 87% of wild-type 4-hydroxylase, isomerase and reductase activity, respectively
G448R
43%, 85% and 93% of wild-type 4-hydroxylase, isomerase and reductase activity, respectively
I272A
-
the mutant shows similar proteinase K sensitivity like the wild type protein. The mutant shows significantly lower potency than wild type PDI in suppressing aggregation of denatured rhodanese
L453E
13%, 23% and 48% of wild-type 4-hydroxylase, isomerase and reductase activity, respectively
R444A
43%, 83% and 79% of wild-type 4-hydroxylase, isomerase and reductase activity, respectively
additional information
the enzyme-deficient cyo1 mutant in Arabidopsis thaliana has albino cotyledons but normal green true leaves, chloroplasts develop abnormally in cyo1 mutant plants grown in the light, but etioplasts are normal in mutants grown in the dark, albino phenotype, overview
additional information
-
the enzyme-deficient cyo1 mutant in Arabidopsis thaliana has albino cotyledons but normal green true leaves, chloroplasts develop abnormally in cyo1 mutant plants grown in the light, but etioplasts are normal in mutants grown in the dark, albino phenotype, overview
additional information
-
certain T-DNA insertions in isoform PDIL2-1 have reduced seed set, due to delays in embryo sac maturation. These mutations act sporophytically, and funicular and micropylar pollen tube guidance are disrupted. A PDIL2-1-yellow fluorescent protein fusion is mainly localized in the endoplasmic reticulum and is expressed in all tissues examined. In ovules, expression in integument tissues is much higher in the micropylar region in later developmental stages, but there is no expression in embryo sacs
additional information
expression of full protein, domain a + part of domain b comprised of residues 1-162, parts of domains b + b' comprised of residues 163-315, and part of domain b' + domain a' including c comprised of resiudes 316-494, respectively, in Escherichia coli. Segment 1-162 lacks isomerase activity, while segment 316-494 displays wild-type like activity
additional information
-
expression of full protein, domain a + part of domain b comprised of residues 1-162, parts of domains b + b' comprised of residues 163-315, and part of domain b' + domain a' including c comprised of resiudes 316-494, respectively, in Escherichia coli. Segment 1-162 lacks isomerase activity, while segment 316-494 displays wild-type like activity
additional information
-
development of a versatile baculovirus expression and secretion system, using the enzyme as a fusion partner. Fusion improves the secretions and antibacterial activities of recombinant nuecin proteins
additional information
-
construction of a PDI-2 defective mutant, mutations in gene pdi-2 result in severe body morphology defects, uncoordinated movement, adult sterility, abnormal molting and aberrant collagen deposition, cuticle collagens are disrupted in pdi-2 mutants, role of PDI-2 in collagen biogenesis can be restored following complementation of the mutant with human PDI, complementation of the pdi-2 mutant phenotype requires intact thioredoxin active sites, overview
additional information
-
pdi-3(ka1) crosses with specific collagen and collagen enzyme mutants, three transgenic lines all express the spliced transgenic product, phenotypes and genotypes, overview
additional information
-
construction of deletion mutants DELTA28RB60, L28 and L50
additional information
-
construction of deletion mutants DELTA28RB60, L28 and L50
-
additional information
ncgl2478 gene in-frame deletion increasing the size of growth inhibition zones. Site-directed mutagenesis confirms Cys24 as the resolving Cys residue, while Cys21 is the nucleophilic cysteine that is oxidized to a sulfenic acid and then forms an intramolecular disulfide bond with Cys24 or a mixed disulfide with MSH under oxidative stress
additional information
-
ncgl2478 gene in-frame deletion increasing the size of growth inhibition zones. Site-directed mutagenesis confirms Cys24 as the resolving Cys residue, while Cys21 is the nucleophilic cysteine that is oxidized to a sulfenic acid and then forms an intramolecular disulfide bond with Cys24 or a mixed disulfide with MSH under oxidative stress
additional information
-
ncgl2478 gene in-frame deletion increasing the size of growth inhibition zones. Site-directed mutagenesis confirms Cys24 as the resolving Cys residue, while Cys21 is the nucleophilic cysteine that is oxidized to a sulfenic acid and then forms an intramolecular disulfide bond with Cys24 or a mixed disulfide with MSH under oxidative stress
-
additional information
-
ncgl2478 gene in-frame deletion increasing the size of growth inhibition zones. Site-directed mutagenesis confirms Cys24 as the resolving Cys residue, while Cys21 is the nucleophilic cysteine that is oxidized to a sulfenic acid and then forms an intramolecular disulfide bond with Cys24 or a mixed disulfide with MSH under oxidative stress
-
additional information
-
ncgl2478 gene in-frame deletion increasing the size of growth inhibition zones. Site-directed mutagenesis confirms Cys24 as the resolving Cys residue, while Cys21 is the nucleophilic cysteine that is oxidized to a sulfenic acid and then forms an intramolecular disulfide bond with Cys24 or a mixed disulfide with MSH under oxidative stress
-
additional information
-
ncgl2478 gene in-frame deletion increasing the size of growth inhibition zones. Site-directed mutagenesis confirms Cys24 as the resolving Cys residue, while Cys21 is the nucleophilic cysteine that is oxidized to a sulfenic acid and then forms an intramolecular disulfide bond with Cys24 or a mixed disulfide with MSH under oxidative stress
-
additional information
-
ncgl2478 gene in-frame deletion increasing the size of growth inhibition zones. Site-directed mutagenesis confirms Cys24 as the resolving Cys residue, while Cys21 is the nucleophilic cysteine that is oxidized to a sulfenic acid and then forms an intramolecular disulfide bond with Cys24 or a mixed disulfide with MSH under oxidative stress
-
additional information
-
ncgl2478 gene in-frame deletion increasing the size of growth inhibition zones. Site-directed mutagenesis confirms Cys24 as the resolving Cys residue, while Cys21 is the nucleophilic cysteine that is oxidized to a sulfenic acid and then forms an intramolecular disulfide bond with Cys24 or a mixed disulfide with MSH under oxidative stress
-
additional information
-
a naturally occuring mutant strain with mutated, nonfunctional PDI shows complete resistance to infection, attachement and entry, of Chlamydia species, expression of enzymatically nonfunctional PDI can restore Chlamydia sp. attachment but not entry into mutant CHO6 cells, while expression of functional PDI restores the complete Chlamydia infection, overview
