Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Agp mutant
?
-
folding of Agp mutant, DsbC, mutant of Agp, an AppA homologue, containing the AppA nonconsecutive disulfide bond
-
-
?
alkaline protease inhibitor
?
alpha-globulin
?
PDIL1-1 facilitates the oxidative folding of alpha-globulin
-
-
?
alpha-synuclein
?
-
-
-
?
apolipoprotein B
?
-
-
-
-
?
apolipoprotein B100
?
-
the enzyme assists in the oxidative folding of apolipoprotein B100
-
-
?
bovine pancreatic trypsin inhibitor
?
-
-
-
-
?
carboxypeptidase Y
?
-
maturation of carboxypeptidase Y
-
-
?
cholera toxin
?
-
reduced (but not oxidized) protein-disulfide isomerase displaces the cholera toxin A1 subunit from the holotoxin without unfolding the A1 subunit
-
-
?
citrate synthase
stabilized citrate synthase
-
DsbG suppresses aggregation of luciferase at 43°C, enzyme has both PDI and chaperone activity
-
?
conotoxins sTx3.1
?
disulfide formation, macromolecular crowding has little effect on the protein disulfide isomerase-catalyzed oxidative folding and disulfide isomerization of conotoxin
-
-
?
conotoxins tx3a
?
disulfide formation, macromolecular crowding has little effect on the protein disulfide isomerase-catalyzed oxidative folding and disulfide isomerization of conotoxin
-
-
?
creatine kinase
?
-
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
-
-
?
D-glyceraldehyde 3-phosphate dehydrogenase
?
-
-
-
-
?
degenerated RNase type III
?
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
-
-
?
denatured D-glceraldehyde-3-phosphate dehydrogenase
refolded D-glceraldehyde-3-phosphate dehydrogenase
-
interaction of PDI with cyclophilin B increases its chaperone activity
-
?
denatured D-glyceraldehyde-3-phosphate dehydrogenase
refolded D-glyceraldehyde-3-phosphate dehydrogenase
-
chaperone activity of PDI
-
?
denatured eclosion hormone
active eclosion hormon
-
PDI acts as a chaperone and refolds the insect neuropeptide eclosion hormone
-
?
denatured lysozyme
?
-
PDI catalyzes the formation, rearrangement, and breakage of disulfide bonds, oxidative refolding by PDI almost completely restores lysozyme activity, overview
-
-
?
denatured lysozyme
native lysozyme
denatured rhodanese
?
-
PDI exhibits chaperone activity with rhodanese
-
-
?
denatured rhodanese
refolded rhodanese
-
interaction of PDI with cyclophilin B increases its chaperone activity
-
?
denatured RNase A
?
recombinant CYO1 renatures RNase A
-
-
?
denatured Rnase A
active Rnase A
-
-
-
-
?
denatured RNase A + GSH
renatured RNase A + GSSG
-
-
-
-
?
denatured-reduced lysozyme
?
-
oxidase activity of PDI
-
-
?
dieosin glutathione disulfide
eosin glutathione sulfide
-
-
-
?
E2A homodimer
E2A-basic helix-loop-helix protein heterodimer
-
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
-
?
envelope glycoprotein 120
envelope glycoprotein 120
-
i.e. human immunodeficiency virus gp120
-
?
estrogen receptor alpha
?
folded cholera toxin
unfolded cholera toxin
-
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
-
?
glutathione disulfide
glutathione
-
-
-
?
glycoprotein 120
glycoprotein 120
-
PDI may play a role in HIV-1 infection by reducing HIV-1 envelope glycoprotein 120
-
?
GSSG
GSH
-
disulfide reduction of GSSG, the disulfide reduction activity of both PDI-thioredoxin reductase and PDI-DTT is reduced
-
-
?
insulin + DTT
?
bovine substrate, reductase activity with DTT
-
-
?
Insulin-(SS) + dithiothreitol
Insulin-(SH)2 + oxidized dithiothreitol
-
-
-
?
Insulin-(SS) + GSH
Insulin-(SH)2 + GSSG
integrin alphaIIb
?
-
-
-
-
?
integrin alphaIIbbeta3
?
-
-
-
-
?
integrin alphaMb2
?
-
-
-
-
?
integrin alphaVb3
?
-
-
-
-
?
integrin alphaVbeta3
?
-
-
-
-
?
integrin beta3
?
-
-
-
-
?
integrin subunit alpha11
?
-
the enzyme activates integrin subunit alpha11
-
-
?
integrin subunit beta1
?
-
the enzyme activates integrin subunit beta1
-
-
?
kalata B1
?
-
and derivatives, PDI dramatically enhanced the correct oxidative folding of linear and cyclic kalata B1 at physiological pH, determination of folding intermediates
-
-
?
lactate dehydrogenase
?
-
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
-
-
?
luciferase
stabilized luciferase
-
DsbG suppresses aggregation of luciferase at 43°C, enzyme has both PDI and chaperone activity
-
?
lysozyme
?
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
-
-
?
lysozyme
aggregated lysozyme
-
PDI has antichaperone activity facilitating protein aggregation
-
?
NADP malate dehydrogenase
?
-
substrate for isoform PDI-M only
-
-
?
NADPH oxidase A
?
-
-
-
-
?
NADPH thioredoxin reductase
?
-
-
-
-
?
neuronal nitric oxide synthase
?
-
the enzyme catalyzes neuronal nitric oxide synthase dimerization
-
-
?
oxidized insulin
reduced insulin
-
-
-
-
?
oxidized insulin + dithiothreitol
reduced insulin
gPDI-2, low activity with gPDI-3, no activity with gPDI-1
-
?
oxidoreductase Ero1
?
-
disulfide bond formation in the oxidoreductase Ero1, endoplasmic reticular protein interacts with PDILT
-
-
?
peroxiredoxin
?
-
-
-
-
?
phytase
?
-
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
-
-
?
Pipe
?
-
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
-
-
?
procollagen I
?
-
-
-
-
?
procollagen III
?
-
-
-
-
?
protein-(SSG)2n
protein(SS)n + n(GSSG)
-
-
-
-
?
reduced bovine pancreatic trypsin inhibitor
oxidized bovine pancreatic trypsin inhibitor
gPDI-2, no cativity with gPDI-1 and gPDI-3
-
?
reduced denatured RNase A + GSH
reduced renatured RNase A + GSSG
-
-
-
-
?
reduced Ero1alpha
oxidized Ero1alpha
-
-
-
-
?
reduced glutathione peroxidase 7
oxidized glutathione peroxidase 7
-
-
-
-
?
reduced glutathione peroxidase 8
oxidized glutathione peroxidase 8
-
-
-
-
?
reduced ribonuclease
?
-
refolding of reduced ribonuclease in presence of glutathione, isomerase activity of PDI
-
-
?
reduced ribonuclease A
denatured ribonuclease A
-
-
-
?
reduced RNase
denatured RNase
-
-
-
?
reduced RNase A
RNase A
-
-
-
?
refolding of RNase
?
-
renaturation of reduced RNase
-
-
?
riboflavin binding protein
?
-
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
-
-
?
ribonuclease + dithiothreitol
?
-
-
-
-
?
ribonuclease A
?
-
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
-
-
?
ribonuclease T1
?
-
-
-
-
?
ricin
?
-
reductive activation of ricin and ricin A-chain immunotoxins, assay system involving thioredoxin reductase and NADPH, overview
-
-
?
ricin A-chain immunotoxins
?
-
reductive activation of ricin and ricin A-chain immunotoxins, assay system involving thioredoxin reductase and NADPH, overview
-
-
?
RNase B
?
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
-
-
?
scrambled reoxidized lysozyme
?
-
isomerase activity of PDI
-
-
?
scrambled RNAse
?
-
-
-
?
scrambled RNAse + 2-mercaptoethanol
?
scrambled RNAse + cysteine
?
scrambled RNAse + dithiothreitol
?
-
-
-
-
?
scrambled RNase A
RNase A
-
-
-
?
tachyplesin I
?
-
-
-
-
?
TAMRAX3CX4CX2-CONH2
?
-
-
-
-
?
thrombospondin-1 + alpha-thrombin + antithrombin III
thrombospondin-1-S-S-alpha-thrombin-S-S-antithrombin III
-
PDI catalyzes formation of disulfide linked complexes of thrombospondin
-
?
transforming growth factor-beta1
?
