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Information on EC 5.3.4.1 - protein disulfide-isomerase and Organism(s) Homo sapiens and UniProt Accession P30101

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EC Tree
     5 Isomerases
         5.3 Intramolecular oxidoreductases
             5.3.4 Transposing S-S bonds
                5.3.4.1 protein disulfide-isomerase
IUBMB Comments
Needs reducing agents or partly reduced enzyme; the reaction depends on sulfhydryl-disulfide interchange.
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This record set is specific for:
Homo sapiens
UNIPROT: P30101
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Reaction Schemes
catalyses the rearrangement of -S-S- bonds in proteins
Synonyms
fibronectin, pdi, protein disulfide isomerase, erp57, pdia3, protein disulphide isomerase, cabp1, erp44, disulfide isomerase, erp72, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
multifunctional protein disulfide isomerase
-
protein disulfide isomerase
-
5'-MD
-
-
-
-
58 kDa glucose regulated protein
-
-
-
-
58 kDa microsomal protein
-
-
-
-
AGR2
-
-
CaBP1
-
-
-
-
CaBP2
Cellular thyroid hormone binding protein
-
-
-
-
Disulfide interchange enzyme
-
-
-
-
Disulfide isomerase ER-60
-
-
-
-
DsbA
-
-
-
-
DsbC
-
-
-
-
DsbD
-
-
-
-
endoplasmic reticulum protein EUG1
-
-
-
-
ER protein 57
-
-
ER58
-
-
-
-
ER60
-
-
ERcalcistorin/protein-disulfide isomerase
-
i.e. ECaSt/PDI
ERdj5
-
-
Ero1
-
-
ERP-57
-
-
ERp-72 homolog
-
-
-
-
ERp18
-
-
ERp27
ERp28
Erp46
ERp57
ERP59
-
-
-
-
ERP60
-
-
-
-
ERp72
fibronectin
-
extracellular matrix protein fibronectin contains an intrinsic protein-disulfide isomerase activity
HIP-70
-
-
-
-
Iodothyronine 5'-monodeiodinase
-
-
-
-
multifunctional protein disulfide isomerase
-
P55
-
-
-
-
P58
-
-
-
-
pancreas-specific protein disulfide isomerase
PDI I
-
-
PDI II
-
-
PDIA1
PDIA3
-
-
PDIr
-
-
protein disulfide isomerase
protein disulfide isomerase A1
-
-
protein disulfide isomerase A5
-
Protein disulfide isomerase P5
-
-
-
-
Protein disulfide isomerase-related protein
-
-
-
-
Protein disulphide isomerase
Protein ERp-72
-
-
-
-
protein-disulfide isomerase
-
-
R-cognin
-
-
-
-
Rearrangease
-
-
-
-
Reduced ribonuclease reactivating enzyme
-
-
-
-
Retina cognin
-
-
-
-
S-S rearrangase
-
-
-
-
thioredoxin domain-containing protein 5
-
Thyroid hormone-binding protein
-
-
-
-
Thyroxine deiodinase
-
-
-
-
additional information
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
catalyses the rearrangement of -S-S- bonds in proteins
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
isomerization
-
-
-
-
intramolecular oxidoreduction
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
Protein disulfide-isomerase
Needs reducing agents or partly reduced enzyme; the reaction depends on sulfhydryl-disulfide interchange.
CAS REGISTRY NUMBER
COMMENTARY hide
37318-49-3
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
RNase B
?
show the reaction diagram
the ability of the ERp57-calnexin complex to mediate folding of 3H-labeled RNase B is completely dependent on a functional interaction between ERp57 and calnexin, overview
-
-
?
apolipoprotein B
?
show the reaction diagram
-
-
-
-
?
beta-actin
?
show the reaction diagram
-
-
-
-
?
bovine pancreatic trypsin inhibitor
?
show the reaction diagram
-
-
-
-
?
creatine kinase
?
show the reaction diagram
-
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
?
show the reaction diagram
-
-
-
-
?
denatured D-glyceraldehyde-3-phosphate dehydrogenase
refolded D-glyceraldehyde-3-phosphate dehydrogenase
show the reaction diagram
-
chaperone activity of PDI
-
?
denatured rhodanese
?
show the reaction diagram
-
PDI exhibits chaperone activity with rhodanese
-
-
?
dieosin glutathione disulfide
eosin glutathione sulfide
show the reaction diagram
-
-
-
?
E2A homodimer
E2A-basic helix-loop-helix protein heterodimer
show the reaction diagram
-
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
show the reaction diagram
-
i.e. human immunodeficiency virus gp120
-
?
estrogen receptor alpha
?
show the reaction diagram
glutathione disulfide
glutathione
show the reaction diagram
-
-
-
?
insulin
?
show the reaction diagram
insulin
reduced insulin
show the reaction diagram
-
-
-
?
Insulin-(SS) + GSH
Insulin-(SH)2 + GSSG
show the reaction diagram
integrin alphaIIbbeta3
?
show the reaction diagram
-
-
-
-
?
integrin alphaMb2
?
show the reaction diagram
-
-
-
-
?
integrin alphaVb3
?
show the reaction diagram
-
-
-
-
?
integrin alphaVbeta3
?
show the reaction diagram
-
-
-
-
?
integrin subunit alpha11
?
show the reaction diagram
-
the enzyme activates integrin subunit alpha11
-
-
?
integrin subunit beta1
?
show the reaction diagram
-
the enzyme activates integrin subunit beta1
-
-
?
lactate dehydrogenase
?
show the reaction diagram
-
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
-
-
?
NRCSQGSCWN
NRCSQGSCWN
show the reaction diagram
procollagen I
?
show the reaction diagram
-
-
-
-
?
procollagen III
?
show the reaction diagram
-
-
-
-
?
protein-(SSG)2n
protein(SS)n + n(GSSG)
show the reaction diagram
-
-
-
-
?
Proteins
?
show the reaction diagram
Proteins
Proteins
show the reaction diagram
reduced Ero1alpha
oxidized Ero1alpha
show the reaction diagram
-
-
-
-
?
reduced glutathione peroxidase 7
oxidized glutathione peroxidase 7
show the reaction diagram
-
-
-
-
?
reduced glutathione peroxidase 8
oxidized glutathione peroxidase 8
show the reaction diagram
-
-
-
-
?
rhodanese
?
show the reaction diagram
-
chaperone activity
-
-
?
riboflavin binding protein
?
show the reaction diagram
-
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 A
?
show the reaction diagram
-
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
?
show the reaction diagram
-
-
-
-
?
RNase
?
show the reaction diagram
-
-
-
-
?
