Information on EC 5.3.4.1 - Protein disulfide-isomerase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea

EC NUMBER
COMMENTARY
5.3.4.1
-
RECOMMENDED NAME
GeneOntology No.
Protein disulfide-isomerase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
catalyses the rearrangement of -S-S- bonds in proteins
show the reaction diagram
-
-
-
-
catalyses the rearrangement of -S-S- bonds in proteins
show the reaction diagram
mechanism
-
catalyses the rearrangement of -S-S- bonds in proteins
show the reaction diagram
mechanism
-
catalyses the rearrangement of -S-S- bonds in proteins
show the reaction diagram
mechanism
-
catalyses the rearrangement of -S-S- bonds in proteins
show the reaction diagram
structure of oxidized and reduced active site, the active site motif is -C-X-X-C-
-
catalyses the rearrangement of -S-S- bonds in proteins
show the reaction diagram
disulfide formation and isomerization mechanism by domains a and a', during transfer of oxidizing or reducing equivalents to substrates, the CXXC active site cycles between its oxidized, disulfide and reduced, thiol states
-
catalyses the rearrangement of -S-S- bonds in proteins
show the reaction diagram
active site location, structure, and redox state
-
catalyses the rearrangement of -S-S- bonds in proteins
show the reaction diagram
PDI introduces disulfides into proteins, oxidase activity, and provides quality control by catalyzing the rearrangement of incorrect disulfides, isomerase activity
-
catalyses the rearrangement of -S-S- bonds in proteins
show the reaction diagram
protein with nonconsecutive disulfie bonds require activity of DsbC for their full activity, the disulfide bonds are formed during the translocation across the cytoplasmic membrane
-
catalyses the rearrangement of -S-S- bonds in proteins
show the reaction diagram
active site structure
-
catalyses the rearrangement of -S-S- bonds in proteins
show the reaction diagram
the catalytic domain, residues 88-231, shows a thioredoxin fold with a helical insert, and an active site motif -C-X-X-C-, active site structure
-
catalyses the rearrangement of -S-S- bonds in proteins
show the reaction diagram
reaction mechanism
-
catalyses the rearrangement of -S-S- bonds in proteins
show the reaction diagram
mechanism of enzyme-assisted folding of plant cyclotides
-
catalyses the rearrangement of -S-S- bonds in proteins
show the reaction diagram
substrate binding and catalytic mechanism
-
catalyses the rearrangement of -S-S- bonds in proteins
show the reaction diagram
substrate binding and catalytic mechanism
P17967
catalyses the rearrangement of -S-S- bonds in proteins
show the reaction diagram
the nucleophilic C36 thiol of the protein disulfide isomerase a domain is positioned over the N-terminus of the alpha2 helix. The H38 amide in the reduced enzyme exhibits a maximum rate of exchange at pH 5 due to efficient general base catalysis by the neutral imidazole of its own side chain and suppression of its exchange by the ionization of the C36 thiol. Ionization of this thiol and deprotonation of the H38 side chain suppress the C39 amide hydroxide-catalyzed exchange by a million-fold. The electrostatic potential within the active site stabilizes the two distinct transition states that lead to substrate reduction and oxidation
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
intramolecular oxidoreduction
-
-
-
-
isomerization
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
Protein disulfide-isomerase