-
-
-
-
?
tyramine-S-S-poly(D-lysine)
tyramine-SH + HS-poly(D-lysine)
-
-
-
?
unfolded acidic phospholipase A2
refolded acidic phospholipase A2
-
PDI at a molar ratio to acidic phospholipase A2 of 0.1 increases the reactivation of reduced and denatured acidic phospholipase A2 from 4% to 15%
-
?
unfolded bovine pancreatic ribonuclease A + oxidized glutathione
refolded bovine pancreatic ribonuclease A + reduced glutathione
-
oxidative folding of RNase A, 12fold rate acceleration in the presence of PDI
-
?
unfolded bovine pancreatic trypsin inhibitor
folded bovine pancreatic trypsin inhibitor
-
-
?
unfolded bovine pancreatic trypsin inhibitor
refolded bovine pancreatic trypsin inhibitor
unfolded bovine pancreatic trypsin inhibitor
refolded bovine pancreatic trypsin inhibitor + oxidized glutathione
-
oxidative refolding of denatured bovine pancreatic trypsin inhibitor
-
?
unfolded disulfide-bonded protein
refolded disulfide-bonded protein
-
-
-
?
unfolded insulin
folded insulin
-
-
?
unfolded insulin
refolded insulin
-
-
-
?
unfolded insulin + reduced glutathione
refolded insulin + oxidized glutathione
-
-
-
?
unfolded insulin beta-chain
refolded insulin beta-chain
-
-
-
?
unfolded lysozyme
refolded lysozyme
-
oxidative refolding of reduced and denatured lysozyme in glutathione redox buffer
-
?
unfolded mitochondrial malate dehydrogenase
refolded mitochondrial malate dehydrogenase
-
maximum refolding when the PDI concentration is 20fold higher than the malate dehydrogenase concentration
-
?
unfolded pro-carboxypeptidase Y
refolded pro-carboxypeptidase Y
-
-
-
?
unfolded proinsulin
refolded proinsulin
-
PDI acts both as a chaperone and as an isomerase during folding and disulfid bond formation of proinsulin, chaperone and isomerization activity is required at the beginning of proinsulin folding, the late refolding process only depends on the isomerase activity
-
?
unfolded RNase
refolded RNase
unfolded RNase A
refolded RNase
-
-
-
?
unfolded RNase A
refolded RNase A
unfolded RNase A + reduced glutathione
refolded RNase A + oxidized glutathione
-
-
-
?
unfolded rRNaSe
refolded rRNase
-
refolding of reduced rRNaSe
-
?
unofolded bovine pancreatic ribonuclease A + oxidized dithiothreitol
refolded bovine pancreatic ribonuclease A + reduced dithiothreitol
-
oxidative folding of RNase A
-
?
vitronectin + thrombin + antithrombin
vitronectin-thrombin-antithrombin
-
PDI catalyzes the formation of disulfide-linked complexes of vitronectin with thrombin-antithrombin
-
?
additional information
?
-
alkaline protease inhibitor
?
-
folding and rearrangement of alkaline protease inhibitor
-
-
?
alkaline protease inhibitor
?
-
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
-
-
?
alkaline protease inhibitor
?
-
folding and rearrangement of alkaline protease inhibitor
-
-
?
alkaline protease inhibitor
?
-
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
-
-
?
conotoxin lt14a
?
-
-
-
?
conotoxin lt14a
?
-
-
-
?
conotoxin lt14a
?
-
-
-
?
conotoxin lt14a
?
-
-
-
?
conotoxin lt14a
?
-
-
-
?
conotoxin lt14a
?
-
-
-
-
?
conotoxin lt14a
?
-
-
-
?
conotoxin lt14a
?
-
-
-
?
conotoxin lt14a
?
-
-
-
?
conotoxin lt14a
?
-
-
-
?
conotoxin lt14a
?
-
-
-
?
conotoxin lt14a
?
-
-
-
?
denatured lysozyme
native lysozyme
-
-
-
?
denatured lysozyme
native lysozyme
-
-
-
?
denatured lysozyme
native lysozyme
-
-
-
?
denatured lysozyme
native lysozyme
-
-
-
?
denatured lysozyme
native lysozyme
-
-
-
?
denatured lysozyme
native lysozyme
-
-
-
-
?
denatured lysozyme
native lysozyme
-
-
-
?
denatured lysozyme
native lysozyme
-
-
-
?
denatured lysozyme
native lysozyme
-
-
-
?
denatured lysozyme
native lysozyme
-
-
-
?
denatured lysozyme
native lysozyme
-
-
-
?
denatured lysozyme
native lysozyme
-
-
-
?
estrogen receptor alpha
?
-
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
-
-
?
estrogen receptor alpha
?
-
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
-
-
?
HED-SSM
MSH + HED
a mixed disulfide
-
-
?
HED-SSM
MSH + HED
a mixed disulfide
-
-
?
HED-SSM
MSH + HED
a mixed disulfide
-
-
?
HED-SSM
MSH + HED
a mixed disulfide
-
-
?
HED-SSM
MSH + HED
a mixed disulfide
-
-
?
HED-SSM
MSH + HED
a mixed disulfide
-
-
?
HED-SSM
MSH + HED
a mixed disulfide
-
-
?
insulin
?
recombinant CYO1 accelerates disulfide bond reduction in the model substrate insulin
-
-
?
insulin
?
-
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
-
-
?
insulin
?
-
reduction of sidulfide bonds
-
-
?
insulin
?
-
reductase activity of PDI
-
-
?
insulin
?
-
PDI exhibits reductase activity with insulin
-
-
?
insulin
?
-
reduction of disulfide bonds
-
-
?
insulin
?
-
bovine substrate, reduction of disulfide bonds
-
-
?
insulin
?
-
disulfide-bond reduction in substrate insulin, reduction activity by Holmgren's turbimetric method
-
-
?
insulin
?
reduction of insulin disulfide bonds
-
-
?
insulin
?
reduction of insulin disulfide bonds
-
-
?
insulin
reduced insulin
-
-
-
?
insulin
reduced insulin
-
-
-
-
?
Insulin-(SS) + GSH
Insulin-(SH)2 + GSSG
-
-
-
-
?
Insulin-(SS) + GSH
Insulin-(SH)2 + GSSG
-
-
-
-
?
Insulin-(SS) + GSH
Insulin-(SH)2 + GSSG
-
-
-
?
Insulin-(SS) + GSH
Insulin-(SH)2 + GSSG
-
-
-
?
Insulin-(SS) + GSH
Insulin-(SH)2 + GSSG
-
-
-
?
Insulin-(SS) + GSH
Insulin-(SH)2 + GSSG
-
-
-
?
Insulin-(SS) + GSH
Insulin-(SH)2 + GSSG
-
-
-
-
?
Insulin-(SS) + GSH
Insulin-(SH)2 + GSSG
-
-
-
?
Insulin-(SS) + GSH
Insulin-(SH)2 + GSSG
-
protein disulfide isomerase supports proinsulin folding as chaperone and isomerase
-
-
?
Insulin-(SS) + GSH
Insulin-(SH)2 + GSSG
-
-
-
?
Insulin-(SS) + GSH
Insulin-(SH)2 + GSSG
-
-
-
-
?
Insulin-(SS) + GSH
Insulin-(SH)2 + GSSG
-
-
-
-
?
Insulin-(SS) + GSH
Insulin-(SH)2 + GSSG
-
-
-
-
?
Insulin-(SS) + GSH
Insulin-(SH)2 + GSSG
-
-
-
-
?
Insulin-(SS) + GSH
Insulin-(SH)2 + GSSG
-
-
-
-
?
Insulin-(SS) + GSH
Insulin-(SH)2 + GSSG
-
-
-
?
NRCSQGSCWN
?
-
-
-
-
?
NRCSQGSCWN
?
-
disulfide-bond formation within the thiol substrate peptide NRCSQGSCWN, oxidation activity requires GSH/GSSG
-
-
?
NRCSQGSCWN
NRCSQGSCWN
-
-
-
?
NRCSQGSCWN
NRCSQGSCWN
-
-
-
?
Proteins
?
-
-
-
-
?
Proteins
?
-
native, reduced or with wrong disulfide bonds
-
-
?
Proteins
?
-
facilitates the formation of the correct disulfide bonds within newly synthesized polypeptides
-
-
?
Proteins
?
-
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
-
-
?
Proteins
?
-
involved in cotranslational disulfide bond formation
-
-
?
Proteins
?
-
implicated in the biosynthesis of secretory proteins
-
-
?
Proteins
?
-
enzyme may play a physiological role in the catalysis of S-S-bond formation in prolactin
-
-
?
Proteins
?
-
native, reduced or with wrong disulfide bonds
-
-
?
Proteins
?
-
may play a role in the formation of disulfide bonds in extracellular and periplasmic proteins
-
-
?
Proteins
?
-
native, reduced or with wrong disulfide bonds
-
-
?
Proteins
?
-
facilitates the formation of disulfides during the folding and processing of membrane and secretory proteins
-
-
?
Proteins
?
-
enzyme may be involved in the formation of intra-chain and inter-chain disulfide bonds in procollagen
-
-
?
Proteins
?
-
may play a role in retaining prolyl 4-hydroxylase in its native conformation
-
-
?
Proteins
?
-
native, reduced or with wrong disulfide bonds
-
-
?
Proteins
?