RNase A
?
show the reaction diagram
sRNase
?
show the reaction diagram
-
-
-
-
?
tachyplesin I
?
show the reaction diagram
-
-
-
-
?
thrombospondin-1 + alpha-thrombin + antithrombin III
thrombospondin-1-S-S-alpha-thrombin-S-S-antithrombin III
show the reaction diagram
-
PDI catalyzes formation of disulfide linked complexes of thrombospondin
-
?
tissue factor
?
show the reaction diagram
transforming growth factor-beta1
?
show the reaction diagram
-
-
-
-
?
unfolded bovine pancreatic trypsin inhibitor
refolded bovine pancreatic trypsin inhibitor
show the reaction diagram
-
-
-
?
unfolded disulfide-bonded protein
refolded disulfide-bonded protein
show the reaction diagram
-
-
-
?
unfolded insulin + reduced glutathione
refolded insulin + oxidized glutathione
show the reaction diagram
-
-
-
?
unfolded proinsulin
refolded proinsulin
show the reaction diagram
-
PDI acts both as a chaperone and as an isomerase during folding and disulfid bond formation of proinsulin, chaperone and isomerization activity is required at the beginning of proinsulin folding, the late refolding process only depends on the isomerase activity
-
?
unfolded RNase
refolded RNase
show the reaction diagram
unfolded RNase A
refolded RNase A
show the reaction diagram
unfolded rRNaSe
refolded rRNase
show the reaction diagram
-
refolding of reduced rRNaSe
-
?
vitronectin + thrombin + antithrombin
vitronectin-thrombin-antithrombin
show the reaction diagram
-
PDI catalyzes the formation of disulfide-linked complexes of vitronectin with thrombin-antithrombin
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
beta-actin
?
show the reaction diagram
-
-
-
-
?
E2A homodimer
E2A-basic helix-loop-helix protein heterodimer
show the reaction diagram
-
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
?
show the reaction diagram
-
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
show the reaction diagram
-
-
-
?
Insulin-(SS) + GSH
Insulin-(SH)2 + GSSG
show the reaction diagram
integrin alphaIIbbeta3
?
show the reaction diagram
-
-
-
-
?
integrin alphaMb2
?
show the reaction diagram
-
-
-
-
?
integrin alphaVb3
?
show the reaction diagram
-
-
-
-
?
integrin alphaVbeta3
?
show the reaction diagram
-
-
-
-
?
integrin subunit alpha11
?
show the reaction diagram
-
the enzyme activates integrin subunit alpha11
-
-
?
integrin subunit beta1
?
show the reaction diagram
-
the enzyme activates integrin subunit beta1
-
-
?
protein-(SSG)2n
protein(SS)n + n(GSSG)
show the reaction diagram
-
-
-
-
?
Proteins
?
show the reaction diagram
tissue factor
?
show the reaction diagram
transforming growth factor-beta1
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
glutathione
thioredoxin
-
the enzymes PDI, P5, ERp72, ERp46 and ERp18 contains a thioredoxin binding site and the CGHC active site
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ag+
-
PDI binds Ag+
Cu+
-
the enzyme can bind 10 Cu+/mol and form a tetramer
Cu2+
-
PDI binds a maximum of 4 mol Cu2+ and is able to reduce it to Cu+, the bound Cu+ is surface-exposed
Mn2+
-
modulates the thiol isomerase activity of protein disulfide isomerase that is bound to integrin alphaVbeta3 and induces its transition to the ligand-competent state
Zn2+
-
Zn2+ induces dimers/oligomers with decreased isomerase activity
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
12-O-Tetradecanoylphorbol 13-acetate
-
binds to and moderately inhibits PDI
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
3,3',5-triiodo-L-thyronine
3,3',5-triiodothyronine
-
-
3,4-dichlorophenol
-
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
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
anti-PDI Fab fragments
-
-
-
bacitracin
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
CCF642
-
-
-
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
Estrogens
-
-
-
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
iodoacetamide
kanamycin
-
analysis of binding and dissociation constants with PDI and PDI domain deletion mutants
LOC14
-
-
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
N-ethylmaleimide
-
abolishes PDI oxidoreductase but not chaperone activity
neomycin
-
analysis of binding and dissociation constants with PDI and PDI domain deletion mutants
paromomycin
-
analysis of binding and dissociation constants with PDI and PDI domain deletion mutants
Pentachlorophenol
-
inhibits PDI 3,3',5-triiodo-L-thyronine binding activity
phenyl vinyl sulfonate
-
-
Phenylarsine oxide
-
complete inhibition at 0.01-0.1 mM in vivo
quercetin 3-rutinoside
-
-
quercetin-3-rutinoside
-
-
ribostamycin
-
analysis of binding and dissociation constants with PDI and PDI domain deletion mutants
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
Somatostatin
-
streptomycin
-
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
tetrachlorobisphenyl A
-
TCBPA, inhibits PDI 3,3',5-triiodo-L-thyronine binding activity
thionitrobenzoic acid
molecular docking simulation into the redox-active site, residues C37, G38, H39, C40. Inhibitor binds to hydrophobic amino acidsA34, W36, C37, C40, H39, T68 and F80. The redox inhibitory conformations are energetically and statistically favored
Vancomycin
-
analysis of binding and dissociation constants with PDI and PDI domain deletion mutants
vincristine
-
inhibits chaperone activity but not isomerase activity of both isoforms PDI and P5 in vitro. A 100:1 molar ratio of vincristine to enzyme is sufficient to almost completely inhibit chaperone activity
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
calnexin
interacts with the enzyme via the b and b' domains, binding site and structure, overview
-
DTT
-
absolutely required for activity
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.028 - 0.063
RNase
-
0.007 - 0.05
RNAse A
-
additional information
additional information
-
light scattering and fluorescence measurement kinetics of wild-type PDI and mutant abb'a' lacking the C-terminal domain c, overview
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000028 - 0.0011
RNase
-
0.017
sRNase
-
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4
-
assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.5 - 7.5
-
approx. 50% of maximal activity at pH 5.5, approx. 75% of maximal activity at pH 7.5
5 - 7
-
approx. 50% of maximal activity at pH 5.5, approx. 80% of maximal activity at pH 7.0, oxidation of NRCSQGSCWN
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
cell surface
Manually annotated by BRENDA team
expression of ERp27
Manually annotated by BRENDA team
TXNDC5 is highly expressed in patient-derived lung cancer specimens, immunohistochemic analysis
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
expression of ERp27
Manually annotated by BRENDA team
expression of ERp27
Manually annotated by BRENDA team
-
SV40 transformed, cultured, confluent, weak activity
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