additional information
-
construction of several functional-Trx-domain mutants, that are affected in their in vivo oxidative folding activity to different extents, overview
additional information
-
the mutational introduction of the AppA nonconsecutive disulfide bond into the AppA homologue Agp, which is independent of DsbC, renders the Agp mutant dependent on DsbC, overview
additional information
-
dsbC null mutants do not show an altered phenotype, mutation of the entire DsbC disulfide isomerization pathway causes an increased sensitivity to the redox-active copper in cells
additional information
reduction of gene and protein expression by RNAi impacts tick blood feeding and oviposition. Injection of a combination of isoforms PDI-1/PDI-3 dsRNA has synergistic effects on tick viability. In PDI-1/PDI-3 dsRNA-injected ticks the midgut and cuticle are severely damaged. Disruption of PDI genes leads to a significant reduction of disulfide bond-containing vitellogenin expression in ticks
additional information
reduction of gene and protein expression by RNAi impacts tick blood feeding and oviposition. Injection of a combination of isoforms PDI-1/PDI-3 dsRNA has synergistic effects on tick viability. In PDI-1/PDI-3 dsRNA-injected ticks the midgut and cuticle are severely damaged. Disruption of PDI genes leads to a significant reduction of disulfide bond-containing vitellogenin expression in ticks
additional information
reduction of gene and protein expression by RNAi impacts tick blood feeding and oviposition. Injection of a combination of isoforms PDI-1/PDI-3 dsRNA has synergistic effects on tick viability. In PDI-1/PDI-3 dsRNA-injected ticks the midgut and cuticle are severely damaged. Disruption of PDI genes leads to a significant reduction of disulfide bond-containing vitellogenin expression in ticks
additional information
-
reduction of gene and protein expression by RNAi impacts tick blood feeding and oviposition. Injection of a combination of isoforms PDI-1/PDI-3 dsRNA has synergistic effects on tick viability. In PDI-1/PDI-3 dsRNA-injected ticks the midgut and cuticle are severely damaged. Disruption of PDI genes leads to a significant reduction of disulfide bond-containing vitellogenin expression in ticks
additional information
reduction of gene and protein expression by RNAi impacts tick viability. In PDI-2 dsRNA-injected ticks the midgut and cuticle are severely damaged. Disruption of PDI genes leads to a significant reduction of disulfide bond-containing vitellogenin expression in ticks
additional information
reduction of gene and protein expression by RNAi impacts tick viability. In PDI-2 dsRNA-injected ticks the midgut and cuticle are severely damaged. Disruption of PDI genes leads to a significant reduction of disulfide bond-containing vitellogenin expression in ticks
additional information
reduction of gene and protein expression by RNAi impacts tick viability. In PDI-2 dsRNA-injected ticks the midgut and cuticle are severely damaged. Disruption of PDI genes leads to a significant reduction of disulfide bond-containing vitellogenin expression in ticks
additional information
-
reduction of gene and protein expression by RNAi impacts tick viability. In PDI-2 dsRNA-injected ticks the midgut and cuticle are severely damaged. Disruption of PDI genes leads to a significant reduction of disulfide bond-containing vitellogenin expression in ticks
additional information
reduction of gene and protein expression by RNAi has no significant impact by itself. Injection of a combination of isoforms PDI-1/PDI-3 dsRNA has synergistic effects on tick viability. In PDI-1/PDI-3 dsRNA-injected ticks the midgut and cuticle are severely damaged. Disruption of PDI genes leads to a significant reduction of disulfide bond-containing vitellogenin expression in ticks
additional information
reduction of gene and protein expression by RNAi has no significant impact by itself. Injection of a combination of isoforms PDI-1/PDI-3 dsRNA has synergistic effects on tick viability. In PDI-1/PDI-3 dsRNA-injected ticks the midgut and cuticle are severely damaged. Disruption of PDI genes leads to a significant reduction of disulfide bond-containing vitellogenin expression in ticks
additional information
reduction of gene and protein expression by RNAi has no significant impact by itself. Injection of a combination of isoforms PDI-1/PDI-3 dsRNA has synergistic effects on tick viability. In PDI-1/PDI-3 dsRNA-injected ticks the midgut and cuticle are severely damaged. Disruption of PDI genes leads to a significant reduction of disulfide bond-containing vitellogenin expression in ticks
additional information
-
reduction of gene and protein expression by RNAi has no significant impact by itself. Injection of a combination of isoforms PDI-1/PDI-3 dsRNA has synergistic effects on tick viability. In PDI-1/PDI-3 dsRNA-injected ticks the midgut and cuticle are severely damaged. Disruption of PDI genes leads to a significant reduction of disulfide bond-containing vitellogenin expression in ticks
additional information
-
under thermally denaturing conditions of 80°C or at 1 M guanidine-HCl the wild-type PDI is still active in renaturing LDH, while the mutant abb'a', lacking the C-terminal domain c, loses its chaperone function
additional information
construction of several deletion mutants of PDI by elimination of partial domains or whole domains, overview
additional information
-
chromosomal insertion of the human PDI gene into the Saccharomyces cerevisiae PDI1 disruption mutant strain cannot rescue the mutant, the human enzyme is functionally not equivalent to the yeast enzyme, tetrad analysis, overview
additional information
construction of deletion mutants of ERp27 with deletions at the N terminus to P34 and/or at the C terminus to Leu257, overview
additional information
-
construction of deletion mutants of ERp27 with deletions at the N terminus to P34 and/or at the C terminus to Leu257, overview
additional information
-
eliminating the isomerase activity of PDI does not affect ERalpha-ERE complex formation, overview
additional information
-
transfection of EA.hy926 cells and exposure to Mn2+ results in the appearance of surface protein thiol groups, which can be found in PDI and integrin alphaVbeta3, both proteins colocalizing on the cellular surface, and the formation of the PDI-alphaVbeta3 complex, which dissociates upon reduction. The PDI-alphaVbeta3 complex induces conversion of the integrin to the ligand-competent high-affinity state