-
enzyme may be involved in the formation of intra-chain and inter-chain disulfide bonds in procollagen
-
-
?
Proteins
?
-
platelet enzyme may play a role in the various haemostatic and tissue remodelling processes in which platelets are involved
-
-
?
Proteins
?
-
implicated in the biosynthesis of secretory proteins
-
-
?
Proteins
?
-
native, reduced or with wrong disulfide bonds
-
-
?
Proteins
?
-
may play a role in the formation of disulfide bonds in extracellular and periplasmic proteins
-
-
?
Proteins
?
-
catalysis of native disulfide bond formation
-
-
?
Proteins
?
-
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
-
-
?
Proteins
?
-
native, reduced or with wrong disulfide bonds
-
-
?
Proteins
?
-
may play a role in the formation of disulfide bonds in extracellular and periplasmic proteins
-
-
?
Proteins
?
-
enzyme may be involved in the formation of intra-chain and inter-chain disulfide bonds in procollagen
-
-
?
Proteins
?
-
native, reduced or with wrong disulfide bonds
-
-
?
Proteins
?
-
may play a role in the formation of disulfide bonds in extracellular and periplasmic proteins
-
-
?
Proteins
?
-
native, reduced or with wrong disulfide bonds
-
-
?
Proteins
?
-
may play a role in the formation of disulfide bonds in extracellular and periplasmic proteins
-
-
?
Proteins
?
-
native, reduced or with wrong disulfide bonds
-
-
?
Proteins
?
-
may play a role in the formation of disulfide bonds in extracellular and periplasmic proteins
-
-
?
Proteins
?
-
native, reduced or with wrong disulfide bonds
-
-
?
Proteins
?
-
may play a role in the formation of disulfide bonds in extracellular and periplasmic proteins
-
-
?
Proteins
?
-
native, reduced or with wrong disulfide bonds
-
-
?
Proteins
?
-
proposed physiological role as catalyst of formation of native disulfide bonds in nascent and newly synthesized secretory proteins
-
-
?
Proteins
?
-
involved in cotranslational disulfide bond formation
-
-
?
Proteins
?
-
implicated in the biosynthesis of secretory proteins
-
-
?
Proteins
?
-
native, reduced or with wrong disulfide bonds
-
-
?
Proteins
?
-
involved in the assembly of wheat storage proteins within the endoplasmic reticulum
-
-
?
Proteins
?
-
plays a role in the formation of disulfide bonds during biosynthesis of wheat storage proteins
-
-
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
-
-
-
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
-
-
-
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
cosubstrate: DTT, 2-mercaptoethanol, GSH, or Cys
with correct disulfide bonds
?
Proteins
Proteins
-
cosubstrate dithiothreitol can be replaced by GSH, cysteamine, 2-mercaptoethanol, thioglycollic acid or L-Cys, but at significantly higher concentrations
with correct disulfide bonds
?
Proteins
Proteins
-
incorrectly disulfide-linked ribonuclease
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
-
-
-
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
refolding and activation of human carbonic anhydrase IV, GSSG promotes the activation
with correct disulfide bonds
?
Proteins
Proteins
-
-
-
-
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
-
-
-
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
incorrectly disulfide-linked bovine pancreatic ribonuclease
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
incorrectly disulfide-linked Bowman Birk soybean trypsin
with correct disulfide bonds
?
Proteins
Proteins
-
incorrectly disulfide-linked lysozyme
with correct disulfide bonds
?
Proteins
Proteins
-
incorrectly disulfide-linked RNAse
with correct disulfide bonds
?
Proteins
Proteins
-
-
-
-
?
Proteins
Proteins
-
refolding of scrambled ribonuclease
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
refolding of scrambled ribonuclease
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
refolding of scrambled lysosyme
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
-
-
-
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
-
-
-
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
eduction of insulin and oxidative folding of ribonuclease A
with correct disulfide bonds
?
Proteins
Proteins
-
incorrectly disulfide-linked RNAse
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
-
-
-
?
Proteins
Proteins
-
refolding of scrambled ribonuclease
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
cosubstrate: DTT, 2-mercaptoethanol, GSH, or Cys
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
?
Proteins
Proteins
-
-
-
-
?
rhodanese
?
-
chaperone activity
-
-
?
rhodanese
?
-
the protein substrate is devoid of disulfide bonds, chaperone activity
-
-
?
rhodanese
?
-
prevention of rhodanese degeneration, chaperone activity
-
-
?
rhodanese
?
-
prevention of rhodanese degeneration, chaperone activity
-
-
?
ribonuclease
?
-
refolding of ribonuclease, isomerase activity, renaturation of reduced ribonuclease, in presence of GSH and GSSG
-
-
?
RNase
?
-
refolding of RNase, renaturation of reduced bovine pancreatic RNase
-
-
?
RNase
?
-
the enzyme is able to renature the denatured and reduced RNase
-
-
?
RNase
?
-
refolding of RNase, renaturation of reduced and of scrambled RNase with almost equal activity
-
-
?
RNase A
?
-
-
-
-
?
RNase A
?
-
oxidase activity of PDI
-
-
?
RNase A
?
-
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
-
-
?
RNase A
?
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
-
-
?
RNase A
?
-
PDI exhibits isomerase activity with RNase A
-
-
?
RNase A
?
-
reduced and denatured substrate, oxidase/isomerase activity on the refolding of the substrate
-
-
?
RNase A
?
-
reduced and denatured substrate from bovine pancreas
-
-
?
RNase A + DTT
?
the enzyme contains a WCGHCK active site
-
-
?
RNase A + DTT
?
the enzyme contains a WCGHCQ active site
-
-
?
scrambled ribonuclease
?
-
-
-
-
?
scrambled ribonuclease
?
-
-
-
-
?
scrambled RNAse + 2-mercaptoethanol
?
-
-
-
-
?
scrambled RNAse + 2-mercaptoethanol
?
-
-
-
-
?
scrambled RNAse + cysteine
?
-
-
-
-
?
scrambled RNAse + cysteine
?
-
-
-
-
?
scrambled RNAse A
?
the enzyme catalyzes intramolecular disulfide interchange in scrambled RNase A and restores both native disulfide pairing and ribonuclease activity
-
-
?
scrambled RNAse A
?
the enzyme catalyzes intramolecular disulfide interchange in scrambled RNase A and restores both native disulfide pairing and ribonuclease activity
-
-
?
tissue factor
?
-
-
-
-
?
tissue factor
?
-
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
-
-
?
tissue factor
?
-
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
-
-
?
unfolded bovine pancreatic trypsin inhibitor
refolded bovine pancreatic trypsin inhibitor
-
-
-
?
unfolded bovine pancreatic trypsin inhibitor
refolded bovine pancreatic trypsin inhibitor
-
-
-
?
unfolded bovine pancreatic trypsin inhibitor
refolded bovine pancreatic trypsin inhibitor
-
-
-
?
unfolded RNase
refolded RNase
-
-
-
?
unfolded RNase
refolded RNase
-
-
?
unfolded RNase
refolded RNase
-
-
-
?
unfolded RNase
refolded RNase
-
-
-
?
unfolded RNase
refolded RNase
-
-
-
?
unfolded RNase
refolded RNase
-
-
-
?
unfolded RNase
refolded RNase
-
oxidative folding of RNase
-
?
unfolded RNase
refolded RNase
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
-
?
unfolded RNase A
refolded RNase A
-
-
-
?
unfolded RNase A
refolded RNase A
-
-
-
?
unfolded RNase A
refolded RNase A
-
-
-
?
unfolded RNase A
refolded RNase A
-
-
-
?
unfolded RNase A
refolded RNase A
-
all five consecutive PDI domains, a-b-b'-a'-c are necessary for PDI's disulfide isomerase and chaperone activity
-
?
unfolded RNase A
refolded RNase A
-
PDI binds to DNA and may be involved in DNA-nuclear matrix anchoring
-
?
unfolded RNase A
refolded RNase A
-
PDI catalyzes disulfide isomerization of misfolded, i.e. scrambled RNaseA into native RNase A
-
?
unfolded RNase A
refolded RNase A
-
PDI catalyzes disulfide isomerization of misfolded, i.e. scrambled RNaseA into native RNase A
-
?
unfolded RNase A
refolded RNase A
-
PDI functions in a plasma environment
-
?
unfolded RNase A
refolded RNase A
-
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
-
?
unfolded RNase A
refolded RNase A
-
tyrosine and tryptophane residues in peptides are the recognition motifs for their binding
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
the enzyme shows dithiol-disulfide-oxidoreductase activity, and contains a conserved WCGHC active site and two thioredoxin domains
-
-
?
additional information
?
-
-
the enzyme shows dithiol-disulfide-oxidoreductase activity, and contains a conserved WCGHC active site and two thioredoxin domains
-
-
?
additional information
?
