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apolipoprotein B100
?
-
the enzyme assists in the oxidative folding of apolipoprotein B100
-
-
?
insulin
reduced insulin
-
-
-
-
?
Insulin-(SS) + GSH
Insulin-(SH)2 + GSSG
-
-
-
?
lysozyme
aggregated lysozyme
-
PDI has antichaperone activity facilitating protein aggregation
-
?
reduced ribonuclease
?
-
refolding of reduced ribonuclease in presence of glutathione, isomerase activity of PDI
-
-
?
RNase A
?
-
reduced and denatured substrate from bovine pancreas
-
-
?
unfolded insulin beta-chain
refolded insulin beta-chain
-
-
-
?
additional information
?
-
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
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
?
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 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
?
-
-
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
-
-
?
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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
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-(cyclopropanecarbonyl)piperazin-1-yl]methyl]-1,2-benzothiazol-3(2H)-one
-
potent, reversible inhibition
3,3',5-triiodo-L-thyronine
3,4-dichlorophenol
-
inhibits PDI 3,3',5-triiodo-L-thyronine binding activity
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-nonylphenol
-
inhibits PDI 3,3',5-triiodo-L-thyronine binding activity
4-octylphenol
-
inhibits PDI 3,3',5-triiodo-L-thyronine binding activity
Diazobenzene sulfonic acid
-
considerably more effective after preincubation with DTT
iodoacetate
-
inactivation by alkylation follows pseudo-first-order kinetics
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
Pentachlorophenol
-
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
3,3',5-triiodo-L-thyronine
-
30% inhibition at 0.0125 mM
3,3',5-triiodo-L-thyronine
-
inhibits PDI isomerase activity
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
iodoacetamide
-
-
iodoacetamide
-
incubation after pretreatment with DTT or GSH
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
-
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Freedman, R.B.; Hawkins, H.C.; Murant, S.J.; Reid, L.
Protein disulphide-isomerase: a homologue of thioredixin implicated in the biosynthesis of secretory proteins
Biochem. Soc. Trans.
16
96-99
1988
Bos taurus, Homo sapiens, Rattus norvegicus
brenda
Pihlajaniemi, T.; Helaakoski, T.; Tasanen, K.; Myllyl, R.; Huhtala, M.L.; Koivu, J.; Kivirikko, K.I.
Molecular cloning of the beta-subunit of human prolyl 4-hydroxylase. This subunit and protein disulfide isomerase are products of the same gene
EMBO J.
6
643-649
1987
Homo sapiens, Rattus norvegicus
brenda
Kaetzel, C.S.; Rao, C.K.; Lamm, M.E.
Protein disulphide-isomerase from human placenta and rat liver
Biochem. J.
241
39-47
1987
Homo sapiens, Rattus norvegicus
brenda
Lambert, N.; Freedman, R.B.
The latency of rat liver microsomal protein disulphide-isomerase
Biochem. J.
228
635-645
1985
Rattus norvegicus
brenda
Lambert, N.; Freedman, R.B.
Chemical modification of essential residues in purified rat liver protein disulphide-isomerase
Biochem. Soc. Trans.
12
1042
1984
Rattus norvegicus
-
brenda
Mills, E.N.C.; Lambert, N.; Freedman, R.B.
Identification of protein disulphide-isomerase as a major acidic polypeptide in rat liver microsomal membranes
Biochem. J.
213
245-248
1983
Rattus norvegicus
brenda
Brockway, B.E.; Foster, S.J.; Freedman, R.B.; Hillson, D.A.
The distribution of protein disulphide-isomerase activity in mammalian tissues
Biochem. Soc. Trans.
10
115-116
1982
Ovis aries, Rattus norvegicus
-
brenda
Freedman, R.B.
Protein disulfide isomerase: multiple roles in the modification of nascent secretory proteins
Cell
57
1069-1072
1989
Bos taurus, Canis lupus familiaris, Homo sapiens, Mammalia, Rattus norvegicus
brenda
Gilbert, H.F.; Kruzel, M.L.; Lyles, M.M.; Harper, J.W.
Expression and purification of recombinant rat protein disulfide isomerase from Escherichia coli
Protein Expr. Purif.
2
194-198
1991
Rattus norvegicus
brenda
Freedman, R.B.; Bulleid, N.J.; Hawkins, H.C.; Paver, J.L.