additional information
-
knockdown of PDI in MCF-7 human breast cancer cells with RNAi down-regulates estrogen receptor alpha protein but upregulates estrogen receptor beta protein, resulting in a drastic increase in estrogen receptor alpha/beta ratio, which is a crucial determinant of different cellular responses to estrogens. PDI can directly interact with estrogen receptor alpha, but it does not interact with estrogen receptor beta
additional information
-
analysis of binding and dissociation constants of various antibiotics with PDI and PDI domain deletion mutants lacking domains abb', domains b'a'c, domains aba'c
additional information
-
overexpression has significant effects on cell-cell fusion mediated by Newcastle disease virus. Overexpression results in increased membrane fusion, and enhanced production of free thiols in Newcastle disease virus fusion protein when expressed without hemagglutinin-neuraminidase protein but drecreased free thiols in Newcastle disease virus fusion protein expressed with hemagglutinin-neuraminidase protein. Overexpression favors a postfusion conformation of surface-expressed Newcastle disease virus fusion protein in the presence of hemagglutinin-neuraminidase protein
additional information
-
overexpression of isoform procollagen-proline, 2-oxoglutarate-4-dioxygenase beta subunit results in increased protein disulfide isomerase activity and abrogates the apoptosis-enhancing effect of inhibitor bacitracin. Overexpression of a mutant lacking protein disulfide isomerase activity does not increase cellular enzymic activity or block the effects of bacitracin
additional information
-
HeLa cells are transfected with PDI-targeting siRNA for PDI knockdown leading to resistance to Chlamydia inefctions
additional information
-
wild-type PDI or PDI mutated in all four redox cysteines overexpression in vascular smooth muscle cells induces spontaneous preemptive NADPH oxidase activation and Nox1 mRNA expression, with 2.5fold enhanced basal cellular ROS production and membrane NADPH oxidase activity, with 3-fold increase in Nox1, but not Nox4 mRNA, phenotype, overview. Knockdown of PDI leads to Nox1 mRNA and protein downregulation
additional information
-
transiently silencing PDI mRNA and increasing the intracellular levels of members of the PDI family, PDI, ERp72, and PDIp, have an effect on the mRNA levels, assembly and secretion of an IgG4 isotype, overview
additional information
loss of the two cysteines in the C-terminal a' domain increases the Km for substarte RNase A, and loss of an additional cysteine in the a domain resulted in an even further increase of the Km
additional information
-
loss of the two cysteines in the C-terminal a' domain increases the Km for substarte RNase A, and loss of an additional cysteine in the a domain resulted in an even further increase of the Km
additional information
-
transfection of HUVECs with PDI siRNA using electroporation by nucleofector
additional information
mutation of the cysteine residues in PDIp's active sites, resulting in mutants DELTAC1, DELTAC2 and DELTAC1DELTAC2, completely abolishes its enzymatic activity but does not affect its chaperone activity, the b-b' fragment of PDIp, which does not contain the active sites and is devoid of enzymatic activity, still has chaperone activity
additional information
-
mutation of the cysteine residues in PDIp's active sites, resulting in mutants DELTAC1, DELTAC2 and DELTAC1DELTAC2, completely abolishes its enzymatic activity but does not affect its chaperone activity, the b-b' fragment of PDIp, which does not contain the active sites and is devoid of enzymatic activity, still has chaperone activity
additional information
-
knockdown of PDI by RNA-mediated interference inhibits the degradation of MHC class I molecules catalysed by human cytomegalovirus glycoprotein US2 but not by its functional homolog US11. Overexpression of the substrate-binding mutant of PDI, but not the catalytically inactive mutant, dominant-negatively inhibits US2-mediated dislocation of MHC class I molecules by preventing their release from US2. PDI associated with signal peptide peptidase, SPP, independently of US2 and knockdown of PDI inhibits SPP-mediated degradation of CD3d but not Derlin-1-dependent degradation of CFTR DeltaF508
additional information
TXNDC5 knockdown in lung cancer cells generation of TXNDC5 mutants with individual thioredoxin-like domain being deleted. Knockdown of TXNDC5 in lung cancer cells leads to more localization of Srx in the cytosol. Mutation of cysteines in the thioredoxin domains of TXNDC5 leads to the loss of its binding to Srx. Knockdown of TXNDC5 sensitizes human lung cancer cells to endoplasmic reticulum (ER) stress-induced cell death and enhances EGF-induced MAPK activation in in A549 cells
additional information
-
TXNDC5 knockdown in lung cancer cells generation of TXNDC5 mutants with individual thioredoxin-like domain being deleted. Knockdown of TXNDC5 in lung cancer cells leads to more localization of Srx in the cytosol. Mutation of cysteines in the thioredoxin domains of TXNDC5 leads to the loss of its binding to Srx. Knockdown of TXNDC5 sensitizes human lung cancer cells to endoplasmic reticulum (ER) stress-induced cell death and enhances EGF-induced MAPK activation in in A549 cells
additional information
-
downregulation of protein disulfide isomerase gene expression by siRNA leads to an average 36.8% inhibition of gene expression and correlates with a 3.2fold increase in tumor necrosis factor alpha release into the cell supernatant
additional information
-
PDI gene silencing in NS0/2N2 cells by transfection with two different PDI siRNAs, PDI1 and PDI2, respectively. Transiently silencing PDI mRNA in NS0/2N2 cells and increasing the intracellular levels of members of the PDI family, PDI, ERp72, and PDIp, have an effect on the mRNA levels, assembly and secretion of an IgG4 isotype, overview
additional information
-
mutant Agr2-/- mice lacking AGR2 are viable but are highly susceptible to colitis, the mutant mice show a 3fold reduced Muc2 mRNA level
additional information
-
replacement of the signal sequence and ER retention sequence by those of Pichia pastoris for elimination of glycosylation sites facilitating the recombinant expression in yeast
additional information
AY919669
replacement of the signal sequence and ER retention sequence by those of Pichia pastoris for elimination of glycosylation sites facilitating the recombinant expression in yeast
additional information
-