-
-
structure and mechanism of PDI in disulfide formation and oxidative protein folding, overview
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
the enzyme has oxidative folding activity
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
3,3',5-triiodo-L-thyronine-binding activity
-
-
?
additional information
?
-
-
the enzyme may be significant in the action of triiodothyronine towards the target cells
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
PDI is a better thiol oxidant than a disulfide protein reductant
-
-
?
additional information
?
-
-
substrate specificity of PDI
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
PDI catalyzes the isomerization of disulfide bonds on misfolded proteins
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
structure and mechanism of PDI in disulfide formation and oxidative protein folding, overview
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
in vivo, disulfide bond formation is mainly catalyzed by protein disulfide isomerase
-
-
?
additional information
?
-
-
in vivo, disulfide bond formation is mainly catalyzed by protein disulfide isomerase
-
-
?
additional information
?
-
the enzyme shows oxidase and isomerase activities, overview
-
-
?
additional information
?
-
-
the enzyme shows oxidase and isomerase activities, overview
-
-
?
additional information
?
-
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
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
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
-
-
-
additional information
?
-
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
-
-
-
additional information
?
-
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
-
-
-
additional information
?
-
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
-
-
-
additional information
?
-
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
-
-
-
additional information
?
-
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
-
-
-
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
PDI behaves mainly as an oxidase/isomerase and exhibits chaperone-like activity
-
-
?
additional information
?
-
-
DsbC resolves incorrect disulfides whose formation has been catalyzed by redox-active copper
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
the enzyme plays a crucial role in folding periplasmatically excreted proteins
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
DsbC and DbsG also possess thioredoxin-like domains, substrate specificity of PDI
-
-
?
additional information
?
-
-
substrate disulfide bonds, overview, the AppA homologue Agp, a periplasmic phosphatase, lacks nonconsecutive disulfide bonds and is no substrate for DsbC
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
PDI has the ability to catalyze dithiol-disulfide exchange reactions, chaperone activity and propensity to form subunits of multi-enzyme complexes, overview
-
-
?
additional information
?
-
-
the enzyme shows disulfide reduction and chaperone activities, it facilitates the folding of secreted proteins with multiple disulfide bonds by catalyzing disulfide-bond rearrangement
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
the enzyme acts as a thyroid-hormone binding protein
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
enzyme is involved in the proper folding or quality control of storage proteins
-
-
?
additional information
?
-
-
GmPDIL-1 and GmPDIL-2 function as molecular chaperones, and prevent the aggregation of unfolded rhodanese, while GmPDIL-3a and GmPDIL-3b do not
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
HlPDI-1 might be involved in tick blood feeding and Babesia parasite infection in ticks
-
-
?
additional information
?
-
HlPDI-1 might be involved in tick blood feeding and Babesia parasite infection in ticks
-
-
?
additional information
?
-
HlPDI-1 might be involved in tick blood feeding and Babesia parasite infection in ticks
-
-
?
additional information
?
-
-
HlPDI-1 might be involved in tick blood feeding and Babesia parasite infection in ticks
-
-
?
additional information
?
-
HlPDI-3 might be involved in tick blood feeding and Babesia parasite infection in ticks
-
-
?
additional information
?
-
HlPDI-3 might be involved in tick blood feeding and Babesia parasite infection in ticks
-
-
?
additional information
?
-
HlPDI-3 might be involved in tick blood feeding and Babesia parasite infection in ticks
-
-
?
additional information
?
-
-
HlPDI-3 might be involved in tick blood feeding and Babesia parasite infection in ticks
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
isomerase activity is assayed using the insulin/glutathione coupled assay
-
-
?
additional information
?
-
-
substrate specificity of PDI
-
-
?
additional information
?
-
the four domains a, b, b', and a' show cooperative properties in both isomerase and chaperone functions of PDi
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
structure and mechanism of PDI in disulfide formation and oxidative protein folding, overview
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
ERp57 interacts with the lectin chaperone calnexin, binding structure, and active site structure, overview
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
the enzyme shows disulfide exchange activity
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
protein disulfide isomerase contributes to the activation of cryptic initiator protein tissue factoron microvesicles in vitro
-
-
?
additional information
?
-
-
protein disulfide isomerase PDI directly interacts with thiol-containing fibrinogen receptor alphaIIbbeta3. PDI has greater ability to isomerize disulfide bonds than the alphaIIbbeta3 integrin
-
-
?
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
-
-
?
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
-
-
?
additional information
?
-
-
recombinant human PDI does not influence factor X activation by factor VIIa soluble tissue factor
-
-
?
additional information
?
-
-
reduced protein disulfide isomerase activates initiator protein tissue factor by isomerzation of a mixed disulfide and a free thiol to an intramolecular disulfide
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
PDI catalyzes disulfide bond formation in the endoplasmic reticulum
-
-
?
additional information
?
-
-
PDI catalyzes disulfide bond formation in the endoplasmic reticulum
-
-
?
additional information
?
-
-
PDI specifically associates with signal peptide peptidase, SPP, independently of human cytomegalovirus glycoprotein US2, but not with Derlin-1
-
-
?
additional information
?
-
-
PDI specifically binds 3,3',5-triiodo-L-thyronine
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
PDI directly interacts with calreticulin
-
-
?
additional information
?
-
-
the enzyme has a single E2-binding site
-
-
?
additional information
?
-
-
the enzyme has three catalytic activities including thiol-disulfide oxireductase, disulfide isomerase, and redox-dependent chaperone
-
-
?
additional information
?
-
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
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
the enzyme has a single E2-binding site
-
-
?
additional information
?
-
-
PDI also functions as a dehydroascorbate reductase and a molecular chaperone besides its disulfide-isomerizing function
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
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, 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
-
-
?
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, 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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
PDILT forms intermolecular disulfide bonds in testis
-
-
?
additional information
?
-
-
PDILT forms intermolecular disulfide bonds, but shows no intramolecular disulfide bonds
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
the enzyme mediates conformational changes by thiol-disulfide exchange
-
-
?
additional information
?
-
-
PDI is required in vivo for both fibrin generation and platelet thrombus formation
-
-
?
additional information
?
-
-
protein disulfide isomerase directly promotes initiator protein tissue factor-dependent fibrin production during thrombus formation in vivo
-
-
?
additional information
?
-
-
enzyme converts initiator protein tissue factor cysteine residues from glutathionylated to disulfide state
-
-
?
additional information
?
-
-
AGR2 is essential for production of intestinal mucin MUC2, but is not required for establishment of intestinal secretory epithelial cell lineages
-
-
?
additional information
?
-
-
PDI specifically binds 3,3',5-triiodo-L-thyronine
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
a cysteine residue in the thioredoxin-like domain of AGR2 forms mixed disulfide bonds with MUC2, mutational analysis of the AGR2-MUC2 interaction, overview
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
PDIL2-3 activity is dispensable in the oxidative folding of alpha-globulin
-
-
?
additional information
?
-
PDIL2-3 activity is dispensable in the oxidative folding of alpha-globulin
-
-
?
additional information
?
-
-
PDIL2-3 activity is dispensable in the oxidative folding of alpha-globulin
-
-
?
additional information
?
-
-
the enzyme assists protein folding in malaria parasites
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
the enzyme assists protein folding in malaria parasites
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
the enzyme assists protein folding in malaria parasites
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
the enzyme shows disulfide oxidase/isomerase, reductase, and chaperone activities, overview
-
-
?
additional information
?
-
the enzyme assists protein folding in malaria parasites
-
-
?
additional information
?
-
-
the enzyme assists protein folding in malaria parasites
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
the enzyme assists protein folding in malaria parasites
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
the enzyme assists protein folding in malaria parasites
-
-
?
additional information
?
-
-
the enzyme assists protein folding in malaria parasites
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
the enzyme assists protein folding in malaria parasites
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
the enzyme assists protein folding in malaria parasites
-
-
?
additional information
?
-
-
the enzyme assists protein folding in malaria parasites
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
isoform PDI-A shows no activity with insulin, NADPH thioredoxin reductase , NADP malate dehydrogenase, peroxiredoxin, or RNase A
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
PDI has dehydroascorbate reductase activity
-
?
additional information
?
-
-
PDI has dehydroascorbate reductase activity, PDI may play a role in the intraluminal dehydroascorbate reduction
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
substrate specificity of PDI
-
-
?
additional information
?
-
cell-surface PDI is required for transnitrosation of metallothionein by S-nitroso-albumin in intact pulmonary vascular endothelial cells, overview
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
the enzyme shows hormone binding activity, e.g. of L-T3 and 17beta-estradiol hormones
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
PDI specifically binds 3,3',5-triiodo-L-thyronine
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
ERp72 substrate specificity of ERp72, overview. Ep72 does not interact with calnexin
-
-
?
additional information
?
-
-
ERp72 substrate specificity of ERp72, overview. Ep72 does not interact with calnexin
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
the enzyme renatures denatured RNase A
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
the enzyme has an essential role that is distinct from its function in formation of native disulphides
-
-
?
additional information
?