Needs reducing agents or partly reduced enzyme; the reaction depends on sulfhydryl-disulfide interchange.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5'-MD
-
-
-
-
58 kDa glucose regulated protein
-
-
-
-
58 kDa microsomal protein
-
-
-
-
AGR2
-
-
anterior gradient homolog 2
-
-
BPA-binding protein
-
-
CaBP1
-
-
-
-
CaBP2
-
-
-
-
CaBP2
P13667
-
CaBP2
P38659
-
Cellular thyroid hormone binding protein
-
-
-
-
cotyledon-specific chloroplast biogenesis factor CYO1
Q93YN0
-
disulfide bond isomerase
-
-
disulfide bond-forming enzyme
-
-
Disulfide interchange enzyme
-
-
-
-
disulfide isomerase
-
-
Disulfide isomerase ER-60
-
-
-
-
disulfide-bond isomerase
-
-
DsbA
-
-
-
-
DsbC
-
-
-
-
DsbD
-
-
-
-
Endoplasmic reticulum protein EUG1
-
-
-
-
ER protein 57
-
-
ER58
-
-
-
-
ERcalcistorin/protein-disulfide isomerase
-
i.e. ECaSt/PDI
ERcalcistorin/protein-disulfide isomerase
-
-
ERcalcistorin/protein-disulfide isomerase
Sea urchin
-
i.e. ECaSt/PDI
ERP-57
-
-
ERp-72 homolog
-
-
-
-
ERp18
-
-
ERp27
Q96DN0
-
ERp44
-
-
ERp57
-
-
-
-
ERp57
P30101
-
ERp57
-
-
ERp57
P38659
-
ERP59
-
-
-
-
ERP60
-
-
-
-
ERp72
-
-
-
-
ERp72
P13667
-
ERp72
P38659
-
fibronectin
-
extracellular matrix protein fibronectin contains an intrinsic protein-disulfide isomerase activity
gPDI-1
O97451
-
gPDI-2
O97452
-
gPDI-3
Q9U015
-
HIP-70
-
-
-
-
multifunctional protein disulfide isomerase
P07237, P13667, P30101, Q13087
-
P5
-
PDI homologue
P55
-
-
-
-
P58
-
-
-
-
pancreas-specific protein disulfide isomerase
-
-
pancreas-specific protein disulfide isomerase
Q13087
-
pancreas-specific protein disulfide isomerase
-
-
PDI
-
-
-
-
PDI
Q1HGL1
-
PDI
A5LHV9, A5LHW0, A5LHW1
-
PDI
P13667
-
PDI
A7YBW7, A7YBX0, A7YBX2, A7YBX4
-
PDI
Q53LQ0, Q67UF5
-
PDI
Q4Z2V7
-
PDI
Q4Z2V7
-
-
PDI
AY919669
-
PDI
Plasmodium knowlesi H
Q2XQR5
-
-
PDI
Q2XQR3
-
PDI
Plasmodium vivax Sal1
Q2XQR3
-
-
PDI
Q7RRT0
-
PDI
Saccharomyces cerevisiae trg1/TRG1
-
-
-
PDI
Schizosaccharomyces pombe KP1
O13811
-
-
PDI
Streptomyces sp. NCIM 5127
-
-
-
PDI A4
P13667
-
PDI I
-
-
PDI II
-
-
pdi-15
A7YBX4
-
pdi-40
A7YBX2
-
pdi-47
A7YBX0
-
pdi-52
A7YBW7
-
PDI-P5
E1CAJ6
-
PDI-related protein
-
-
PDIA1
P07237
-
PDIA2
Q13087
-
PDIA3
-
-
PDIA3
D0QEL0
-
PDIA3
E1CAJ6
-
PDIA4
P13667
-
PDIL-1
-
-
PDIL-2
-
-
PDIL1-1
Q53LQ0
-
PDIL2-3
Q67UF5
-
PDILT
-
-
PDIp
-
-
-
-
PDIp
Q13087
-
PDIp
-
-
PDIp
-
-
PDIr
-
-
protein disulfide isomaerase
-
-
protein disulfide isomaerase
Saccharomyces cerevisiae trg1/TRG1
-
-
-
protein disulfide isomerase
A0SHR2
-
protein disulfide isomerase
-
-
protein disulfide isomerase
Q93YN0
-
protein disulfide isomerase
-
-
protein disulfide isomerase
-, A3RMS2
-
protein disulfide isomerase
-
-
protein disulfide isomerase
Chlamydomonas reinhardtii 2137a
-
-
-
protein disulfide isomerase
Q1HGL1
-
protein disulfide isomerase
-
-
protein disulfide isomerase
-
-
protein disulfide isomerase
-
-
protein disulfide isomerase
-
-
protein disulfide isomerase
-
-
protein disulfide isomerase
P13667
-
protein disulfide isomerase
-
-
protein disulfide isomerase
Q9C1Z8
-
protein disulfide isomerase
-
-
protein disulfide isomerase
-
-
protein disulfide isomerase
P27773
-
protein disulfide isomerase
-
-
protein disulfide isomerase
Q53LQ0, Q67UF5
-
protein disulfide isomerase
Q4Z2V7
-
protein disulfide isomerase
Q4Z2V7
-
-
protein disulfide isomerase
Q5UAH0
-
protein disulfide isomerase
-
-
protein disulfide isomerase
AY919669
-
protein disulfide isomerase
Q2XQR5
-
protein disulfide isomerase
Plasmodium knowlesi H
Q2XQR5
-
-
protein disulfide isomerase
Q2XQR3
-
protein disulfide isomerase
Plasmodium vivax Sal1
Q2XQR3
-
-