in endothelial cells. On activation of endothelial cells, PDI remains confined to the intracellular stores of the dense tubular system and is neither released nor targeted to the cell surface
-
Manually annotated by BRENDA team
additional information
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PDIA3_HUMAN
505
0
56782
Swiss-Prot
Secretory Pathway (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
116000
gel filtration, the C-terminal fragment comprising residues 441-491 contributes to the anomalous molecular mass determination by gel filtration
17770
-
MALDI mass spectrometry
27700
x * 27700, ERp27, SDS-PAGE
54000
-
x * 54000, ERP-57
55000
-
x * 55000, SDS-PAGE
56300
-
1 * 56300, calculated from amino acid sequence
57000
-
x * 57000, SDS-PAGE, immunoprecipitation
57700
-
1 * 57700, analytical ultracentrifugation
58000
61200
-
x * 61200, SDS-PAGE under reducing conditions
62000
-
x * 62000, SDS-PAGE
64000
1 * 64000, analytical ultracentrifugation
69000
light scattering
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
acetylation
acetylation of the active site-flanking lysine residues can act to reversibly modulate enzyme activity
glutathionylation
-
-
glycoprotein
-
O-linked N-acetyl-D-glucosamine
nitrosylation
-
S-nitrosylation
no glycoprotein
-
-
phosphoprotein
-
-
proteolytic modification
-
-
S-nitrosylation
additional information
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ERp57 and its isolated bb' and b' domains in complex with the lectin chaperone calnexin, hanging drop vapour diffusion method, equilibration of 14 mg/ml protein in 50 mM Tris-HCl, 0.15 M NaCl, 1 mM DTT, pH 7.5, against 30% w/v PEG 3350, 0.1 M (NH4)2SO4, 0.1 M HEPES buffer, pH 7.5, for 1-3 days at 20°C, X-ray diffraction structure determination and analysis at 2.0 A resoution
hanging drop vapor diffusion method, using 0.01 M zinc chloride, 20% (w/v) polyethylene glycol 6000, and 0.1 M Tris-HCl (pH 8.0)
hanging drop vapor diffusion method, using 0.2 M ammonium sulfate, 0.1 M bis-Tris pH 5.5, 25% (w/v) PEG 3350
hanging-drop vapour-diffusion, mixing of 0.003 ml protein solution i.e. 15 mg/ml protein, 25 mM HEPES, pH 7.5 with 0.003 mL reservoir solution containing 20-23% polyethylene glycol 5000, 200 mM ammonium acetate, 100 mM HEPES, pH 7.5 and 5% glycerol
-
molecular modeling offers a role for the conserved residue R103 in coordinating the oxidative transition-state complex
small angle X-ray scattering analysis of purified recombinant wild-type and deletion mutant PDIs, structure modeling, the enzyme forms an approximately flat elliptical cylinder
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K274A
site-directed mutagenesis, the mutant shows affected interaction with calnexin
K332A
site-directed mutagenesis, the mutant shows binding affinity with calnexin identical to wild-type enzyme
R282A
site-directed mutagenesis, the mutant shows affected interaction with calnexin
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
F449R
F449W
F449Y
F452R
115% of wild-type 4-hydroxylase activity
F454A
-
binds DELTA-somatostatin like wild-type
G448R
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
I272A
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
K326E
the mutant shows 56% of wild type activity
K326E/E431K
the mutant shows 82.2% of wild type activity
K401Q
the mutant shows about 1.5fold less activity than the wild type enzyme
K450A
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
L453E
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
R444A
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
additional information
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
PDI active site can be reduced by glutathion
-
652503
PDI can be reduced by dithiothreitol
-
650995
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
from platelet
-
glutathione Sepharose column chromatography
-
glutathione-Sepharose bead chromatography and gel filtration
glutathione-Sepharose resin column chromatography and gel filtration
Ni Sepharose column chromatography
-
Ni-affinity resin column chromatography, and Superdex 200 gel filtration
Ni-Sepharose column chromatography and Resource Q column chromatography
-
purification from outdated platelets
-
purification of the a domain and the a' domain, expressed in Escherichia coli
-
purification of the structural domains and domain combinations expressed in Escherichia coli
-
purified from a fibronectin and fibrinogen-rich byproduct of factor VIII production
-
recombinant b domain of PDI
-
recombinant enzyme
-
recombinant GST-tagged bb' fragment and b' fragment from Escherichia coli strain Bl21(DE3) by glutathione affinity chromatography and gel filtration
recombinant His-tagged enzyme from Escherichia coli strain AD494(DE3) by nickel affinity chromatography
-
recombinant His-tagged wild-type and mutant PDIs from Escherichia coli strain M15 by nickel affinity and cation exchange chromatography
recombinant His-tagged wild-type and mutant proteins from Escherichia coli strain BL21(DE3) by nickel affinity and anion exchange chromatography
recombinant His-tagged wild-type PDI and mutant abb'a' from Escherichia coli strain BL21(DE3) by nickel affinity and anion exchange chromatography
-
recombinant PDI
recombinant PDI expressed in Escherichia coli
-
recombinant wild-type and mutant enzymes from Escherichia coli
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of GST-fusion full-length ERp57 lacking the signal sequence, A24-L505, and the bb', P134-G376, and b', F241-G376, fragments in Escherichia coli strain BL21(DE3)
sequence comparison
baculovirus expression system
-
cloning of cDNA
-
cloning of the a and a' domain, expression in Escherichia coli
-
expressed in Escherichia coli
-
expressed in Escherichia coli BL21 (DE3) pLysS cells
-
expressed in Escherichia coli BL21(DE3) cells
expressed in H-1299 lung cancer cells
-
expression Escherichia coli
-
expression in COS-7 cell
-
expression in COS-7 cells
-
expression in Escherichia coli
-
expression in Escherichia coli and Sf9 insect cells
-
expression of enzyme form PDIp in Escherichia coli
-
expression of GST-tagged bb' fragment, residues P135-S357, and of b' fragment, residues L236-S357, in Escherichia coli strain Bl21(DE3)
expression of His-tagged enzyme in Escherichia coli strain AD494(DE3)
-
expression of His-tagged wild-type and mutant PDIs in Escherichia coli strain M15
expression of His-tagged wild-type PDI and mutant abb'a' lacking the C-terminal domain c in Escherichia coli strain BL21(DE3)
-
expression of myc-tagged mutant PDI in HeLa cells
-
expression of PDI b domain in Escherichia coli
-
expression of protein disulfide isomerase a domain in Escherichia coli
expression of the domains and domain combinations in Escherichia coli
-