-
-
essential enzyme for yeast cell growth, both oxidase and isomerase activities are required
-
-
?
additional information
?
-
-
PDI plays a key role in catalyzing the folding of secretory proteins
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
the enzyme is an essential catalyst of disulfide formation with two cysteines in the active site facilitating thiol-disulfide exchange
-
-
?
additional information
?
-
-
the organism is completely dependent on PDI activity for growth
-
-
?
additional information
?
-
-
all 5 domains of PDI are required for full catalytic activity
-
-
?
additional information
?
-
-
Eug1p, Mpd1p, Mpd2p, and Eps1p partially compensate for PDI, substrate specificity of PDI
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
structure and mechanism of PDI in disulfide formation and oxidative protein folding, overview
-
-
?
additional information
?
-
-
structure and mechanism of PDI in disulfide formation and oxidative protein folding, overview
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
protein disulfide isomerase has a concentration-dependent chaperone-activity and inhibits the aggregation of rhodanese, which has no disulfide bonds
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
the organism is completely dependent on PDI activity for growth
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
PDI is involved in the cellular growth and response to nutritional and oxidative stress, regulation, overview
-
-
?
additional information
?
-
-
PDI is involved in the cellular growth and response to nutritional and oxidative stress, regulation, overview
-
-
?
additional information
?
-
PDI is involved in the cellular growth and response to nutritional and oxidative stress, regulation, overview
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
the isozymes catalyze refolding of reduced and denatured lysozyme
-
-
?
additional information
?
-
-
the isozymes catalyze refolding of reduced and denatured lysozyme
-
-
?
additional information
?
-
the single domain PDI-1 and the class 1 PDI-2 are not essential for the organism
-
-
?
additional information
?
-
-
the single domain PDI-1 and the class 1 PDI-2 are not essential for the organism
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
alkaline protease inhibitor
?
apolipoprotein B100
?
-
the enzyme assists in the oxidative folding of apolipoprotein B100
-
-
?
carboxypeptidase Y
?
-
maturation of carboxypeptidase Y
-
-
?
denatured RNase A + GSH
renatured RNase A + GSSG
-
-
-
-
?
E2A homodimer
E2A-basic helix-loop-helix protein heterodimer
-
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
-
?
estrogen receptor alpha
?
-
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
-
-
?
glutathione disulfide
glutathione
-
-
-
?
Insulin-(SS) + GSH
Insulin-(SH)2 + GSSG
integrin alphaIIbbeta3
?
-
-
-
-
?
integrin alphaMb2
?
-
-
-
-
?
integrin alphaVb3
?
-
-
-
-
?
integrin alphaVbeta3
?
-
-
-
-
?
integrin subunit alpha11
?
-
the enzyme activates integrin subunit alpha11
-
-
?
integrin subunit beta1
?
-
the enzyme activates integrin subunit beta1
-
-
?
NADPH oxidase A
?
-
-
-
-
?
neuronal nitric oxide synthase
?
-
the enzyme catalyzes neuronal nitric oxide synthase dimerization
-
-
?
protein-(SSG)2n
protein(SS)n + n(GSSG)
-
-
-
-
?
reduced denatured RNase A + GSH
reduced renatured RNase A + GSSG
-
-
-
-
?
reduced ribonuclease A
denatured ribonuclease A
-
-
-
?
reduced RNase
denatured RNase
-
-
-
?
transforming growth factor-beta1
?
-
-
-
-
?
unfolded RNase
refolded RNase
-
-
?
additional information
?
-
alkaline protease inhibitor
?
-
folding and rearrangement of alkaline protease inhibitor
-
-
?
alkaline protease inhibitor
?
-
folding and rearrangement of alkaline protease inhibitor
-
-
?
HED-SSM
MSH + HED
a mixed disulfide
-
-
?
HED-SSM
MSH + HED
a mixed disulfide
-
-
?
HED-SSM
MSH + HED
a mixed disulfide
-
-
?
HED-SSM
MSH + HED
a mixed disulfide
-
-
?
HED-SSM
MSH + HED
a mixed disulfide
-
-
?
HED-SSM
MSH + HED
a mixed disulfide
-
-
?
HED-SSM
MSH + HED
a mixed disulfide
-
-
?
Insulin-(SS) + GSH
Insulin-(SH)2 + GSSG
-
-
-
-
?
Insulin-(SS) + GSH
Insulin-(SH)2 + GSSG
-
-
-
-
?
Insulin-(SS) + GSH
Insulin-(SH)2 + GSSG
-
-
-
?
Insulin-(SS) + GSH
Insulin-(SH)2 + GSSG
-
protein disulfide isomerase supports proinsulin folding as chaperone and isomerase
-
-
?
Insulin-(SS) + GSH
Insulin-(SH)2 + GSSG
-
-
-
-
?
Insulin-(SS) + GSH
Insulin-(SH)2 + GSSG
-
-
-
-
?
Insulin-(SS) + GSH
Insulin-(SH)2 + GSSG
-
-
-
-
?
Insulin-(SS) + GSH
Insulin-(SH)2 + GSSG
-
-
-
-
?
Insulin-(SS) + GSH
Insulin-(SH)2 + GSSG
-
-
-
-
?
Proteins
?
-
-
-
-
?
Proteins
?
-
native, reduced or with wrong disulfide bonds
-
-
?
Proteins
?
-
facilitates the formation of the correct disulfide bonds within newly synthesized polypeptides
-
-
?
Proteins
?
-
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
-
-
?
Proteins
?
-
involved in cotranslational disulfide bond formation
-
-
?
Proteins
?
-
implicated in the biosynthesis of secretory proteins
-
-
?
Proteins
?
-
enzyme may play a physiological role in the catalysis of S-S-bond formation in prolactin
-
-
?
Proteins
?
-
native, reduced or with wrong disulfide bonds
-
-
?
Proteins
?
-
may play a role in the formation of disulfide bonds in extracellular and periplasmic proteins
-
-
?
Proteins
?
-
native, reduced or with wrong disulfide bonds
-
-
?
Proteins
?
-
facilitates the formation of disulfides during the folding and processing of membrane and secretory proteins
-
-
?
Proteins
?
-
enzyme may be involved in the formation of intra-chain and inter-chain disulfide bonds in procollagen
-
-
?
Proteins
?
-
may play a role in retaining prolyl 4-hydroxylase in its native conformation
-
-
?
Proteins
?
-
native, reduced or with wrong disulfide bonds
-
-
?
Proteins
?
-
enzyme may be involved in the formation of intra-chain and inter-chain disulfide bonds in procollagen
-
-
?
Proteins
?
-
platelet enzyme may play a role in the various haemostatic and tissue remodelling processes in which platelets are involved
-
-
?
Proteins
?
-
implicated in the biosynthesis of secretory proteins
-
-
?
Proteins
?
-
native, reduced or with wrong disulfide bonds
-
-
?
Proteins
?
-
may play a role in the formation of disulfide bonds in extracellular and periplasmic proteins
-
-
?
Proteins
?
-
catalysis of native disulfide bond formation
-
-
?
Proteins
?
-
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
-
-
?
Proteins
?
-
native, reduced or with wrong disulfide bonds
-
-
?
Proteins
?
-
may play a role in the formation of disulfide bonds in extracellular and periplasmic proteins
-
-
?
Proteins
?
-
enzyme may be involved in the formation of intra-chain and inter-chain disulfide bonds in procollagen
-
-
?
Proteins
?
-
native, reduced or with wrong disulfide bonds
-
-
?
Proteins
?
-
may play a role in the formation of disulfide bonds in extracellular and periplasmic proteins
-
-
?
Proteins
?
-
native, reduced or with wrong disulfide bonds
-
-
?
Proteins
?
-
may play a role in the formation of disulfide bonds in extracellular and periplasmic proteins
-
-
?
Proteins
?
-
native, reduced or with wrong disulfide bonds
-
-
?
Proteins
?
-
may play a role in the formation of disulfide bonds in extracellular and periplasmic proteins
-
-
?
Proteins
?
-
native, reduced or with wrong disulfide bonds
-
-
?
Proteins
?
-
may play a role in the formation of disulfide bonds in extracellular and periplasmic proteins
-
-
?
Proteins
?
-
native, reduced or with wrong disulfide bonds
-
-
?
Proteins
?
-
proposed physiological role as catalyst of formation of native disulfide bonds in nascent and newly synthesized secretory proteins
-
-
?
Proteins
?
-
involved in cotranslational disulfide bond formation
-
-
?
Proteins
?
-
implicated in the biosynthesis of secretory proteins
-
-
?
Proteins
?
-
native, reduced or with wrong disulfide bonds
-
-
?
Proteins
?
-
involved in the assembly of wheat storage proteins within the endoplasmic reticulum
-
-
?
Proteins
?