protein disulfide isomerase
Q7RRT0
-
protein disulfide isomerase
P38659
-
protein disulfide isomerase
-
-
protein disulfide isomerase
D0EJL8
-
protein disulfide isomerase
O13811
-
protein disulfide isomerase
Schizosaccharomyces pombe KP1
O13811
-
-
protein disulfide isomerase
-
-
protein disulfide isomerase
Streptomyces sp. NCIM 5127
-
-
-
protein disulfide isomerase
P12865
-
protein disulfide isomerase 3
Q9U015
-
protein disulfide isomerase A1
-
-
protein disulfide isomerase A3
P27773
-
protein disulfide isomerase A3
-
-
protein disulfide isomerase associated 3
D0QEL0
-
Protein disulfide isomerase P5
-
-
-
-
protein disulfide isomerase-1
A5LHW0
-
protein disulfide isomerase-2
A5LHV9
-
protein disulfide isomerase-3
A5LHW1
-
protein disulfide isomerase-like protein of the testis
-
-
protein disulfide isomerase-P5
E1CAJ6
-
protein disulfide isomerase-related chaperone Wind
-
-
Protein disulfide isomerase-related protein
-
-
-
-
protein disulfide isomerase::
-
-
protein disulfide oxidoreductase
-
-
protein disulfide-isomerase A4
P38659
-
Protein disulphide isomerase
-
-
-
-
Protein disulphide isomerase
-
-
Protein disulphide isomerase
-
-
Protein ERp-72
-
-
-
-
protein-disulfide isomerase
-
-
protein-disulfide isomerase
-
-
protein-disulfide isomerase
A7YBW7, A7YBX0, A7YBX2, A7YBX4
-
protein-disulfide isomerase
-
-
protein-disulfide isomerase
-
-
R-cognin
-
-
-
-
RB60
Chlamydomonas reinhardtii 2137a
-
-
-
Rearrangease
-
-
-
-
Reduced ribonuclease reactivating enzyme
-
-
-
-
Retina cognin
-
-
-
-
S-S rearrangase
-
-
-
-
thiol-protein oxidoreductase
Q1HGL1
-
Thyroid hormone-binding protein
-
-
-
-
Thyroxine deiodinase
-
-
-
-
Iodothyronine 5'-monodeiodinase
-
-
-
-
additional information
A0SHR2
the enzyme belongs to the family of protein disulfide isomerases
additional information
-
PDI belongs to the thioredoxin superfamily
additional information
-
PDI, DsbC, and DbsG belong to the thioredoxin superfamily
additional information
-
the enzyme belongs to the Dsb family
additional information
-
the enzyme is a member of the thioredoxin fold superfamily
additional information
-
protein disulfide-isomerase is identical with the beta-subunit of the prolyl 4-hydroxylase tetramer
additional information
-
PDI and other PDI family proteins are members of the thioredoxin superfamily
additional information
-
ERP-57 is a member of the thiol oxidoreductase family
additional information
-
PDI belongs to the thioredoxin superfamily
additional information
-
protein disulfide isomerase is identical to the beta-subunit of prolyl-4-hydroxylase
additional information
-
protein disulfide isomerase is identical to the beta-subunit of prolyl-4-hydroxylase; thyroid hormone binding protein is apparently identical to protein disulfide isomerase
additional information
-
the enzyme belongs to the protein disulfide isomerase family
additional information
-
the enzyme belongs to the yeast hPDI enzyme family
additional information
-
the enzyme is a member of the PDI family
additional information
-
the enzyme is a member of the protein disulfide isomerase family of oxidoreductases
additional information
P07237, P13667, P30101
the enzyme belongs to the protein disulfide isomerase family
additional information
Q13087
PDIp is a member of the protein disulfide isomerase PDI family
additional information
Q13087
the enzyme belongs to the protein disulfide isomerase family
additional information
Q96DN0
the enzyme belongs to the family of protein disulfide isomerases
additional information
-