construction of mutants deficient in either DsbA or DsbC, or both, the dsbA mutant does no longer produce extracellular enzymes elastase, alkaline phosphatase, and lipase, while in the dcbC mutant the lipase activity is doubled, introduction of dsbC into the dsbA mutant results in low extracellular lipase activity, overview
additional information
suppression of cell-surface PDI expression with antisense oligodeoxynucleotide in RPAE cells
additional information
-
construction of a mutant PDI defective in the a' domain, which bears the isomerase activity, a PDI deletion yeast mutant cannot be rescued by the rat PDI
additional information
-
a domain a'-deletion mutant shows reduced activity in refolding of RNase compared to the wild-type enzyme
additional information
-
the PDI1 disruption mutant strain cannot be rescued by chromosomal insertion of the human PDI gene, the human enzyme is not functionally equivalent to the yeast enzyme, tetrad analysis, overview
additional information
-
PDI can rescue a PDI-deficient mutant strain as well as mutants deficient in PDI homologues Eug1p, Mpd1p, Mpd2p, and Eps1p
additional information
-
the PDI1 disruption mutant strain cannot be rescued by chromosomal insertion of the human PDI gene, the human enzyme is not functionally equivalent to the yeast enzyme, tetrad analysis, overview
-
additional information
gene silencing of PDI-1 and PDI-2 by RNAi constructs does not influence the cell growth
additional information
-
gene silencing of PDI-1 and PDI-2 by RNAi constructs does not influence the cell growth
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
50
70 - 75
50
after 30 min at 50°C, the enzyme retains half of its enzyme activity
50
after 30 min at 50°C, the enzyme retains half of its enzyme activity
50
after 30 min at 50°C, the enzyme retains half of its enzyme activity
50
after 30 min at 50°C, the enzyme retains half of its enzyme activity
50
after 30 min at 50°C, the enzyme retains half of its enzyme activity
50
after 30 min at 50°C, the enzyme retains half of its enzyme activity
50
after 30 min at 50°C, the enzyme retains half of its enzyme activity
50
after 30 min at 50°C, the enzyme retains half of its enzyme activity
50
after 30 min at 50°C, the enzyme retains half of its enzyme activity
50
after 30 min at 50°C, the enzyme retains half of its enzyme activity
50
after 30 min at 50°C, the enzyme retains half of its enzyme activity
70 - 75
CxRP2 is heat sensitive losing substantial activity after 30 min at 70-75°C, overview
70 - 75
-
CxRP2 is heat sensitive losing substantial activity after 30 min at 70-75 °C, overview
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
enzyme stability is considerably higher in endosperm isolated 40 days after anthesis than in mature wheat
-
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, 1 mM phenylmethylsulfonyl fluoride, 0.5 mM DTT, 20% w/v glycerol, half-life: 20 days
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, DEAE Sephacel column chromatography, and ACA44 gel filtration
-
chelating Sepharose column chromatography and Resource Q column chromatography
-
complete His-Tag purification resin column chromatography and Superdex 200 gel filtration
-
glutathione Sepharose column chromatography, and Superdex 200 gel filtration
native enzyme from brain by anion exchange and bisphenyl A affinity chromatography, recombinant His-tagged enzyme from Escherichia coli by nickel affinity chromatography
-
native enzyme from tachyzoit extracts by tizoxanide affinity chromatography, recombinant His-tagged enzyme from Escherichia coli by Co2+ affinity chromatography
-
Ni-NTA column chromatography
Ni-Sepharose 6 column chromatography, and TSK gel G3000SW gel filtration
Ni2+-chelating Sepharose column chromatography, and Sephadex G-25 gel filtration
partial
protein disulfide isomerase activity and glutathione-insulin transhydrogenase activity, EC 1.8.4.2, are catalyzed by a single enzyme protein
-
protein disulfide-isomerase is identical with the beta-subunit of the prolyl 4-hydroxylase tetramer, alpha2beta2
-
purification of the structural domains and domain combinations expressed in Escherichia coli
-
purified from a fibronectin and fibrinogen-rich byproduct of factor VIII production
-
recombinant b and b' domains and the bb' fragments of ERp57 and ERp72 from Escherichia coli
recombinant enzyme from Escherichia coli to homogeneity and over 95% purity
recombinant GST-tagged bb' fragment and b' fragment from Escherichia coli strain Bl21(DE3) by glutathione affinity chromatography and gel filtration
recombinant GST-tagged or His-tagged enzyme from Escherichia coli strain BL21(DE3) by glutathione or nickel affinity chromatography, respectively, native enzyme partially by isoelectric focusing/2D PAGE
recombinant His-tagged DsbA and DsbC from Escherichia coli strain BL(DE3) by nickel affinity chromatography
-
recombinant His-tagged enzyme from Escherichia coli strain AD494(DE3) by nickel affinity chromatography
recombinant His-tagged mature isozymes PDIA3 and PDI-P5 from Escherichia coli strain HMS174 (DE3) by nickel affinity chromatography and anion exchange chromatography, the His-tag of PDI-P5 is cleaved off
recombinant His-tagged PDI from Escherichia coli by nickel affinnity chromatography
-
recombinant His-tagged PDI from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration
-
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
-
recombinant His-tagged wild-type and mutant PDIs from Escherichia coli strain M15 by nickel affinity and cation exchange chromatography
recombinant His-tagged wild-type and mutant proteins from Escherichia coli strain BL21(DE3) by nickel affinity and anion exchange chromatography
recombinant His-tagged wild-type PDI and mutant abb'a' from Escherichia coli strain BL21(DE3) by nickel affinity and anion exchange chromatography
-
recombinant His-tagged wild-type PDI and mutant PDI defective in the a' domain from Escherichia coli by nickel affnity chromatography
-
recombinant His6-tagged isolated dimerization domains of DsbC and DsbG from strain BL21 (DE3) by nickel affinity chromatography and gel filtration
-
recombinant His6-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration
recombinant His6-tagged wild-type and mutant Wind from Escherichia coli strain XL 1-Blue by nickel affinity chromatography
-
recombinant mature GmPDIL-3a (Thr24-Leu520) and GmPDIL-3b (Ser27-Leu523), excluding the putative signal peptides, from Escherichia coli strain BL21(DE3)
-
recombinant PDI
recombinant wild-type and mutant enzyme from Escherichia coli strain BL21(DE3) by heat precipitation at 80°C, gel filtration, and anion exchange chromatography
-