expression of wild-type and mutant ERP-57 in COS-7 cells, co-expression with wild-type and mutant receptors, broken disulfide bond bridge mutant hGnRH receptors and calnexin, interaction analysis, overview
-
expression Sf9 insect cells
functional complementation of an enzyme-deficient PDI-2-mutant strain of Caenorhabditis elegans, overview
-
gene TXNDC5, recombinant expression of Myc-tagged wild-type and mutant TXNDC5s in HEK-293T cells, pull-down assay with recombinant, co-expressed FLAG-tagged Srx
PDI, expression of substrate-trapping mutants of PDI family members ERp46, ERp18, ERp57, ERp72, and P5 in HT-1080 cells, the mutant enzymes form mixed disulfides
-
PDI, quantitative expression analysis, overexpression in CHO cells
-
protein disulfide isomerase and the beta-subunit of prolyl 4-hydroxylase, EC 1.14.11.2, are products of the same gene
-
recombinant constitutive overexpression in Mus musculus NSC-34 cells and neuroblastoma Neuro2a cells. PDI overexpression decreases mutant SOD1-induced cell death, overview
-
recombinant expression of wild-type and mutant enzymes in Escherichia coli. Recombinant PDIp protects the Escherichia coli cells against heat shock and oxidative stress-induced cell death independently of its enzymatic activity
sequence comparison
the gene encoding ERp27 is located at 14,958,241–14,982,750 bp on chromosome 12 and has 7 exons, DNA and amino acid sequence determination and anaylsis, sequence comparison, expression of GFP-fusion ERp27 in COS-7 cell endoplasmic reticulum, expression of N-terminally His-tagged wild-type and mutant ERp57, and of PDI a, b, and b' domains, in Escherichia coli strain BL21(DE3)
transfection of EA.hy926 cells
-
wild-type and/or mutant PDI overexpression in vascular smooth muscle cells and in HEK-293T cells
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
PDI is induced by unfolded protein response, UPR, signaling transduction pathways activated by protein misfolding in the endoplasmic reticulum, overview. PDI is upregulated before symptom onset in spinal cords of ALS postmortem tissue
-
protein disulfide isomerase is up-regulated during the unfolded protein response in acute myeloid leukemia. PDI is up-regulated in U-937 cells after induction of endoplasmic reticulum stress
-
the enzyme is induced during endoplasmic reticulum stress. The enzyme levels are markedly increased in Alzheimer's disease, Parkinson's disease, amyotropic lateral sclerosis and other neurodegenerative diseases
-
the enzyme is upregulated in amyotrophic lateral sclerosis
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
-
development of a method to determine quantitatively the redox state of active-site cysteines found in the Cys-Xaa-Xaa-Cys motif in living cells. Method is based on the alkylation of cysteines by methoxy polyethylene glycol 5000 maleimide. In vivo, protein disulfide isomerase is present in two semi-oxidized forms in which either the first active site in the a domain or the second active site in the a' domain is oxidized. In HEK-293 cells, about 50% of enzyme is fully reduced, in 18% a domain is oxidized, a' reduced, in 15%, the a domain is reduced, a' oxidized, and 16% of enzyme are fully oxidized
diagnostics
medicine
pharmacology
-
protein disulfide isomerase is a potential therapeutic target in amyotrophic lateral sclerosis and (+-)-trans-1,2-bis(mercaptoacetamido)cyclohexane and other molecular mimics of protein disulfide isomerase could be of benefit in amyotrophic lateral sclerosis and other neurodegenerative diseases related to protein misfolding
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Darby, N.J.; Creighton, T.E.
Functional properties of the individual thioredoxin-like domains of protein disulfide isomerase
Biochemistry
34
11725-11735
1995
Homo sapiens
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Chen, K.; Detwiler, T.C.; Essex, D.W.
Characterization of protein disulfide isomerase released from activated platelets
Br. J. Haematol.
90
425-431
1995
Homo sapiens
Manually annotated by BRENDA team
Bourdi, M.; Demady, D.; Martin, J.L.; Jabbour, S.K.; Martin, B.M.; George, J.W.; Pohl, L.R.
cDNA cloning and baculovirus expression of the human liver endoplasmic reticulum P58: characterization as a protein disulfide isomerase isoform, but not as a protease or a carnitine acyltransferase
Arch. Biochem. Biophys.
323
397-403
1995
Homo sapiens
Manually annotated by BRENDA team
Darby, N.J.; Kemmink, J.; Creighton, T.E.
Identifying and characterizing a structural domain of protein disulfide isomerase
Biochemistry
35
10517-10528
1996
Homo sapiens
Manually annotated by BRENDA team
Desilva, M.G.; Lu, J.; Donadel, G.; Modi, W.S.; Xie, H.; Notkins, A.L.; Lan, M.S.
Characterization and chromosomal localization of a new protein disulfide isomerase, PDIp, highly expressed in human pancreas
DNA Cell Biol.
15
9-16
1996
Homo sapiens
Manually annotated by BRENDA team
Myllyl, R.; Koivu, J.; Pihlajaniemi, T.; Kivirikko, K.I.
Protein disulphide-isomerase activity in various cells synthesizing collagen
Eur. J. Biochem.
134
7-11
1983
Gallus gallus, Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Tasanen, K.; Parkkonen, T.; Chow, L.T.; Kivirikko, K.I.; Pihlajaniemi, T.
Characterization of the human gene for a polypeptide that acts both as the beta subunit of prolyl 4-hydroxylase and as protein disulfide isomerase
J. Biol. Chem.
263
16218-16224
1988
Homo sapiens
Manually annotated by BRENDA team
Guthapfel, R.; Gueguen, P.; Quemeneur, E.
Reexamination of hormone-binding properties of protein disulfide-isomerase
Eur. J. Biochem.
242
315-319
1996
Homo sapiens
Manually annotated by BRENDA team
Tsibris, J.C.M.; Hunt, L.T.; Ballejo, G.; Barker, W.C.; Toney, L.J.; Spellacy, W.N.
Selective inhibition of protein disulfide isomerase by estrogens
J. Biol. Chem.
264
13967-13970
1989
Homo sapiens
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Kivirikko, K.I.; Myllyl, R.
Recent developments in posttranslational modification: intracellular processing
Methods Enzymol.
144
96-114
1987
Gallus gallus, Homo sapiens
Manually annotated by BRENDA team
Wang, X.Q.; Gui, L.L.; Dai, Y.; Wang, C.C.; Chang, W.R.; Liang, D.C.
Purification, crystallization and preliminary crystallographic studies on the N-terminal fragment of human protein disulfide isomerase
Acta Crystallogr. Sect. D
55
1958-1960
1999
Homo sapiens
Manually annotated by BRENDA team
Milev, Y.; Essex, D.W.
Protein disulfide isomerase catalyzes the formation of disulfide-linked complexes of thrombospondin-1 with thrombin-antithrombin III
Arch. Biochem. Biophys.
361
120-126
1999
Homo sapiens
Manually annotated by BRENDA team
Narindrasorasak, S.; Yao, P.; Sarkar, B.
Protein disulfide isomerase, a multifunctional protein chaperone, shows copper-binding activity
Biochem. Biophys. Res. Commun.
311
405-414
2003
Homo sapiens
Manually annotated by BRENDA team
Essex, D.W.; Miller, A.; Swiatkowska, M.; Feinman, R.D.
