Any feedback?
Information on EC 5.3.4.1 - protein disulfide-isomerase and Organism(s) Rattus norvegicus and UniProt Accession P38659
for references in articles please use BRENDA:EC5.3.4.1Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
5.3.4.1 protein disulfide-isomeraseIUBMB Comments
Needs reducing agents or partly reduced enzyme; the reaction depends on sulfhydryl-disulfide interchange.
Specify your search results
Word Map
- 5.3.4.1
- collagen
- laminin
- integrins
- endothelial
- actin
- fibrosis
-
adhesive
-
basement
- mesenchymal
- vessel
- fiber
- metastasis
- proteoglycans
- vitronectin
- fibrinogen
- matrices
- nephropathy
- albumin
- gelatin
-
interstitial
-
mesangial
- platelet
- monolayer
- cytoskeleton
- glomerular
- rgd
- vimentin
- e-cadherin
-
cell-cell
- adhesions
- zeta
- myofibroblasts
- willebrand
-
epithelial-mesenchymal
- factor-beta
- fak
- fibrin
- metalloproteinases
-
preterm
-
dish
-
biomaterials
- procollagens
- heparan
-
alpha-smooth
- dermal
- tgf-beta
- plasminogen
-
fibrillar
- drug development
-
heparin-binding
- synthesis
- thrombospondin
- medicine
- industry
- diagnostics
- pharmacology
- biotechnology
- analysis
The taxonomic range for the selected organisms is: Rattus norvegicus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
fibronectin, pdi, protein disulfide isomerase, erp57, pdia3, protein disulphide isomerase, cabp1, erp44, disulfide isomerase, erp72, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
5'-MD
-
-
-
-
58 kDa glucose regulated protein
-
-
-
-
58 kDa microsomal protein
-
-
-
-
CaBP1
-
-
-
-
CaBP2
-
-
-
-
Cellular thyroid hormone binding protein
-
-
-
-
Disulfide interchange enzyme
-
-
-
-
Disulfide isomerase ER-60
-
-
-
-
DsbA
-
-
-
-
DsbC
-
-
-
-
DsbD
-
-
-
-
endoplasmic reticulum protein EUG1
-
-
-
-
ER58
-
-
-
-
ERp-72 homolog
-
-
-
-
ERp57
-
-
-
-
ERP59
-
-
-
-
ERP60
-
-
-
-
ERp72
-
-
-
-
HIP-70
-
-
-
-
Iodothyronine 5'-monodeiodinase
-
-
-
-
P55
-
-
-
-
P58
-
-
-
-
PDI
PDIp
-
-
-
-
protein disulfide isomerase
Protein disulfide isomerase P5
-
-
-
-
Protein disulfide isomerase-related protein
-
-
-
-
Protein disulphide isomerase
-
-
-
-
Protein ERp-72
-
-
-
-
R-cognin
-
-
-
-
Rearrangease
-
-
-
-
Reduced ribonuclease reactivating enzyme
-
-
-
-
Retina cognin
-
-
-
-
S-S rearrangase
-
-
-
-
Thyroid hormone-binding protein
-
-
-
-
Thyroxine deiodinase
-
-
-
-
PDI
-
-
-
-
PDI
-
-
protein disulfide isomerase
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
catalyses the rearrangement of -S-S- bonds in proteins
disulfide formation and isomerization mechanism by domains a and a', during transfer of oxidizing or reducing equivalents to substrates, the CXXC active site cycles between its oxidized, disulfide and reduced, thiol states
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
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
37318-49-3
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
apolipoprotein B100
?
-
the enzyme assists in the oxidative folding of apolipoprotein B100
-
-
?
lysozyme
aggregated lysozyme
-
PDI has antichaperone activity facilitating protein aggregation
-
?
reduced ribonuclease
?
-
refolding of reduced ribonuclease in presence of glutathione, isomerase activity of PDI
-
-
?
Proteins
?
-
proposed physiological role as catalyst of formation of native disulfide bonds in nascent and newly synthesized secretory 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
?
-
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
?
-
-
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
?
-
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
?
-
-
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'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
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
apolipoprotein B100
?
-
the enzyme assists in the oxidative folding of apolipoprotein B100
-
-
?
Proteins
?
-
proposed physiological role as catalyst of formation of native disulfide bonds in nascent and newly synthesized secretory proteins
-
-
?