recombinant wild-type and mutant PDI from Escherichia coli to homogeneity
-
Ni2+-chelating Sepharose column chromatography, and Sephadex G-25 gel filtration
Ni2+-chelating Sepharose column chromatography, and Sephadex G-25 gel filtration
Ni2+-chelating Sepharose column chromatography, and Sephadex G-25 gel filtration
Ni2+-chelating Sepharose column chromatography, and Sephadex G-25 gel filtration
Ni2+-chelating Sepharose column chromatography, and Sephadex G-25 gel filtration
Ni2+-chelating Sepharose column chromatography, and Sephadex G-25 gel filtration
-
Ni2+-chelating Sepharose column chromatography, and Sephadex G-25 gel filtration
Ni2+-chelating Sepharose column chromatography, and Sephadex G-25 gel filtration
Ni2+-chelating Sepharose column chromatography, and Sephadex G-25 gel filtration
Ni2+-chelating Sepharose column chromatography, and Sephadex G-25 gel filtration
Ni2+-chelating Sepharose column chromatography, and Sephadex G-25 gel filtration
Ni2+-chelating Sepharose column chromatography, and Sephadex G-25 gel filtration
recombinant His-tagged enzyme from Escherichia coli strain AD494(DE3) by nickel affinity chromatography
-
recombinant His-tagged enzyme from Escherichia coli strain AD494(DE3) by nickel affinity chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cDNA cloning from library, DNA and amino acid sequence determination and analysis, genetic structure comparison and phylogenetic tree
cloning from RNA by 3' race RT-PCR, DNA and amino acid sequence determination and analysis, sequence comparison, expression as GST-tagged or His-tagged enzyme in Escherichia coli strain BL21(DE3)
DNA and amino acid sequence determination and analysis, sequence comparison and phylogenetic analysis, expression of the enzyme fused to the human tissue plasminogen activator signal sequence in Escherichia coli strain DH10B
DNA and amino acid sequence determination and anaylsis, phylogenetic tree, expression in Escherichia coli as a soluble cytoplasmic protein
DNA and amino acid sequence determination, expression of His-tagged enzyme in Escherichia coli strain DH5alpha
-
DNA sequence determination of PDI-1 and PDI-2, which show low overall identity, genomic organization and expression analysis in Trypanosoma brucei, expression of both enzyme forms as GST-tagged proteins in Escherichia coli
DNA sequence determination of testis-specific PDILT, expression in HeLa cells endoplasmic reticulum as Myc-tagged protein
-
DNA sequence determination, expression of GFP-tagged wild-type enzyme and mutants Y53S and K84D in COS-7 cells, expression of C-terminally or N-terminally His6-tagged wild-type and mutant Wind in Escherichia coli strain XL 1-Blue and in Vero cells, the affinity for substrate Pipe is higher with the N-terminally His-tagged enzyme compared to the C-terminally tagged one
-
expressed in Escherichia coli
expressed in Escherichia coli BL21 cells
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli Origami B (DE3) cells
expression in Escherichia coli
expression of b and b' domains and the bb' fragments of ERp57 and ERp72 in Escherichia coli
expression of enzymatically nonfunctional PDI can restore Chlamydia sp. attachment but not entry into mutant CHO6 cells, while expression of functional PDI restores the complete Chlamydia infection, overview
-
expression of GFP- or ORF-tagged RB60, wild-type and deletion mutants, in vitro protein synthesis using the T3 TNT-coupled reticulocyte lysate system
-
expression of GST-fusion full-length ERp57 lacking the signal sequence, A24-L505, and the bb', P134-G376, and b', F241-G376, fragments in Escherichia coli strain BL21(DE3)
expression of GST-tagged bb' fragment, residues P135-S357, and of b' fragment, residues L236-S357, in Escherichia coli strain Bl21(DE3)
expression of His-tagged enzyme in Escherichia coli strain AD494(DE3)
expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
-
expression of His-tagged wild-type and mutant PDIs in Escherichia coli strain M15
expression of His-tagged wild-type PDI and mutant abb'a' lacking the C-terminal domain c in Escherichia coli strain BL21(DE3)
-
expression of His-tagged wild-type PDI and mutant PDI defective in the a' domain, which bears the isomerase activity, in Escherichia coli
-
expression of His6-tagged isolated dimerization domains of DsbC and DsbG in strain BL21 (DE3)
-
expression of wild-type and mutant ERP-57 in COS-7 cells, co-expression with wild-type and mutant receptors, broken disulfide bond bridge mutant hGnRH receptors and calnexin, interaction analysis, overview
-
expression of wild-type and mutant PDI in Escherichia coli strain BL21(DE3)
-
functional and mutational analysis of a conserved family of three PDIs in Caenorhabditis elegans
-
functional complementation of an enzyme-deficient PDI-2-mutant strain of Caenorhabditis elegans, overview
-
gene cyo1, isolation of CYO1 from the cyo1 mutant strain by T-DNA tagging, DNA and amino acid sequence determination and analysis, functional complementation by the wild-type cyo1 gene, cyo1 expression analysis, overview
gene HlPDI-1, DNA and amino acid sequence determination and anaylsis, phylogenetic tree, functional expression in Escherichia coli strain BL21 (DE3)
gene HlPDI-2, DNA and amino acid sequence determination and anaylsis, phylogenetic tree, functional expression in Escherichia coli strain BL21 (DE3)
gene HlPDI-3, DNA and amino acid sequence determination and anaylsis, phylogenetic tree, functional expression in Escherichia coli strain BL21 (DE3)
gene ncgl2478, quantitative real?time PCR analysis, sequence comparisons, recombinant expression of His6-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
gene pdi, DNA and amino acid sequence determination and analysis, His-tagged PDI is co-expressed with the cyclotide precursor protein Oak1 in Escherichia coli strain BL21(DE3) using the pREP4 helper plasmid
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gene PDI, DNA and amino acid sequence determination and analysis, restriction mapping, expression in Escherichia coli strain MV1184
gene pdi, DNA and amino avid sequence determination and analysis, expression of PDI in Pichia pastoris strain overexpressing the Plasmodium falciparum disulfide-rich, transmission-blocking vaccine candidate protein Pfs25, isozymes A and B, the co-expression results in 3fold enhanced levels of the Pfs25 isozymes A and B as well as in enhaced PpPDI expression, overview
gene pdi, DNA and amino avid sequence determination and anaylsis, expression of PDI in Pichia pastoris strain overexpressing the Plasmodium falciparum disulfide-rich, transmission-blocking vaccine candidate protein Pfs25, isozymes A and B, the co-expression results in enhanced levels of the Pfs25 isozymes A and B as well as enhanced PfPDI expression, overview