Protein disulfide isomerase catalyzes the formation of disulfide-linked complexes of vitronectin with thrombin-antithrombin
Biochemistry
38
10398-10405
1999
Homo sapiens
Manually annotated by BRENDA team
Essex, D.W.; Li, M.; Miller, A.; Feinman, R.D.
Protein disulfide isomerase and sulfhydryl-dependent pathways in platelet activation
Biochemistry
40
6070-6075
2001
Homo sapiens
Manually annotated by BRENDA team
Sun, X.X.; Dai, Y.; Liu, H.P.; Chen, S.M.; Wang, C.C.
Contributions of protein disulfide isomerase domains to its chaperone activity
Biochim. Biophys. Acta
1481
45-54
2000
Homo sapiens
Manually annotated by BRENDA team
Mayumi, S.; Azuma, A.; Kobayashi, H.; Sodeoka, M.; Yano, K.; Sugimoto, S.; Endo, Y.; Hashimoto, Y.
Identification of protein disulfide isomerase as a phorbol ester-binding protein
Biol. Pharm. Bull.
23
1111-1113
2000
Homo sapiens
Manually annotated by BRENDA team
Koivunen, P.; Pirneskoski, A.; Karvonen, P.; Ljung, J.; Helaakoski, T.; Notbohm, H.; Kivirikko, K.I.
The acidic C-terminal domain of protein disulfide isomerase is not critical for the enzyme subunit function or for the chaperone or disulfide isomerase activities of the polypeptide
EMBO J.
18
65-74
1999
Homo sapiens (P07237)
Manually annotated by BRENDA team
Lumb, R.A.; Bulleid, N.J.
Is protein disulfide isomerase a redox-dependent molecular chaperone?
EMBO J.
21
6763-6770
2002
Homo sapiens
Manually annotated by BRENDA team
Darby, N.J.; van Straaten, M.; Penka, E.; Vincentelli, R.; Kemmink, J.
Identifying and characterizing a second structural domain of protein disulfide isomerase
FEBS Lett.
448
167-172
1999
Homo sapiens
Manually annotated by BRENDA team
Markus, M.; Benezra, R.
Two isoforms of protein disulfide isomerase alter the dimerization status of E2A proteins by a redox mechanism
J. Biol. Chem.
274
1040-1049
1999
Homo sapiens
Manually annotated by BRENDA team
Lucero, H.A.; Kaminer, B.
The role of calcium on the activity of ERcalcistorin/protein-disulfide isomerase and the significance of the C-terminal and its calcium binding. A comparison with mammalian protein-disulfide isomerase
J. Biol. Chem.
274
3243-3251
1999
Oryctolagus cuniculus, Homo sapiens, Echinoidea
Manually annotated by BRENDA team
Langenbach, K.J.; Sottile, J.
Identification of protein-disulfide isomerase activity in fibronectin
J. Biol. Chem.
274
7032-7038
1999
Homo sapiens
Manually annotated by BRENDA team
Klappa, P.; Koivunen, P.; Pirneskoski, A.; Karvonen, P.; Ruddock, L.W.; Kivirikko, K.I.; Freedman, R.B.
Mutations that destabilize the a' domain of human protein-disulfide isomerase indirectly affect peptide binding
J. Biol. Chem.
275
13213-13218
2000
Homo sapiens
Manually annotated by BRENDA team
Winter, J.; Klappa, P.; Freedman, R.B.; Lilie, H.; Rudolph, R.
Catalytic activity and chaperone function of human protein-disulfide isomerase are required for the efficient refolding of proinsulin
J. Biol. Chem.
277
310-317
2002
Homo sapiens
Manually annotated by BRENDA team
Alanen, H.I.; Williamson, R.A.; Howard, M.J.; Lappi, A.K.; Jaentti, H.P.; Rautio, S.M.; Kellokumpu, S.; Ruddock, L.W.
Functional characterization of ERp18, a new endoplasmic reticulum-located thioredoxin superfamily member
J. Biol. Chem.
278
28912-28920
2003
Homo sapiens
Manually annotated by BRENDA team
Barbouche, R.; Miquelis, R.; Jones, I.M.; Fenouillet, E.
Protein-disulfide isomerase-mediated reduction of two disulfide bonds of HIV envelope glycoprotein 120 occurs post-CXCR4 binding and is required for fusion
J. Biol. Chem.
278
3131-3136
2003
Homo sapiens
Manually annotated by BRENDA team
Schwaller, M.; Wilkinson, B.; Gilbert, H.F.
Reduction-reoxidation cycles contribute to catalysis of disulfide isomerization by protein-disulfide isomerase
J. Biol. Chem.
278
7154-7159
2003
Homo sapiens
Manually annotated by BRENDA team
Pirneskoski, A.; Klappa, P.; Lobell, M.; Williamson, R.A.; Byrne, L.; Alanen, H.I.; Salo, K.E.; Kivirikko, K.I.; Freedman, R.B.; Ruddock, L.W.
Molecular characterization of the principal substrate binding site of the ubiquitous folding catalyst protein disulfide isomerase
J. Biol. Chem.
279
10374-10381
2004
Homo sapiens
Manually annotated by BRENDA team
Kemmink, J.; Dijkstra, K.; Mariani, M.; Scheek, R.M.; Penka, E.; Nilges, M.; Darby, N.J.
The structure in solution of the b domain of protein disulfide isomerase
J. Biomol. NMR
13
357-368
1999
Homo sapiens
Manually annotated by BRENDA team
VanderWaal, R.P.; Spitz, D.R.; Griffith, C.L.; Higashikubo, R.; Roti Roti, J.L.
Evidence that protein disulfide isomerase (PDI) is involved in DNA-nuclear matrix anchoring
J. Cell. Biochem.
85
689-702
2002
Homo sapiens
Manually annotated by BRENDA team
Lappi, A.K.; Lensink, M.F.; Alanen, H.I.; Salo, K.E.H.; Lobell, M.; Juffer, A.H.; Ruddock, L.W.
A conserved arginine plays a role in the catalytic cycle of the protein disulphide isomerases
J. Mol. Biol.
335
283-295
2003
Homo sapiens
Manually annotated by BRENDA team
Ruoppolo, M.; Orru, S.; Talamo, F.; Ljung, J.; Pirneskoski, A.; Kivirikko, K.I.; Marino, G.; Koivunen, P.
Mutations in domain a' of protein disulfide isomerase affect the folding pathway of bovine pancreatic ribonuclease A
Protein Sci.
12
939-952
2003
Ovis aries, Homo sapiens
Manually annotated by BRENDA team
Kimura, T.; Hosoda, Y.; Kitamura, Y.; Nakamura, H.; Horibe, T.; Kikuchi, M.
Functional differences between human and yeast protein disulfide isomerase family proteins
Biochem. Biophys. Res. Commun.