-
plays a role in the formation of disulfide bonds during biosynthesis of wheat storage proteins
-
-
?
tissue factor
?
-
-
-
-
?
tissue factor
?
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
structure and mechanism of PDI in disulfide formation and oxidative protein folding, overview
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
the enzyme may be significant in the action of triiodothyronine towards the target cells
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
structure and mechanism of PDI in disulfide formation and oxidative protein folding, overview
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
in vivo, disulfide bond formation is mainly catalyzed by protein disulfide isomerase
-
-
?
additional information
?
-
-
in vivo, disulfide bond formation is mainly catalyzed by protein disulfide isomerase
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
DsbC resolves incorrect disulfides whose formation has been catalyzed by redox-active copper
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
the enzyme plays a crucial role in folding periplasmatically excreted proteins
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
the enzyme acts as a thyroid-hormone binding protein
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
enzyme is involved in the proper folding or quality control of storage proteins
-
-
?
additional information
?
-
-
GmPDIL-1 and GmPDIL-2 function as molecular chaperones, and prevent the aggregation of unfolded rhodanese, while GmPDIL-3a and GmPDIL-3b do not
-
-
?
additional information
?
-
HlPDI-1 might be involved in tick blood feeding and Babesia parasite infection in ticks
-
-
?
additional information
?
-
HlPDI-1 might be involved in tick blood feeding and Babesia parasite infection in ticks
-
-
?
additional information
?
-
HlPDI-1 might be involved in tick blood feeding and Babesia parasite infection in ticks
-
-
?
additional information
?
-
-
HlPDI-1 might be involved in tick blood feeding and Babesia parasite infection in ticks
-
-
?
additional information
?
-
HlPDI-3 might be involved in tick blood feeding and Babesia parasite infection in ticks
-
-
?
additional information
?
-
HlPDI-3 might be involved in tick blood feeding and Babesia parasite infection in ticks
-
-
?
additional information
?
-
HlPDI-3 might be involved in tick blood feeding and Babesia parasite infection in ticks
-
-
?
additional information
?
-
-
HlPDI-3 might be involved in tick blood feeding and Babesia parasite infection in ticks
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
structure and mechanism of PDI in disulfide formation and oxidative protein folding, overview
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
protein disulfide isomerase contributes to the activation of cryptic initiator protein tissue factoron microvesicles in vitro
-
-
?
additional information
?
-
-
protein disulfide isomerase PDI directly interacts with thiol-containing fibrinogen receptor alphaIIbbeta3. PDI has greater ability to isomerize disulfide bonds than the alphaIIbbeta3 integrin
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
PDI catalyzes disulfide bond formation in the endoplasmic reticulum
-
-
?
additional information
?
-
-
PDI catalyzes disulfide bond formation in the endoplasmic reticulum
-
-
?
additional information
?
-
-
PDI specifically associates with signal peptide peptidase, SPP, independently of human cytomegalovirus glycoprotein US2, but not with Derlin-1
-
-
?
additional information
?
-
-
PDI specifically binds 3,3',5-triiodo-L-thyronine
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
the enzyme has a single E2-binding site
-
-
?
additional information
?
-
-
the enzyme has three catalytic activities including thiol-disulfide oxireductase, disulfide isomerase, and redox-dependent chaperone
-
-
?
additional information
?
-
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
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
the enzyme has a single E2-binding site
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
PDILT forms intermolecular disulfide bonds in testis
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
PDI is required in vivo for both fibrin generation and platelet thrombus formation
-
-
?
additional information
?
-
-
protein disulfide isomerase directly promotes initiator protein tissue factor-dependent fibrin production during thrombus formation in vivo
-
-
?
additional information
?
-
-
AGR2 is essential for production of intestinal mucin MUC2, but is not required for establishment of intestinal secretory epithelial cell lineages
-
-
?
additional information
?
-
-
PDI specifically binds 3,3',5-triiodo-L-thyronine
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
the enzyme assists protein folding in malaria parasites
-
-
?
additional information
?
-
-
the enzyme assists protein folding in malaria parasites
-
-
?
additional information
?
-
-
the enzyme assists protein folding in malaria parasites
-
-
?
additional information
?
-
the enzyme assists protein folding in malaria parasites
-
-
?
additional information
?
-
-
the enzyme assists protein folding in malaria parasites
-
-
?
additional information
?
-
the enzyme assists protein folding in malaria parasites
-
-
?
additional information
?
-
the enzyme assists protein folding in malaria parasites
-
-
?
additional information
?
-
-
the enzyme assists protein folding in malaria parasites
-
-
?
additional information
?
-
the enzyme assists protein folding in malaria parasites
-
-
?
additional information
?
-
the enzyme assists protein folding in malaria parasites
-
-
?
additional information
?
-
-
the enzyme assists protein folding in malaria parasites
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
PDI has dehydroascorbate reductase activity, PDI may play a role in the intraluminal dehydroascorbate reduction
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
cell-surface PDI is required for transnitrosation of metallothionein by S-nitroso-albumin in intact pulmonary vascular endothelial cells, overview
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
PDI specifically binds 3,3',5-triiodo-L-thyronine
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
the enzyme has an essential role that is distinct from its function in formation of native disulphides
-
-
?
additional information
?
-
-
essential enzyme for yeast cell growth, both oxidase and isomerase activities are required
-
-
?
additional information
?
-
-
PDI plays a key role in catalyzing the folding of secretory proteins
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
the enzyme is an essential catalyst of disulfide formation with two cysteines in the active site facilitating thiol-disulfide exchange
-
-
?
additional information
?
-
-
the organism is completely dependent on PDI activity for growth
-
-
?
additional information
?
-
structure and mechanism of PDI in disulfide formation and oxidative protein folding, overview
-
-
?
additional information
?
-
-
structure and mechanism of PDI in disulfide formation and oxidative protein folding, overview
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
the organism is completely dependent on PDI activity for growth
-
-
?
additional information
?
-
PDI is involved in the cellular growth and response to nutritional and oxidative stress, regulation, overview
-
-
?
additional information
?
-
-
PDI is involved in the cellular growth and response to nutritional and oxidative stress, regulation, overview
-
-
?
additional information
?
-
PDI is involved in the cellular growth and response to nutritional and oxidative stress, regulation, overview
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
the single domain PDI-1 and the class 1 PDI-2 are not essential for the organism
-
-
?
additional information
?