AY919669
gene PDI2, DNA and amino acid sequence determination and analysis, cloning into the Escherichia coli-yeast shuttle vector pRS316 to generate the recombinant plasmid pYPDI2 in Escherichia coli strain strain MV1184, which is recombinantly introduced in Schizosaccharomyces pombe cells, that show up to 2.73fold increased PDI enzyme activity, with significantly higher activity in the stationary phase than in the exponential phase
gene TXNDC5, recombinant expression of Myc-tagged wild-type and mutant TXNDC5s in HEK-293T cells, pull-down assay with recombinant, co-expressed FLAG-tagged Srx
genes dsbA and dsbC, DNA sequence determination and analysis, expression of His-tagged DsbA and DsbC in Escherichia coli strain BL(DE3)
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genes PDIS-1 and PDIS-2, DNA and amino acid sequence determination and anaylsis, expression in Escherichia coli as soluble folded proteins
-
GmPDIL-3a and GmPDIL-3b isozymes, cloning of mature GmPDIL-3a (Thr24-Leu520) and GmPDIL-3b (Ser27-Leu523), excluding the putative signal peptides, expression in Escherichia coli strain BL21(DE3)
-
in addition to a dsbA-like gene, a dsnC gene, coding for a periplasmic protein with disulfide isomerase activity
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isozyme pdi-15, DNA and amino acid sequence determination and analysis, sequence comparison with other Leishmania species, overview
isozyme pdi-40, DNA and amino acid sequence determination and analysis, sequence comparison with other Leishmania species, overview
isozyme pdi-47, DNA and amino acid sequence determination and analysis, sequence comparison with other Leishmania species, overview
isozyme pdi-52, DNA and amino acid sequence determination and analysis, sequence comparison with other Leishmania species, overview
isozymes PDI-8, PDI-9, PDI-11, and PDI-14, localization on chromosome-8, chromosome-9, chromosome-11, and chromosome-14, respectively, DNA and amino acid sequence determination and analysis, sequence comparison and phylogenetic analysis, expression of the enzyme fused to the human tissue plasminogen activator signal sequence in Escherichia coli, strain DH10B
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isozymes PDIA3 and PDI-P5 precursors, DNA and amino acid sequence determination and analysis, expression of His-tagged mature isozymes in Escherichia coli strain HMS174 (DE3)
overexpression of PDI in GH3 cells, that release growth hormone via the T3-receptor, leads to reduced T3-induced GH release in the cells, mechanism, overview
-
overexpression of wild-type and mutant enzyme in Escherichia coli strain BL21(DE3)
-
overexpression of wild-type isozymes A and B and of the chimeric PDI mutant in Pichia pastoris using the PFs25 clone, co-expression of Pichia pastoris PDI in Pfs25
AY919669
PDI cloning from CHO-K1 cells, expression as N-terminally HA-tagged enzyme in GP2-293 cells, complementation by expression of full-length PDI restores Chlamydia trachomatis binding and infectivity in the enzyme-deficient CHO-6 mutant cell line, as wellas to diphtheria toxin sensitivity, PDI might complement an endoplasmic reticulum transport function, or other indirect functions, resulting in the change of phenotype for chlamydial susceptibility, overview
-
PDI, expression of substrate-trapping mutants of PDI family members ERp46, ERp18, ERp57, ERp72, and P5 in HT-1080 cells, the mutant enzymes form mixed disulfides
-
PDI, quantitative expression analysis, overexpression in CHO and in NS0/2N2 cells
-
PDIA3, DNA and amino acid sequence determination and analysis, quantitative expression analysis, genetic structure and phylogenetic analysis
protein disulfide isomerase and the beta-subunit of prolyl 4-hydroxylase, EC 1.14.11.2, are products of the same gene
-
recombinant constitutive overexpression in Mus musculus NSC-34 cells and neuroblastoma Neuro2a cells. PDI overexpression decreases mutant SOD1-induced cell death, overview
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recombinant expression of wild-type and mutant enzymes in Escherichia coli. Recombinant PDIp protects the Escherichia coli cells against heat shock and oxidative stress-induced cell death independently of its enzymatic activity
the gene encoding ERp27 is located at 14,958,24114,982,750 bp on chromosome 12 and has 7 exons, DNA and amino acid sequence determination and anaylsis, sequence comparison, expression of GFP-fusion ERp27 in COS-7 cell endoplasmic reticulum, expression of N-terminally His-tagged wild-type and mutant ERp57, and of PDI a, b, and b' domains, in Escherichia coli strain BL21(DE3)
wild-type and/or mutant PDI overexpression in vascular smooth muscle cells and in HEK-293T cells
-
DNA and amino acid sequence determination and analysis, sequence comparison and phylogenetic analysis, expression of the enzyme fused to the human tissue plasminogen activator signal sequence in Escherichia coli strain DH10B
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DNA and amino acid sequence determination and analysis, sequence comparison and phylogenetic analysis, expression of the enzyme fused to the human tissue plasminogen activator signal sequence in Escherichia coli strain DH10B
DNA and amino acid sequence determination and analysis, sequence comparison and phylogenetic analysis, expression of the enzyme fused to the human tissue plasminogen activator signal sequence in Escherichia coli strain DH10B
DNA and amino acid sequence determination and analysis, sequence comparison and phylogenetic analysis, expression of the enzyme fused to the human tissue plasminogen activator signal sequence in Escherichia coli strain DH10B
expressed in Escherichia coli BL21(DE3) cells
expression in Escherichia coli
-
expression of His-tagged enzyme in Escherichia coli strain AD494(DE3)
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression of GmPDIL-3a and GmPDIL-3b in the cotyledon increases during seed maturation when synthesis of storage proteins is initiated
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ncgl2478 expression is induced in the stress-responsive extra-cytoplasmic function-sigma (ECF-sigma) factor SigH-dependent manner by stress. SigH positively regulates NCgl2478 expression in Corynebacterium glutamicum. SigH directly activates the expression of ncgl2478 by specifically recognizing an operator within the ncgl2478 promoter region
oxidative stress, hypoxia, and toxic perfluorooctane sulfonate exposure induce PDIA3, PDIA3 is significantly increased in the liver of Atlantic salmon exposed to hyperoxic water during smoltification