320
359-365
2004
Saccharomyces cerevisiae, Homo sapiens, Saccharomyces cerevisiae trg1/TRG1
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Tian, R.; Li, S.J.; Wang, D.L.; Zhao, Z.; Liu, Y.; He, R.Q.
The acidic C-terminal domain stabilizes the chaperone function of protein disulfide isomerase
J. Biol. Chem.
279
48830-48835
2004
Homo sapiens
Manually annotated by BRENDA team
Zhao, T.J.; Ou, W.B.; Xie, Q.; Liu, Y.; Yan, Y.B.; Zhou, H.M.
Catalysis of creatine kinase refolding by protein disulfide isomerase involves disulfide cross-link and dimer to tetramer switch
J. Biol. Chem.
280
13470-13476
2005
Homo sapiens
Manually annotated by BRENDA team
Li, S.J.; Hong, X.G.; Shi, Y.Y.; Li, H.; Wang, C.C.
Annular arrangement and collaborative actions of four domains of protein disulfide isomerase - A small angle X-ray scattering study in solution
J. Biol. Chem.
281
6581-6588
2005
Homo sapiens (P07237)
Manually annotated by BRENDA team
Maattanen, P.; Kozlov, G.; Gehring, K.; Thomas, D.Y.
ERp57 and PDI: multifunctional protein disulfide isomerases with similar domain architectures but differing substrate-partner associations
Biochem. Cell Biol.
84
881-889
2006
Homo sapiens (P07237), Homo sapiens (P13667), Homo sapiens (P30101), Homo sapiens (Q13087)
Manually annotated by BRENDA team
Bell, S.E.; Shah, C.M.; Gordge, M.P.
Protein disulfide-isomerase mediates delivery of nitric oxide redox derivatives into platelets
Biochem. J.
403
283-288
2007
Homo sapiens
Manually annotated by BRENDA team
Winter, A.D.; McCormack, G.; Page, A.P.
Protein disulfide isomerase activity is essential for viability and extracellular matrix formation in the nematode Caenorhabditis elegans
Dev. Biol.
308
449-461
2007
Caenorhabditis elegans, Homo sapiens
Manually annotated by BRENDA team
Alanen, H.I.; Williamson, R.A.; Howard, M.J.; Hatahet, F.S.; Salo, K.E.; Kauppila, A.; Kellokumpu, S.; Ruddock, L.W.
ERp27, a new non-catalytic endoplasmic reticulum-located human protein disulfide isomerase family member, interacts with ERp57
J. Biol. Chem.
281
33727-33738
2006
Homo sapiens (Q96DN0), Homo sapiens
Manually annotated by BRENDA team
Versteeg, H.H.; Ruf, W.
Tissue factor coagulant function is enhanced by protein-disulfide isomerase independent of oxidoreductase activity
J. Biol. Chem.
282
25416-25424
2007
Homo sapiens
Manually annotated by BRENDA team
Schultz-Norton, J.R.; McDonald, W.H.; Yates, J.R.; Nardulli, A.M.
Protein disulfide isomerase serves as a molecular chaperone to maintain estrogen receptor alpha structure and function
Mol. Endocrinol.
20
1982-1995
2006
Homo sapiens
Manually annotated by BRENDA team
Kozlov, G.; Maattanen, P.; Schrag, J.D.; Pollock, S.; Cygler, M.; Nagar, B.; Thomas, D.Y.; Gehring, K.
Crystal structure of the bb domains of the protein disulfide isomerase ERp57
Structure
14
1331-1339
2006
Homo sapiens (P30101)
Manually annotated by BRENDA team
Gruber, C.W.; Cemazar, M.; Heras, B.; Martin, J.L.; Craik, D.J.
Protein disulfide isomerase: the structure of oxidative folding
Trends Biochem. Sci.
31
455-464
2006
Arabidopsis thaliana, Chlamydomonas reinhardtii, Escherichia coli, Homo sapiens (P07237), Saccharomyces cerevisiae (P17967), Saccharomyces cerevisiae
Manually annotated by BRENDA team
Appenzeller-Herzog, C.; Ellgaard, L.
In vivo reduction-oxidation state of protein disulfide isomerase: the two active sites independently occur in the reduced and oxidized forms
Antioxid. Redox Signal.
10
55-64
2008
Homo sapiens
Manually annotated by BRENDA team
Fu, X.; Zhu, B.T.
Human pancreas-specific protein disulfide isomerase homolog (PDIp) is redox-regulated through formation of an inter-subunit disulfide bond
Arch. Biochem. Biophys.
485
1-9
2009
Homo sapiens
Manually annotated by BRENDA team
Rancy, P.C.; Thorpe, C.
Oxidative protein folding in vitro: a study of the cooperation between quiescin-sulfhydryl oxidase and protein disulfide isomerase
Biochemistry
47
12047-12056
2008
Homo sapiens
Manually annotated by BRENDA team
Raturi, A.; Miersch, S.; Hudson, J.W.; Mutus, B.
Platelet microparticle-associated protein disulfide isomerase promotes platelet aggregation and inactivates insulin
Biochim. Biophys. Acta
1778
2790-2796
2008
Homo sapiens
Manually annotated by BRENDA team
Gowthaman, U.; Jayakanthan, M.; Sundar, D.
Molecular docking studies of dithionitrobenzoic acid and its related compounds to protein disulfide isomerase: computational screening of inhibitors to HIV-1 entry
BMC Bioinformatics
9 Suppl 12
S14
2008
Homo sapiens (P07237), Homo sapiens
Manually annotated by BRENDA team
Manickam, N.; Sun, X.; Li, M.; Gazitt, Y.; Essex, D.W.
Protein disulphide isomerase in platelet function
Br. J. Haematol.
140
223-229
2008
Homo sapiens
Manually annotated by BRENDA team
Lovat, P.E.; Corazzari, M.; Armstrong, J.L.; Martin, S.; Pagliarini, V.; Hill, D.; Brown, A.M.; Piacentini, M.; Birch-Machin, M.A.; Redfern, C.P.
Increasing melanoma cell death using inhibitors of protein disulfide isomerases to abrogate survival responses to endoplasmic reticulum stress
Cancer Res.
68
5363-5369
2008
Homo sapiens
Manually annotated by BRENDA team
Hernandez, G.; Anderson, J.S.; LeMaster, D.M.
Electrostatic stabilization and general base catalysis in the active site of the human protein disulfide isomerase a domain monitored by hydrogen exchange
ChemBioChem
9
768-778
2008
Homo sapiens (P07237), Homo sapiens
Manually annotated by BRENDA team
Swiatkowska, M.; Szymanski, J.; Padula, G.; Cierniewski, C.S.
Interaction and functional association of protein disulfide isomerase with alphaVbeta3 integrin on endothelial cells
FEBS J.
275
1813-1823
2008
Homo sapiens
Manually annotated by BRENDA team
Wang, L.; Li, S.J.; Sidhu, A.; Zhu, L.; Liang, Y.; Freedman, R.B.; Wang, C.C.