Role of protein disulphide-isomerase in the expression of native proteins
Biochem. Soc. Symp.
55
167-192
1989
Bos taurus, Canis lupus familiaris, Rattus norvegicus
brenda
Ibbetson, A.L.; Freedman, R.B.
Thiol-protein disulphide oxidoreductases. Assay of microsomal membrane-bound glutathione-insulin transhydrogenase and comparison with protein disulphide-isomerase
Biochem. J.
159
377-384
1976
Rattus norvegicus
brenda
Parry, J.W.I.; Clark, J.R.; Tuite, M.F.; Freedman, R.B.
The expression in E. coli and purification of isolated non-thioredoxin-like domains of human PDI
Biochem. Soc. Trans.
23
71S
1995
Rattus norvegicus
brenda
Hawkins, H.C.; Freedman, R.B.
The reactivities and ionization properties of the active-site dithiol groups of mammalian protein disulphide-isomerase
Biochem. J.
275
335-339
1991
Bos taurus, Rattus norvegicus
brenda
Safran, M.; Leonard, J.L.
Characterization of a N-bromoacetyl-L-thyroxine affinity-labeled 55-kilodalton protein as protein disulfide isomerase in cultured glial cells
Endocrinology
129
2011-2016
1991
Rattus norvegicus
brenda
Gilbert, H.F.
Protein disulfide isomerase
Methods Enzymol.
290
26-50
1998
Bos taurus, Saccharomyces cerevisiae, Mammalia, Rattus norvegicus
brenda
Drazic, M.; Cottrell, R.C.
Some properties of the membrane-bound and solubilised forms of the protein disulphide isomerase of rat liver microsomes
Biochim. Biophys. Acta
484
476-485
1977
Rattus norvegicus
brenda
Horiuchi, R.; Yamauchi, K.; Hayashi, H.; Koya, S.; Takeuchi, Y.; Kato, K.; Kobayashi, M.; Takikawa, H.
Purification and characterization of 55-kDa protein with 3,5,3'-triiodo-L-thyronine-binding activity and protein disulfide-isomerase activity from beef liver membrane
Eur. J. Biochem.
183
529-538
1989
Bos taurus, Homo sapiens, Rattus norvegicus
brenda
Noiva, R.
Enzymatic catalysis of disulfide formation
Protein Expr. Purif.
5
1-13
1994
Bacteria, Saccharomyces cerevisiae, eukaryota, Rattus norvegicus
brenda
Ohba, H.; Harano, T.; Omura, T.
Presence of two different types of protein-disulphide isomerase on cytoplasmic and luminal surfaces of endoplasmic reticulum of rat liver
Biochem. Biophys. Res. Commun.
77
830-836
1977
Rattus norvegicus
brenda
Freeman, R.B.; Hirst, T.R.; Tuite, M.F.
Protein disulphide isomerase: building bridges in protein folding
Trends Biochem. Sci.
19
331-336
1994
Bacteria, Bos taurus, Saccharomyces cerevisiae, Gallus gallus, Oryctolagus cuniculus, eukaryota, Homo sapiens, Rattus norvegicus, Trypanosoma brucei
brenda
Sideraki, V.; Gilbert, H.F.
Mechanism of the antichaperone activity of protein disulfide isomerase: facilitated assembly of large, insoluble aggregates of denatured lysozyme and PDI
Biochemistry
39
1180-1188
2000
Rattus norvegicus
brenda
Nardai, G.; Braun, L.; Csala, M.; Mile, V.; Csermely, P.; Benedetti, A.; Mandl, J.; Banhegyi, G.
Protein-disulfide isomerase- and protein thiol-dependent dehydroascorbate reduction and ascorbate accumulation in the lumen of the endoplasmic reticulum
J. Biol. Chem.
276
8825-8828
2001
Rattus norvegicus
brenda
Wilkinson, B.; Gilbert, H.F.
Protein disulfide isomerase
Biochim. Biophys. Acta
1699
35-44
2004
Bos taurus, Saccharomyces cerevisiae, Escherichia coli, Homo sapiens, Rattus norvegicus
brenda
Solovyov, A.; Gilbert, H.F.
Zinc-dependent dimerization of the folding catalyst, protein disulfide isomerase
Protein Sci.