-
-
the single domain PDI-1 and the class 1 PDI-2 are not essential for the organism
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
1,1-bis(4-hydroxyphenyl)ethane
-
i.e.bisphenol E, 15% inhibition at 0.0125 mM
1,3-diphenylpropane
-
8% inhibition at 0.0125 mM
12-O-Tetradecanoylphorbol 13-acetate
-
binds to and moderately inhibits PDI
16F16
-
irreversible inhibition
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
2,4-dinitrochlorobenzene
-
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-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
3,3',5-triiodo-L-thyronine
3,3',5-triiodothyronine
-
-
4,4'-diisothiocyano-2,2'-stilbene disulfonic acid
-
considerably more effective after preincubation with DTT
4,4'-methylenebisphenol
-
12% inhibition at 0.0125 mM
4-(6-methylimidazo[1,2-a]pyridin-2-yl)benzene-1,2-diol
-
-
4-alpha-cumylphenol
-
18% inhibition at 0.0125 mM
4-amino-phenylarsine oxide
-
0.0058 mM, 50% inhibition of tyramine-S-S-poly(D-lysine) reduction
4-chloromercuribenzoic acid
4-hydroxy-2-nonenal
-
44% inhibition at 0.03 mM
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
8-azido-ATP
-
for the ATPase activity, binds at the same site as ATP
acrolein
-
79% inhibition at 0.03 mM
anti-PDI Fab fragments
-
-
-
Ca2+
-
1 mM, 40% inhibition
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-methanethiosulfonate
-
abolishes PDI oxidoreductase but not chaperone activity
Mg2+
-
1 mM, 20% inhibition
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
N-[2-methyl-2-(morpholin-4-yl)propyl]-1,2-benzothiazol-3-amine
-
-
NEM
-
incubation after pretreatment with DTT or GSH
neomycin
-
analysis of binding and dissociation constants with PDI and PDI domain deletion mutants
nitazoxanide
-
a broad-spectrum anti-parasitic drug
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
phenyl vinyl sulfonate
-
-
Phenylarsine oxide
-
complete inhibition at 0.01-0.1 mM in vivo
quercetin 3-rutinoside
-
-
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
streptomycin
-
analysis of binding and dissociation constants with PDI and PDI domain deletion mutants
tert-2-hexenal
-
32% inhibition at 1 mM
-
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
tizoxanide
-
deacetylated metabolite of nitazoxanide
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
Zn2+
-
1 mM, 70% inhibition
3,3',5-triiodo-L-thyronine
-
and analogs
3,3',5-triiodo-L-thyronine
-
inhibits PDI isomerase activity
3,3',5-triiodo-L-thyronine
-
inhibits PDI isomerase activity
3,3',5-triiodo-L-thyronine
-
30% inhibition at 0.0125 mM
3,3',5-triiodo-L-thyronine
-
inhibits PDI isomerase activity
3,4-dichlorophenol
-
inhibits PDI 3,3',5-triiodo-L-thyronine binding activity
3,4-dichlorophenol
-
inhibits PDI 3,3',5-triiodo-L-thyronine binding activity
3,4-dichlorophenol
-
inhibits PDI 3,3',5-triiodo-L-thyronine binding activity
4-chloromercuribenzoic acid
-
4-chloromercuribenzoic acid
-
-
4-nonylphenol
-
inhibits PDI 3,3',5-triiodo-L-thyronine binding activity
4-nonylphenol
-
inhibits PDI 3,3',5-triiodo-L-thyronine binding activity
4-nonylphenol
-
inhibits PDI 3,3',5-triiodo-L-thyronine binding activity
4-octylphenol
-
inhibits PDI 3,3',5-triiodo-L-thyronine binding activity
4-octylphenol
-
inhibits PDI 3,3',5-triiodo-L-thyronine binding activity
4-octylphenol
-
inhibits PDI 3,3',5-triiodo-L-thyronine binding activity
bacitracin
-
-
bacitracin
-
commercial bacitracin consists of 65% bacitracin A and B
bacitracin
-
a PDI-specific inhibitor
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
-
a PDI-specific inhibitor
bacitracin
-
full inhibition of reductase activity at 0.2 mM
bacitracin
-
infusion of blood vessels inhibits platelet thrombus formation and fibrin generation
bacitracin A
-
-
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
Cd2+
-
-
iodoacetamide
-
-
iodoacetamide
-
pH-dependent inactivation
iodoacetamide
alkylation of PDIp by iodoacetamide fully abolishes its enzymatic activity while it still retains most of its chaperone activity
iodoacetamide
-
incubation after pretreatment with DTT or GSH
iodoacetate
-
-
iodoacetate
-
inactivation by alkylation follows pseudo-first-order kinetics
iodoacetate
-
1 mM, almost complete inhibition after reduction with 0.01 mM DTT. No inhibition in absence of DTT
iodoacetate
-
inactivation by alkylation follows pseudo-first-order kinetics
N-ethylmaleimide
-
pH-independent inactivation within the range of pH 6.3-7.0
N-ethylmaleimide
-
abolishes PDI oxidoreductase but not chaperone activity
Pentachlorophenol
-
inhibits PDI 3,3',5-triiodo-L-thyronine binding activity
Pentachlorophenol
-
inhibits PDI 3,3',5-triiodo-L-thyronine binding activity
Pentachlorophenol
-
inhibits PDI 3,3',5-triiodo-L-thyronine binding activity
quercetin-3-rutinoside
-
-
quercetin-3-rutinoside
-
-
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
-
inhibition by PDI-specific antibodiy RL90
-
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
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
-
inhibition of cell surface PDI induces a marked increase in tissue factor procoagulant function
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
-
enzyme silencing decreases Nox1 expression and reactive oxygen species production as well as platelet-derived growth factor-induced Rac1 and RhoA activities
malfunction
-
enzyme silencing prevents Nox responses to angiotensin II and inhibits Akt phosphorylation in vascular cells and parasite phagocytosis in macrophages
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
enzyme-mediated disulfide bond exchange plays a pivotal role in the post-ligation phase of integrin alphaIIbbeta3-mediated adhesion to fibrinogen
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 is a catalyst of oxidative protein folding
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
-
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 receives electrons preferentially from the mycothiol (MSH)/mycothione reductase (Mtr)/NADPH pathway
metabolism
-
the enzyme receives electrons preferentially from the mycothiol (MSH)/mycothione reductase (Mtr)/NADPH pathway
-
metabolism
-
the enzyme receives electrons preferentially from the mycothiol (MSH)/mycothione reductase (Mtr)/NADPH pathway
-
metabolism
-
the enzyme receives electrons preferentially from the mycothiol (MSH)/mycothione reductase (Mtr)/NADPH pathway
-
metabolism
-
the enzyme receives electrons preferentially from the mycothiol (MSH)/mycothione reductase (Mtr)/NADPH pathway
-
metabolism
-
the enzyme receives electrons preferentially from the mycothiol (MSH)/mycothione reductase (Mtr)/NADPH pathway
-
metabolism
-
the enzyme receives electrons preferentially from the mycothiol (MSH)/mycothione reductase (Mtr)/NADPH pathway
-
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
-
FXIII-PDI activity may have a role in platelet function
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
-
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 a multifunctional protein for catalyzing the formation, isomerization, and reduction of disulfide bonds
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
PDIA3 is an endoplasmic reticulum stress protein. It is induced by oxidative stress and plays a role in relation to stress regulation
physiological function
-
PDIp may function as a protein-folding catalyst for secretory digestive enzymes
physiological function
physiological roles of PDIA3 and PDI-P5 in sperm maturation and fertilization, overview
physiological function
-
the enzyme is involved in myocardial angiogenesis, overview
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
-
the enzyme is required for infection by Chlamydia species
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 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 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
-
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
PDIL2-3 does not facilitate the oxidative folding of proglutelins
physiological function
-
protein disulfide isomerase blocks transcription factor C/EBP-alpha translation but not transcription
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
-
enzyme overexpression spontaneously enhances Nox activation and expression. In neutrophils, enzyme redox-dependently associates with p47phox and supports the respiratory burst
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
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
-
protein disulfide isomerase directly interacts with beta-actin Cys374 during cell adhesion and spreading and regulates cytoskeleton reorganization
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
-
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 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
-
the enzyme is associated with the reproductive development and enriched in adult females
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
-
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 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
-
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 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
-
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
-
PDI1 is a virulence factor of Phytophthora parasitica and contributes to plant infection
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
-
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
-
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
-
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
-
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
-
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
-
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 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
-
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
-
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
homotetramer
4 * 72397, PDIL2-3, calculated from amino acid sequence
multimer
-
x * 52000 + x * ?, SDS-PAGE
oligomer
-
x * 62000, gel filtration, x * 56000, calculated
?
x * 55000, SDS-PAGE
?
-
x * 56400, calculated from amino acid sequence
?
-
x * 75000-80000, SDS-PAGE
?
-
x * 47400, calculated from amino acid sequence
?
-
x * 54300, calculation from nucleotide sequence
?
-
x * 27300, calculated from amino acid sequence
?
-
x * 30000, His6-tagged enzyme, SDS-PAGE
?
-
x * 25910, calculation from nucleotide sequence
?
-
x * 55000, SDS-PAGE, another band with MW 45000 represents a proteolytic degradation product
?
-
x * 60000 and x * 63000, SDS-PAGE
?
x * 47850, sequence calculation
?
x * 53680, sequence calculation
?
x * 54890, sequence calculation
?
-
x * 61200, SDS-PAGE under reducing conditions
?
-
x * 57000, SDS-PAGE, immunoprecipitation
?
-
x * 58000, recombinant ECaSt/PDI, SDS-PAGE
?
x * 27700, ERp27, SDS-PAGE
?
-
x * 53100, oxidized enzyme, calculated from amino acid sequence
?
-
x * 58800, reduced enzyme, small-angle X-ray scattering
?
-
x * 66400, oxidized enzyme, small-angle X-ray scattering
?
x * 15000, isozyme pdi-15, SDS-PAGE
?
x * 40000, isozyme pdi-40, SDS-PAGE
?
x * 47000, isozyme pdi-47, SDS-PAGE
?
x * 52000, isozyme pdi-52, SDS-PAGE
?
-
x * 65000, recombinant mature PDILT without signal sequence, SDS-PAGE
?
-
x * 52000, native enzyme, SDS-PAGE, x * 55000, recombinant His-tagged 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 * 55114, calculation from nucleotide sequence
?
-
x * 58900, SDS-PAGE under reducing conditions, other bands with MW 53800 and 55200 represent proteolytic degradation products of the 58900 MW protein
?
x * 26032, calculated from sequence
?
-
x * 26032, calculated from sequence
-
?
x * 52800, calculated from amino acid sequence
?
x * 39490, sequece calculation
?
-
x * 39490, sequece calculation
-
?
x * 48074, PDI-P5, sequence calculation, x * 56859, PDIA3, sequence calculation
?