Reconstitution of human Ero1-Lalpha/protein-disulfide isomerase oxidative folding pathway in vitro: position-dependent difference in role between the a and a' domains of protein disulfide isomerase
J. Biol. Chem.
284
199-206
2009
Homo sapiens
Manually annotated by BRENDA team
Reinhardt, C.; von Bruehl, M.L.; Manukyan, D.; Grahl, L.; Lorenz, M.; Altmann, B.; Dlugai, S.; Hess, S.; Konrad, I.; Orschiedt, L.; Mackman, N.; Ruddock, L.; Massberg, S.; Engelmann, B.
Protein disulfide isomerase acts as an injury response signal that enhances fibrin generation via tissue factor activation
J. Clin. Invest.
118
1110-1122
2008
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Fu, X.; Wang, P.; Zhu, B.T.
Protein disulfide isomerase is a multifunctional regulator of estrogenic status in target cells
J. Steroid Biochem. Mol. Biol.
112
127-137
2008
Homo sapiens
Manually annotated by BRENDA team
Jain, S.; McGinnes, L.W.; Morrison, T.G.
Overexpression of thiol/disulfide isomerases enhances membrane fusion directed by the Newcastle disease virus fusion protein
J. Virol.
82
12039-12048
2008
Homo sapiens
Manually annotated by BRENDA team
Horibe, T.; Kikuchi, M.; Kawakami, K.
Interaction of human protein disulfide isomerase and human P5 with drug compounds: Analysis using biosensor technology
Process Biochem.
43
1330-1337
2008
Homo sapiens
-
Manually annotated by BRENDA team
Persson, E.
Protein disulfide isomerase has no stimulatory chaperone effect on factor X activation by factor VIIa-soluble tissue factor
Thromb. Res.
123
171-176
2008
Bos taurus, Homo sapiens
Manually annotated by BRENDA team
Tian, F.; Zhou, X.; Wikstroem, J.; Karlsson, H.; Sjoeland, H.; Gan, L.M.; Boren, J.; Akyuerek, L.M.
Protein disulfide isomerase increases in myocardial endothelial cells in mice exposed to chronic hypoxia: a stimulatory role in angiogenesis
Am. J. Physiol. Heart Circ. Physiol.
297
H1078-H1086
2009
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Fernandes, D.C.; Manoel, A.H.; Wosniak, J.; Laurindo, F.R.
Protein disulfide isomerase overexpression in vascular smooth muscle cells induces spontaneous preemptive NADPH oxidase activation and Nox1 mRNA expression: effects of nitrosothiol exposure
Arch. Biochem. Biophys.
484
197-204
2009
Homo sapiens
Manually annotated by BRENDA team
Fu, X.M.; Zhu, B.T.
Human pancreas-specific protein disulfide isomerase (PDIp) can function as a chaperone independently of its enzymatic activity by forming stable complexes with denatured substrate proteins
Biochem. J.
429
157-169
2010
Homo sapiens (Q13087), Homo sapiens
Manually annotated by BRENDA team
Hayes, N.V.; Smales, C.M.; Klappa, P.
Protein disulfide isomerase does not control recombinant IgG4 productivity in mammalian cell lines
Biotechnol. Bioeng.
105
770-779
2010
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
van Nispen Tot Pannerden, H.E.; van Dijk, S.M.; Du, V.; Heijnen, H.F.
Platelet protein disulfide isomerase is localized in the dense tubular system and does not become surface expressed after activation
Blood
114
4738-4740
2009
Homo sapiens
Manually annotated by BRENDA team
Walker, A.K.; Farg, M.A.; Bye, C.R.; McLean, C.A.; Horne, M.K.; Atkin, J.D.
Protein disulphide isomerase protects against protein aggregation and is S-nitrosylated in amyotrophic lateral sclerosis
Brain
133
105-116
2010
Homo sapiens
Manually annotated by BRENDA team
Ayala Yanez, R.; Conn, P.M.
Protein disulfide isomerase chaperone ERP-57 decreases plasma membrane expression of the human GnRH receptor
Cell Biochem. Funct.
28
66-73
2010
Homo sapiens
Manually annotated by BRENDA team
Lee, S.O.; Cho, K.; Cho, S.; Kim, I.; Oh, C.; Ahn, K.
Protein disulphide isomerase is required for signal peptide peptidase-mediated protein degradation
EMBO J.
29
363-375
2010
Homo sapiens
Manually annotated by BRENDA team
Denisov, A.Y.; Maeaettaenen, P.; Dabrowski, C.; Kozlov, G.; Thomas, D.Y.; Gehring, K.
Solution structure of the bb domains of human protein disulfide isomerase
FEBS J.
276
1440-1449
2009
Homo sapiens (P07237), Homo sapiens
Manually annotated by BRENDA team
Jessop, C.E.; Watkins, R.H.; Simmons, J.J.; Tasab, M.; Bulleid, N.J.
Protein disulphide isomerase family members show distinct substrate specificity: P5 is targeted to BiP client proteins
J. Cell Sci.
122
4287-4295
2009
Homo sapiens
Manually annotated by BRENDA team
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
-
Manually annotated by BRENDA team
Fu, X.M.; Dai, X.; Ding, J.; Zhu, B.T.
Pancreas-specific protein disulfide isomerase has a cell type-specific expression in various mouse tissues and is absent in human pancreatic adenocarcinoma cells: implications for its functions
J. Mol. Histol.
40
189-199
2009
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Abromaitis, S.; Stephens, R.S.
Attachment and entry of Chlamydia have distinct requirements for host protein disulfide isomerase
PLoS Pathog.
5
e1000357
2009
Cricetulus griseus, Homo sapiens
Manually annotated by BRENDA team
Popescu, N.I.; Lupu, C.; Lupu, F.
Extracellular protein disulfide isomerase regulates coagulation on endothelial cells through modulation of phosphatidylserine exposure
Blood
116
993-1001
2010
Homo sapiens
Manually annotated by BRENDA team
Haefliger, S.; Klebig, C.; Schaubitzer, K.; Schardt, J.; Timchenko, N.; Mueller, B.U.; Pabst, T.
Protein disulfide isomerase blocks CEBPA translation and is up-regulated during the unfolded protein response in AML
Blood
117
5931-5940
2011
Homo sapiens
Manually annotated by BRENDA team
Wang, C.; Chen, S.; Wang, X.; Wang, L.; Wallis, A.K.; Freedman, R.B.; Wang, C.C.
Plasticity of human protein disulfide isomerase: evidence for mobility around the X-linker region and its functional significance
J. Biol. Chem.
285
26788-26797
2010
Homo sapiens
Manually annotated by BRENDA team
Kozlov, G.; Azeroual, S.; Rosenauer, A.; Maeaettaenen, P.; Denisov, A.Y.; Thomas, D.Y.; Gehring, K.