PDI is induced by unfolded protein response, UPR, signaling transduction pathways activated by protein misfolding in the endoplasmic reticulum, overview. PDI is upregulated before symptom onset in spinal cords of ALS postmortem tissue
PDI is induced by unfolded protein response, UPR, signaling transduction pathways activated by protein misfolding in the endoplasmic reticulum, overview. PDI is upregulated before symptom onset in spinal cords of mutant SOD1G93A mice
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protein disulfide isomerase is highly upregulated in hypoxic myocardial capillary endothelial cells
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protein disulfide isomerase is up-regulated during the unfolded protein response in acute myeloid leukemia. PDI is up-regulated in U-937 cells after induction of endoplasmic reticulum stress
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the enzyme is highly expressed in various cancers including brain, lymphoma, kidney, ovarian, prostate, lung and male germ cell tumors
the enzyme is induced during endoplasmic reticulum stress. The enzyme levels are markedly increased in Alzheimer's disease, Parkinson's disease, amyotropic lateral sclerosis and other neurodegenerative diseases
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the protein expression in colorectal cancer tissues is significantly higher than that in adjacent normal tissues
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when Sulfolobus solfataricus cells are incubated with H2O2, paraquat and tert-butyl hydroperoxide, the Sso0192 mRNA level increases. Specifically, a two-fold increase in transcriptional levels is observed within 30 min of the addition of tert-butyl hydroperoxide, while a slight induction is observed 30 min after paraquat and H2O2 treatment
ncgl2478 expression is induced in the stress-responsive extra-cytoplasmic function-sigma (ECF-sigma) factor SigH-dependent manner by stress. SigH positively regulates NCgl2478 expression in Corynebacterium glutamicum. SigH directly activates the expression of ncgl2478 by specifically recognizing an operator within the ncgl2478 promoter region
ncgl2478 expression is induced in the stress-responsive extra-cytoplasmic function-sigma (ECF-sigma) factor SigH-dependent manner by stress. SigH positively regulates NCgl2478 expression in Corynebacterium glutamicum. SigH directly activates the expression of ncgl2478 by specifically recognizing an operator within the ncgl2478 promoter region
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ncgl2478 expression is induced in the stress-responsive extra-cytoplasmic function-sigma (ECF-sigma) factor SigH-dependent manner by stress. SigH positively regulates NCgl2478 expression in Corynebacterium glutamicum. SigH directly activates the expression of ncgl2478 by specifically recognizing an operator within the ncgl2478 promoter region
-
-
ncgl2478 expression is induced in the stress-responsive extra-cytoplasmic function-sigma (ECF-sigma) factor SigH-dependent manner by stress. SigH positively regulates NCgl2478 expression in Corynebacterium glutamicum. SigH directly activates the expression of ncgl2478 by specifically recognizing an operator within the ncgl2478 promoter region
-
-
ncgl2478 expression is induced in the stress-responsive extra-cytoplasmic function-sigma (ECF-sigma) factor SigH-dependent manner by stress. SigH positively regulates NCgl2478 expression in Corynebacterium glutamicum. SigH directly activates the expression of ncgl2478 by specifically recognizing an operator within the ncgl2478 promoter region
-
-
ncgl2478 expression is induced in the stress-responsive extra-cytoplasmic function-sigma (ECF-sigma) factor SigH-dependent manner by stress. SigH positively regulates NCgl2478 expression in Corynebacterium glutamicum. SigH directly activates the expression of ncgl2478 by specifically recognizing an operator within the ncgl2478 promoter region
-
-
ncgl2478 expression is induced in the stress-responsive extra-cytoplasmic function-sigma (ECF-sigma) factor SigH-dependent manner by stress. SigH positively regulates NCgl2478 expression in Corynebacterium glutamicum. SigH directly activates the expression of ncgl2478 by specifically recognizing an operator within the ncgl2478 promoter region
-
-
PDI is induced by unfolded protein response, UPR, signaling transduction pathways activated by protein misfolding in the endoplasmic reticulum, overview. PDI is upregulated before symptom onset in spinal cords of ALS postmortem tissue
-
PDI is induced by unfolded protein response, UPR, signaling transduction pathways activated by protein misfolding in the endoplasmic reticulum, overview. PDI is upregulated before symptom onset in spinal cords of ALS postmortem tissue
-
when Sulfolobus solfataricus cells are incubated with H2O2, paraquat and tert-butyl hydroperoxide, the Sso0192 mRNA level increases. Specifically, a two-fold increase in transcriptional levels is observed within 30 min of the addition of tert-butyl hydroperoxide, while a slight induction is observed 30 min after paraquat and H2O2 treatment
when Sulfolobus solfataricus cells are incubated with H2O2, paraquat and tert-butyl hydroperoxide, the Sso0192 mRNA level increases. Specifically, a two-fold increase in transcriptional levels is observed within 30 min of the addition of tert-butyl hydroperoxide, while a slight induction is observed 30 min after paraquat and H2O2 treatment
-
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
biotechnology
diagnostics
drug development
PDI constitutes a potential target for the development of alternative therapy strategies based on the inhibition of folding and chaperoning of exported proteins
food industry
-
addition of the enzyme increases the free sylfhydryl content in both dough and bread thereby improving dough alveographic characters and bread texture properties
industry
-
PDI assists incorporation of cysteine-containing compounds (CCCs) into hair and wool substrates in order to generate milder methods to dye hair with longer lasting colour by creating new disulfide bonds between hair and peptide. PDI-assists promotion of the migration of CCCs (dyes), previously attached to keratin, along hair fibres, to avoid repetitive hair dyeing procedures. PDI induces controlled release of a CCC protein (e.g. reduced form of RNase A) from wool matrices
medicine
pharmacology
-