13
1902-1907
2004
Rattus norvegicus
brenda
Hiroi, T.; Okada, K.; Imaoka, S.; Osada, M.; Funae, Y.
Bisphenol A binds to protein disulfide isomerase and inhibits its enzymatic and hormone-binding activities
Endocrinology
147
2773-2780
2006
Rattus norvegicus
brenda
Zhang, L.M.; St Croix, C.; Cao, R.; Wasserloos, K.; Watkins, S.C.; Stevens, T.; Li, S.; Tyurin, V.; Kagan, V.E.; Pitt, B.R.
Cell-surface protein disulfide isomerase is required for transnitrosation of metallothionein by S-nitroso-albumin in intact rat pulmonary vascular endothelial cells
Exp. Biol. Med.
231
1507-1515
2006
Rattus norvegicus (P04785)
brenda
Zhou, M.; Jacob, A.; Ho, N.; Miksa, M.; Wu, R.; Maitra, S.R.; Wang, P.
Downregulation of protein disulfide isomerase in sepsis and its role in tumor necrosis factor-alpha release
Crit. Care Med.
12
R100
2008
Mus musculus, Rattus norvegicus
brenda
Hashimoto, S.; Okada, K.; Imaoka, S.
Interaction between bisphenol derivatives and protein disulphide isomerase (PDI) and inhibition of PDI functions: requirement of chemical structure for binding to PDI
J. Biochem.
144
335-342
2008
Rattus norvegicus
brenda
Wang, Y.; Narayan, M.
pH Dependence of the isomerase activity of protein disulfide isomerase: insights into its functional relevance
Protein J.
27
181-185
2008
Rattus norvegicus
brenda
Tamang, D.L.; Alves, B.N.; Elliott, V.; Redelman, D.; Wadhwa, R.; Fraser, S.A.; Hudig, D.
Regulation of perforin lysis: implications for protein disulfide isomerase proteins
Cell. Immunol.
255
82-92
2009
Rattus norvegicus, Mus musculus (P27773), Mus musculus C57BL/6 (P27773)
brenda
Pal, R.; Gonzalez, V.; Narayan, M.
Reshuffling activity of protein disulfide isomerase reduces refolding yield in the structure-forming step of the oxidative protein folding reaction
Chem. Lett.
39
263-265
2010
Rattus norvegicus
-
brenda
Okada, K.; Hashimoto, S.; Funae, Y.; Imaoka, S.
Hydroxylated polychlorinated biphenyls (PCBs) interact with protein disulfide isomerase and inhibit its activity
Chem. Res. Toxicol.
22
899-904
2009
Rattus norvegicus
brenda
Okada, K.; Hashimoto, S.; Imaoka, S.
Biological functions of protein disulfide isomerase as a target of phenolic endocrine-disrupting chemicals
J. Health Sci.
56
1-13
2010
Homo sapiens, Mus musculus, Rattus norvegicus
-
brenda
Walker, A.
Protein disulfide isomerase and the endoplasmic reticulum in amyotrophic lateral sclerosis
J. Neurosci.
30
3865-3867
2010
Homo sapiens, Mus musculus, Rattus norvegicus
brenda
Kozlov, G.; Maeaettaenen, P.; Schrag, J.D.; Hura, G.L.; Gabrielli, L.; Cygler, M.; Thomas, D.Y.; Gehring, K.
Structure of the noncatalytic domains and global fold of the protein disulfide isomerase ERp72
Structure
17
651-659
2009
Rattus norvegicus (P38659), Rattus norvegicus
brenda
Wang, S.; Park, S.; Kodali, V.K.; Han, J.; Yip, T.; Chen, Z.; Davidson, N.O.; Kaufman, R.J.
Identification of protein disulfide isomerase 1 as a key isomerase for disulfide bond formation in apolipoprotein B100
Mol. Biol. Cell
26
594-604
2015
Rattus norvegicus
brenda
Kaplan, A.; Gaschler, M.M.; Dunn, D.E.; Colligan, R.; Brown, L.M.; Palmer, A.G.; Lo, D.C.; Stockwell, B.R.
Small molecule-induced oxidation of protein disulfide isomerase is neuroprotective
Proc. Natl. Acad. Sci. USA
112
E2245-E2252
2015
Rattus norvegicus
brenda