Structure of the catalytic a0a fragment of the protein disulfide isomerase ERp72
J. Mol. Biol.
401
618-625
2010
Homo sapiens (P13667)
Manually annotated by BRENDA team
Lappi, A.K.; Ruddock, L.W.
Reexamination of the role of interplay between glutathione and protein disulfide isomerase
J. Mol. Biol.
409
238-249
2011
Homo sapiens
Manually annotated by BRENDA team
Gulerez, I.E.; Kozlov, G.; Rosenauer, A.; Gehring, K.
Structure of the third catalytic domain of the protein disulfide isomerase ERp46
Acta Crystallogr. Sect. F
68
378-381
2012
Homo sapiens (Q8NBS9)
Manually annotated by BRENDA team
Fu, X.; Wang, P.; Zhu, B.
Characterization of the estradiol-binding site structure of human pancreas-specific protein disulfide isomerase: Indispensable role of the hydrogen bond between His278 and the estradiol 3-hydroxyl group
Biochemistry
50
106-115
2011
Homo sapiens, Homo sapiens ATCC 6706839
Manually annotated by BRENDA team
Hahm, E.; Li, J.; Kim, K.; Huh, S.; Rogelj, S.; Cho, J.
Extracellular protein disulfide isomerase regulates ligand-binding activity of alphaMbeta2 integrin and neutrophil recruitment during vascular inflammation
Blood
121; 3789-800
S1-15
2013
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Laurindo, F.R.; Pescatore, L.A.; Fernandes, D.d.e..C.
Protein disulfide isomerase in redox cell signaling and homeostasis
Free Radic. Biol. Med.
52
1954-1969
2012
Homo sapiens
Manually annotated by BRENDA team
Jurk, K.; Lahav, J.; VAN Aken, H.; Brodde, M.F.; Nofer, J.R.; Kehrel, B.E.
Extracellular protein disulfide isomerase regulates feedback activation of platelet thrombin generation via modulation of coagulation factor binding
J. Thromb. Haemost.
9
2278-2290
2011
Homo sapiens
Manually annotated by BRENDA team
Xu, L.R.; Liu, X.L.; Chen, J.; Liang, Y.
Protein disulfide isomerase interacts with tau protein and inhibits its fibrillization
PLoS ONE
8
e76657
2013
Homo sapiens
Manually annotated by BRENDA team
Winter, J.; Gleiter, S.; Klappa, P.; Lilie, H.
Protein disulfide isomerase isomerizes non-native disulfide bonds in human proinsulin independent of its peptide-binding activity
Protein Sci.
20
588-596
2011
Homo sapiens
Manually annotated by BRENDA team
Bastos-Aristizabal, S.; Kozlov, G.; Gehring, K.
Structural insight into the dimerization of human protein disulfide isomerase
Protein Sci.
23
618-626
2014
Homo sapiens
Manually annotated by BRENDA team
Soares Moretti, A.I.; Martins Laurindo, F.R.
Protein disulfide isomerases Redox connections in and out of the endoplasmic reticulum
Arch. Biochem. Biophys.
617
106-119
2017
Homo sapiens
Manually annotated by BRENDA team
Popielarski, M.; Ponamarczuk, H.; Stasiak, M.; Michalec, L.; Bednarek, R.; Studzian, M.; Pulaski, L.; Swiatkowska, M.
The role of protein disulfide isomerase and thiol bonds modifications in activation of integrin subunit alpha11
Biochem. Biophys. Res. Commun.
495
1635-1641
2018
Homo sapiens
Manually annotated by BRENDA team
Freedman, R.B.; Desmond, J.L.; Byrne, L.J.; Heal, J.W.; Howard, M.J.; Sanghera, N.; Walker, K.L.; Wallis, A.K.; Wells, S.A.; Williamson, R.A.; Roemer, R.A.
Something in the way she moves The functional significance of flexibility in the multiple roles of protein disulfide isomerase (PDI)
Biochim. Biophys. Acta
1865
1383-1394
2017
Homo sapiens
Manually annotated by BRENDA team
Okumura, M.; Kadokura, H.; Inaba, K.
Structures and functions of protein disulfide isomerase family members involved in proteostasis in the endoplasmic reticulum
Free Radic. Biol. Med.
83
314-322
2015
Homo sapiens
Manually annotated by BRENDA team
Perri, E.R.; Thomas, C.J.; Parakh, S.; Spencer, D.M.; Atkin, J.D.
The unfolded protein response and the role of protein disulfide isomerase in neurodegeneration
Front. Cell Dev. Biol.
3
80
2015
Homo sapiens
Manually annotated by BRENDA team
Ali Khan, H.; Mutus, B.
Protein disulfide isomerase a multifunctional protein with multiple physiological roles
Front. Chem.
2
70
2014
Homo sapiens
Manually annotated by BRENDA team
Watanabe, M.M.; Laurindo, F.R.; Fernandes, D.C.
Methods of measuring protein disulfide isomerase activity a critical overview
Front. Chem.
2
73
2014
Homo sapiens
Manually annotated by BRENDA team
Caba, C.; Khan, H.; Auld, J.; Ushioda, R.; Araki, K.; Nagata, K.; Mutus, B.
Conserved residues Lys57 and Lys401 of protein disulfide isomerase maintain an active site conformation for optimal activity Implications for post-translational regulation
Front. Mol. Biosci.
5
18
2018
Homo sapiens (P07237)
Manually annotated by BRENDA team
Schulz, E.; Muenzel, T.
Lumen size matters role of protein disulfide isomerase A1 in vascular remodeling
Hypertension
67
488-489
2016
Homo sapiens
Manually annotated by BRENDA team
Yang, S.; Wang, X.; Cui, L.; Ding, X.; Niu, L.; Yang, F.; Wang, C.; Wang, C.C.; Lou, J.
Compact conformations of human protein disulfide isomerase
PLoS ONE
9
e103472
2014
Homo sapiens (P07237), Homo sapiens
Manually annotated by BRENDA team
Neves, R.P.P.; Fernandes, P.A.; Ramos, M.J.
Mechanistic insights on the reduction of glutathione disulfide by protein disulfide isomerase
Proc. Natl. Acad. Sci. USA
114
E4724-E4733
2017
Homo sapiens (P07237), Homo sapiens
Manually annotated by BRENDA team
Chawsheen, H.A.; Jiang, H.; Ying, Q.; Ding, N.; Thapa, P.; Wei, Q.
The redox regulator sulfiredoxin forms a complex with thioredoxin domain-containing 5 protein in response to ER stress in lung cancer cells
J. Biol. Chem.
294
8991-9006
2019
Homo sapiens (Q8NBS9), Homo sapiens
Manually annotated by BRENDA team