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 * 69000, isoform PDIL3A, SDS-PAGE
?
x * 70000, isoform PDIL2, SDS-PAGE
?
x * 45000, recombinant PDI-1, SDS-PAGE, x * 80000, recombinant PDI-2, SDS-PAGE
dimer
-
-
dimer
-
2 * 57000, SDS-PAGE
dimer
-
2 * 57000, SDS-PAGE under reducing and nonreducing conditions, association between subunits is noncovalent
dimer
-
2 * 60000, SDS-PAGE
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
-
DsbC dimerizes to form a protein binding site flanked by two catalytic thioredoxin domains
dimer
-
DsbG is a homodimer with an N-terminal dimerization domain on each subunit, crystal structure
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 * 63000, SDS-PAGE
dimer
-
2 * 60000, SDS-PAGE
dimer
-
and monomer. 2 * 62000, gel filtration, 2 * 56000, calculated
dimer
-
2 * 22000, DsbA, SDS-PAGE, 2 * 25000, DsbC, SDS-PAGE
dimer
-
2 * 55000, about, sequence calculation, 2 * 52000, analytical ultrafiltration
dimer
-
2 * 55000, SDS-PAGE
dimer
-
2 * 70000, SDS-PAGE
dimer
-
crystallization data
monomer
-
1 * 21100, estimated from amino acid sequence
monomer
1 * 64000, analytical ultracentrifugation
monomer
-
1 * 56300, calculated from amino acid sequence
monomer
-
1 * 57700, analytical ultracentrifugation
monomer
-
and dimer. 1 * 62000, gel filtration, 1 * 56000, calculated
monomer
-
predominantly, isozyme PDI-22, SDS-PAGE and gel filtration
additional information
domain organization of PDI, overview
additional information
-
domain organization of PDI, overview
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
-
PDI domain structure, overview
additional information
-
PDI domain organization, overview
additional information
-
a multidomain protein, tertiary structure and function analysis under pressure conditions above 100 MPa, overview
additional information
-
isozyme domain structure, overview
additional information
-
PDI domain structure, 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
-
PDI domain organization, overview
additional information
-
the catalytic domain, residues 88-231, shows a thioredoxin fold with a helical insert
additional information
-
PDI domain structure, overview
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 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 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 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
-
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
the four domains a, b, b', and a' are arranged in an annular manner
additional information
determination and analysis of the crystal structure of the bb domains of ERp57, 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
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
PDI domain structure, overview
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
-
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
-
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 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 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 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
-
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
-
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
-
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
-
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
-
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
-
PDI domain organization, Eug1p, Mpd1p, Mpd2p, and Eps1p have only one catalytic domain with 2 cysteines, overview
additional information
-
the catalytic domains a and a' are responsible for the oxidase and the isomerase activity, respectively
additional information
PDI domain structure, overview
additional information
-
PDI domain structure, 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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
C21S
site-directed mutagenesis, almost inactive mutant
C24S
site-directed mutagenesis, the mutant shows increased activity compared to wild-type enzyme with a mixed disulfide substrate
C21S
-
site-directed mutagenesis, almost inactive mutant
-
C24S
-
site-directed mutagenesis, the mutant shows increased activity compared to wild-type enzyme with a mixed disulfide substrate
-
C21S
-
site-directed mutagenesis, almost inactive mutant
-
C24S
-
site-directed mutagenesis, the mutant shows increased activity compared to wild-type enzyme with a mixed disulfide substrate
-
C21S
-
site-directed mutagenesis, almost inactive mutant
-
C24S
-
site-directed mutagenesis, the mutant shows increased activity compared to wild-type enzyme with a mixed disulfide substrate
-
C21S
-
site-directed mutagenesis, almost inactive mutant
-
C24S
-
site-directed mutagenesis, the mutant shows increased activity compared to wild-type enzyme with a mixed disulfide substrate
-
C21S
-
site-directed mutagenesis, almost inactive mutant
-
C24S
-
site-directed mutagenesis, the mutant shows increased activity compared to wild-type enzyme with a mixed disulfide substrate
-
C21S
-
site-directed mutagenesis, almost inactive mutant
-
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
D180R/D181R
the mutant shows 26.7% of wild type activity
D439A
119% of wild-type 4-hydroxylase activity
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
E431K
the mutant shows 53.6% of wild type activity
E454A
76% of wild-type 4-hydroxylase activity
F258A
-
strongly reduced binding of DELTA-somatostatin
F258I
-
no binding of DELTA-somatostatin
F258W
-
reduced binding of DELTA-somatostatin
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
F449A
63% of wild-type 4-hydroxylase activity
F449E
9% of wild-type 4-hydroxylase activity
F452R
115% of wild-type 4-hydroxylase activity
F454A
-
binds DELTA-somatostatin like wild-type
H278L
-
the mutant protein does not have an appreciable E2-binding activity
I196W
site-directed mutagenesis, the ERp27 mutant shows a structure and ERp57 binding similar to the wild-type enzyme
I272L
-
no binding of DELTA-somatostatin
I272N
-
no binding of DELTA-somatostatin
I272Q
-
no binding of DELTA-somatostatin
I272W
-
no binding of DELTA-somatostatin
I438E
79% of wild-type 4-hydroxylase activity
K246A
-
reduced binding of DELTA-somatostatin
K259A
-
binds DELTA-somatostatin like wild-type
K274A
site-directed mutagenesis, the mutant shows affected interaction with calnexin
K326E
the mutant shows 56% of wild type activity
K326E/E431K
the mutant shows 82.2% of wild type activity
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
K451A
74% of wild-type 4-hydroxylase activity
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
L242A
-
binds DELTA-somatostatin like wild-type
L242T
-
strongly reduced binding of DELTA-somatostatin
L244A
-
reduced binding of DELTA-somatostatin
L244W
-
strongly reduced binding of DELTA-somatostatin
L255A
-
binds DELTA-somatostatin like wild-type
L255R
-
reduced binding of DELTA-somatostatin
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
L446E
107% of wild-type 4-hydroxylase activity
P235G
the mutant shows 61.3% of wild type activity
P245K
-
no full length protein
Q265L
-
the mutant displays similar E2-binding activity as the corresponding wild type proteins
Q265L/H278L
-
the mutant protein does not have any E2-binding activity
R120D
-
less than 2% of wild-type activity in NRCSQGSCWN oxidation assay
R120K
-
71% of wild-type activity in NRCSQGSCWN oxidation assay
R120Q
-
26% of wild-type activity in NRCSQGSCWN oxidation assay
R120S
-
40% of wild-type activity in NRCSQGSCWN oxidation assay
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
R97E
the mutant shows 68.2% of wild type activity
S249A
-
reduced binding of DELTA-somatostatin
S249K
-
binds DELTA-somatostatin like wild-type
S256D
-
reduced binding of DELTA-somatostatin
V220I
-
binds DELTA-somatostatin like wild-type
V437D
102% of wild-type 4-hydroxylase activity
W128F
-
95% of wild-type activity in NRCSQGSCWN oxidation assay
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
-
Q265L/H278L
-
the mutant protein does not have any E2-binding activity
-
C365S/C368S
active site mutant
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
C35S
-
mutagenesis of Cys35 or Cys379 to a Ser causes loss of activity
C379S
-
mutagenesis of Cys35 or Cys379 to a Ser causes loss of activity
C398A/C401A
-
90% residual isomerase activity
C54A/C57A
-
30% residual isomerase activity
C54A/C57A/C398A/C401A
-
15% residual isomerase activity
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
H37P
-
Mutagenesis of His37 to a Pro causes almost complete loss of 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
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
-
mutation in the last alpha helix of domain a', 7.5-8fold reduced appearance rate of folding product RNase A
F449R
no 4-hydroxylase activity, 85% and 93% of wild-type isomerase and reductase activity, respectively
F449W
59%, 133% and 94% of wild-type 4-hydroxylase, isomerase and reductase activity, respectively
F449W
-
no DELTA-somatostatin binding
F449Y
79%, 42% and 87% of wild-type 4-hydroxylase, isomerase and reductase activity, respectively
F449Y
-
binds DELTA-somatostatin like wild-type
G448R
43%, 85% and 93% of wild-type 4-hydroxylase, isomerase and reductase activity, respectively
G448R
-
binds DELTA-somatostatin like wild-type
I272A
-
no binding of DELTA-somatostatin
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
K450A
113% of wild-type 4-hydroxylase activity
K450A
-
binds DELTA-somatostatin like wild-type
L453E
13%, 23% and 48% of wild-type 4-hydroxylase, isomerase and reductase activity, respectively
L453E
-
no DELTA-somatostatin binding
R444A
43%, 83% and 79% of wild-type 4-hydroxylase, isomerase and reductase activity, respectively
R444A
-
binds DELTA-somatostatin like wild-type
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
-
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
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
-
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
-
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
-
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
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
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
-
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 several deletion mutants of PDI by elimination of partial domains or whole domains, overview
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 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
-
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
-
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
-
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
-
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
-
HeLa cells are transfected with PDI-targeting siRNA for PDI knockdown leading to resistance to Chlamydia inefctions
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
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
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
-
transfection of HUVECs with PDI siRNA using electroporation by nucleofector
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
-
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
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
-
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
-
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
-
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
-
a domain a'-deletion mutant shows reduced activity in refolding of RNase compared to the wild-type enzyme
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
-
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
-
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.