protein disulfide isomerase is a potential therapeutic target in amyotrophic lateral sclerosis and (+-)-trans-1,2-bis(mercaptoacetamido)cyclohexane and other molecular mimics of protein disulfide isomerase could be of benefit in amyotrophic lateral sclerosis and other neurodegenerative diseases related to protein misfolding
synthesis
analysis
-
study on the critical influence of reference genes used for data normalization, shown for protein disulfide isomerase
analysis
-
development of a method to determine quantitatively the redox state of active-site cysteines found in the Cys-Xaa-Xaa-Cys motif in living cells. Method is based on the alkylation of cysteines by methoxy polyethylene glycol 5000 maleimide. In vivo, protein disulfide isomerase is present in two semi-oxidized forms in which either the first active site in the a domain or the second active site in the a' domain is oxidized. In HEK-293 cells, about 50% of enzyme is fully reduced, in 18% a domain is oxidized, a' reduced, in 15%, the a domain is reduced, a' oxidized, and 16% of enzyme are fully oxidized
analysis
PDIA3 and C/EBP? may be valuable markers in fish for exposure and effect to environmental stress
biotechnology
overexpression of Plasmodium falciparum PDI isozymes A and B for production of a disulfide-rich transmission-blocking vaccine candidate Pfs25 in Pichia pastoris, the expression level is enhance by co-expression of the endogenous Pichia pastoris enzyme in Pfs25 3fold, production method evaluation
biotechnology
AY919669
overexpression of Plasmodium falciparum PDI isozymes A and B for production of a disulfide-rich transmission-blocking vaccine candidate Pfs25 in Pichia pastoris, the expression level is enhanced by co-expression of the endogenous Pichia pastoris enzyme in Pfs25 clone 3fold, production method evaluation
diagnostics
-
the absence of PDIp expression in pancreatic adenocarcinoma may serve as an additional biomarker for pancreatic cancer
diagnostics
-
the absence of PDIp expression in pancreatic adenocarcinoma may serve as an additional biomarker for pancreatic cancer
diagnostics
lung cancer patients with high Srx levels have significantly shorter survival and those with high TXNDC5 levels have longer survival. Cellular levels of Srx and TXNDC5 may be useful as biomarkers to predict the survival of individuals with lung cancer
medicine
-
protein disulfide gene expression is significantly decreased by 28% and 69% at 20 h after cecal ligation and puncture or lipopolysaccharide infusion, respectively
medicine
-
lipopolysaccharide decreases protein disulfide isomerase protein expression by 33% in RAW 264.7 cells. Incubation of the cells with bacitracin significantly decreases tumor necrosis factor alpha gene expression and release. Downregulation of protein disulfide isomerase gene expression by siRNA correlates with a 3.2fold increase in tumor necrosis factor alpha release into the cell supernatant
medicine
-
PDI is required in vivo for both fibrin generation and platelet thrombus formation
medicine
-
overexpression has significant effects on cell-cell fusion mediated by Newcastle disease virus. Overexpression results in increased membrane fusion, and enhanced production of free thiols in Newcastle disease virus fusion protein when expressed without hemagglutinin-neuraminidase protein but drecreased free thiols in Newcastle disease virus fusion protein expressed with hemagglutinin-neuraminidase protein. Overexpression favors a postfusion conformation of surface-expressed Newcastle disease virus fusion protein in the presence of hemagglutinin-neuraminidase protein
medicine
-
protein disulfide isomerase directly promotes initiator protein tissue factor-dependent fibrin production during thrombus formation in vivo. After endothelial denudation of carotid artery, enzyme is released at the injury site from adherent platelets and disrupted vessel walls. Inhibition of the enzyme decreases initiator protein tissue factor-triggered fibrin formation. Enzyme infusion increases fibrin generation at the injury site
medicine
-
protein disulfide isomerase PDI directly interacts with thiol-containing fibrinogen receptor alphaIIbbeta3. PDI has greater ability to isomerize disulfide bonds than the alphaIIbbeta3 integrin. Anti-PDI antibodies inhibit signalling-independent activation of the thiol-containing fibrinogen receptor alphaIIbbeta3 by Mn2+
medicine
-
inhibition of isoform procollagen-proline, 2-oxoglutarate-4-dioxygenase beta subunit activity increases apoptosis in response to agents which induce ER-stress such as fenretinide and velcade
medicine
-
presence of protein disulfide isomerase on the surface of platelet-derived microparticles. Enzyme is catalytically active and capable of both promoting platelet aggregation and disrupting insulin signaling. Platelet-derived microparticles increase the initial rates of aggregation by 4fold and the pro-aggregatory activity of micrparticles can be attenuated with an anti-PDI antibody. Anti-PDI antibodies are able to block the degradation of insulin, thereby restoring insulin signaling. Patients with type II diabetes show increased levles of enzyme-containing microparticles in their plasma
medicine
-
PDI represents a potential drug target for anti-amebic therapy
medicine
-
the enzyme is a therapeutic target for preventing and treating inappropriate neutrophil sequestration
medicine
-
the enzyme is a therapeutic target for preventing and treating inappropriate neutrophil sequestration
medicine
-
protein disulfide isomerase upregulation is e.g. associated with cancer, attention-deficite hyperactivity disorder, Alzheimer disease, amyotrophic lateral sclerosis, perinatal asphyxia, brain ischemia, sporadic Creutzfeldt-Jacob disease, major depression, brain injury, tuberous sclerosis, endothelial function, acute coronary syndrome, iscemic heart disease, hepatosteatosis, varioliform gastritis, preeclampsia, obesity, insulin resistance, diabetes, congenital hypothyroid goiter, Helicobacter pylori infection, peridontitis, dehydration, aging, or pregnancy
medicine
the enzyme may be used as a biomarker for cancer diagnosis and a potential drug target for cancer therapy and for treating thrombosis and vascular inflammation
synthesis
-
development of a versatile baculovirus expression and secretion system, using the enzyme as a fusion partner. Fusion improves the secretions and antibacterial activities of recombinant nuecin proteins and may be used for large-scale production of bioactive proteines
EXTERNAL LINKS (specific for EC-Number 5.3.4.1)
Transporter Classification Database (TCDB): 8.A.88.2.3, 8.A.88.2.7
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Release 2026.1 (March 2026)
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