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
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
Ca2+ and Mg2+ have no effect on the enzyme and do not influence Zn2+ effects
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1,1-bis(4-hydroxyphenyl)ethane
-
i.e.bisphenol E, 15% inhibition at 0.0125 mM
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
3,4-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
Diazobenzene sulfonic acid
-
considerably more effective after preincubation with DTT
N-Iodoacetyl-N'-(5-sulfo)-1-naphthyl-diaminoethane
-
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
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
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
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
PDI has a greater relative impact on isomerization reactions and consequently the structure-forming step in oxidative folding at pH 7, as opposed to pHs 8 and 9
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
activities in adult tissues are only 10-40% of those found in newborn
-
activities in adult tissues are only 10-40% of those found in newborn
-
activities in adult tissues are only 10-40% of those found in newborn
-
activities in adult tissues are only 10-40% of those found in newborn
-
activities in adult tissues are only 10-40% of those found in newborn
-
activities in adult tissues are only 10-40% of those found in newborn
-
activities in adult tissues are only 10-40% of those found in newborn
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
cullular enzyme distribution, immunohistochemic detection, overview
-
-
-
-
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
-
located on both sides of the membrane. The inside-located enzyme is immunochemically different from the outside-located enzyme
-
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
physiological function
physiological function
-
PDI is a key enzyme involved in formation of correct pattern of disulfide bonds in proteins. PDI also plays an important role in the hypothalamic-pituitary-thyroid axis, mechanism, overview
physiological function
-
PDI is an abundant enzyme that forms, breaks, and isomerizes disulfide bonds and is therefore an important cellular defense against protein misfolding. PDI can be protective against mutant SOD1 aggregation and toxicity
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PDIA4_RAT
643
0
72720
Swiss-Prot
Secretory Pathway (Reliability: 1)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
52000
-
2 * 55000, about, sequence calculation, 2 * 52000, analytical ultrafiltration
55000
58900
-
x * 58900, SDS-PAGE under reducing conditions, other bands with MW 53800 and 55200 represent proteolytic degradation products of the 58900 MW protein
additional information
-
Zn2+ induces formation of larger enzyme aggregates with MW up to 600 kDa and above
55000
-
2 * 55000, about, sequence calculation, 2 * 52000, analytical ultrafiltration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
-
2 * 55000, about, sequence calculation, 2 * 52000, analytical ultrafiltration
additional information
?
-
x * 58900, SDS-PAGE under reducing conditions, other bands with MW 53800 and 55200 represent proteolytic degradation products of the 58900 MW protein
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
-
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
-
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
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant b and b' domains and the bb' fragments of ERp57 and ERp72, hanging drop vapor diffusion method, 0.002 ml protein solution containing 10 mg/ml protein in 50 mM Tris-HCl, pH 7.5, 0.15 M NaCl, and 1 mM DTT, are mixed with 0.002 ml reservoir solution containing 18% w/v PEG MME 2000, 25% glycerol, and 0.1 M Tris, pH 8.0, suspended over 1 ml reservoir solution, 1-3 days, 20°C, X-ray diffraction structure determination and analysis at 1.9 A resolution, overview
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C294S/C325S
-
site-directed mutagenesis, exchange of the enzyme's cysteine residues involved in rearrangement of disulfide bonds by function in thiol/disulfide exchange
C55S/C379S
-
The double active site mutant Cys55Ser, Cys379Ser is not capable of catalyzing protein folding
G36A
-
Mutagenesis of Trp34 to Ser and Gly36 to Ala has little effect on activity. Mutagenesis of amino acid residues within the active site sequence, Trp34 to a Ser and Gly36 to an Ala has little effect on activity
L39R
-
Mutagenesis of Lys39 to an Arg results in only a modest loss of activity
W34S
-
Mutagenesis of Trp34 to Ser and Gly36 to Ala has little effect on activity. Mutagenesis of amino acid residues within the active site sequence, Trp34 to a Ser and Gly36 to an Ala has little effect on activity
additional information
suppression of cell-surface PDI expression with antisense oligodeoxynucleotide in RPAE cells
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
70 - 75
-
CxRP2 is heat sensitive losing substantial activity after 30 min at 70-75 °C, overview
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant b and b' domains and the bb' fragments of ERp57 and ERp72 from Escherichia coli
native enzyme from brain by anion exchange and bisphenyl A affinity chromatography, recombinant His-tagged enzyme from Escherichia coli by nickel affinity chromatography
-
recombinant wild-type and mutant PDI from Escherichia coli to homogeneity
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of b and b' domains and the bb' fragments of ERp57 and ERp72 in Escherichia coli
DNA and amino acid sequence determination, expression of His-tagged enzyme in Escherichia coli strain DH5alpha
-
expression of wild-type and mutant PDI in Escherichia coli strain BL21(DE3)
-
overexpression of PDI in GH3 cells, that release growth hormone via the T3-receptor, leads to reduced T3-induced GH release in the cells, mechanism, overview
-
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
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
-
protein disulfide gene expression is significantly decreased by 28% and 69% at 20 h after cecal ligation and puncture or lipopolysaccharide infusion, respectively
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
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
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
Lambert, N.; Freedman, R.B.
The latency of rat liver microsomal protein disulphide-isomerase
Biochem. J.
228
635-645
1985
Rattus norvegicus
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
-
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
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
-
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
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
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
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
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
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
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
Gilbert, H.F.
Protein disulfide isomerase
Methods Enzymol.
290
26-50
1998
Bos taurus, Saccharomyces cerevisiae, Mammalia, Rattus norvegicus
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
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
Noiva, R.
Enzymatic catalysis of disulfide formation
Protein Expr. Purif.
5
1-13
1994
Bacteria, Saccharomyces cerevisiae, eukaryota, Rattus norvegicus
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
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
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
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
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
Solovyov, A.; Gilbert, H.F.
Zinc-dependent dimerization of the folding catalyst, protein disulfide isomerase
Protein Sci.
13
1902-1907
2004
Rattus norvegicus
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
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)
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
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
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
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)
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
-
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
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
-
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
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
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
EXTERNAL LINKS (specific for EC-Number 5.3.4.1)
Transporter Classification Database (TCDB): 8.A.88.2.3, 8.A.88.2.7
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