protein disulfide isomerase is identical to the beta-subunit of prolyl-4-hydroxylase
additional information
-
the enzyme is a member of the PDI enzyme family
additional information
-
the enzyme is a member of the PDI family
additional information
-
PDI belongs to the thioredoxin superfamily
additional information
-
PDI, Eug1p, Mpd1p, Mpd2p, and Eps1p belong to the thioredoxin superfamily
additional information
-
the enzymes yPDI, Mpd1p, Mpd2p, and Eug1p belong to the yeast yPDI enzyme family
additional information
Saccharomyces cerevisiae trg1/TRG1
-
the enzymes yPDI, Mpd1p, Mpd2p, and Eug1p belong to the yeast yPDI enzyme family
-
CAS REGISTRY NUMBER
COMMENTARY
37318-49-3
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
a tick cultured on rabbit hosts, constitutive gene
SwissProt
Manually annotated by BRENDA team
12 genes coding for protein disulfide isomerase. Expression of six PDI genes is significantly up-regulated by unfolded protein response and sharply attenuated by the transcription inhibitor, actinomycin D. PDI and binding protein BIP2 expression is not affected in the unfolded protein response signaling mediator Atire1-2 mutant. The expression of four PDI genes is decreased in the unfolded protein response signaling mediator Atbzip60 mutant
-
-
Manually annotated by BRENDA team
calf
-
-
Manually annotated by BRENDA team
ox; protein disulfide isomerase activity and glutathione-insulin transhydrogenase activity, EC 1.8.4.2, are catalyzed by a single enzyme protein
-
-
Manually annotated by BRENDA team
protein disulfide isomerase activity and glutathione-insulin transhydrogenase activity, EC 1.8.4.2, are catalyzed by a single enzyme protein
-
-
Manually annotated by BRENDA team
thyroid hormone binding protein is apparently identical to protein disulfide isomerase
-
-
Manually annotated by BRENDA team
isozyme PDI-2; wild-type strain N2 and diverse mutant strains, overview, isozymes PDI-1, PDI-2 and PDI-3 encoded by genes pdi-1, pdi-2 and pdi-3
SwissProt
Manually annotated by BRENDA team
wild-type strain N2 and diverse mutant strains, overview, isozymes PDI-1 and PDI-3 encoded by genes pdi-1 and pdi-3
-
-
Manually annotated by BRENDA team
Chlamydomonas reinhardtii 2137a
strain 2137a
-
-
Manually annotated by BRENDA team
a marine snail
-
-
Manually annotated by BRENDA team
isoform Pdi-2
-
-
Manually annotated by BRENDA team
gene dsbB
-
-
Manually annotated by BRENDA team
isozymes DsbC and DsbG
-
-
Manually annotated by BRENDA team
proteins with protein disulfide isomerase activity: DsbA, DsbC and DsbD
-
-
Manually annotated by BRENDA team
several strains, overview
-
-
Manually annotated by BRENDA team
protein disulfide-isomerase is identical with the beta-subunit of the prolyl 4-hydroxylase tetramer, alpha2beta2
-
-
Manually annotated by BRENDA team
; PD-2 precursor
SwissProt
Manually annotated by BRENDA team
; PD-3 precursor
SwissProt
Manually annotated by BRENDA team
cv. Jack, genes PDIS-1 and PDIS-2
-
-
Manually annotated by BRENDA team
cv. Jack, isozymes GmPDIL-1, GmPDIL-2, GmPDIL-3a, and GmPDIL-3b
-
-
Manually annotated by BRENDA team
isoform Pdi-1
SwissProt
Manually annotated by BRENDA team
isoform Pdi-2
A5LHV9
SwissProt
Manually annotated by BRENDA team
isoform Pdi-3
SwissProt
Manually annotated by BRENDA team
isozyme HlPDI-1; a tick cultured on rabbit hosts, gene HlPDI-1
SwissProt
Manually annotated by BRENDA team
isozyme HlPDI-2; a tick cultured on rabbit hosts, gene HlPDI-2
A5LHV9
SwissProt
Manually annotated by BRENDA team
isozyme HlPDI-3; a tick cultured on rabbit hosts, gene HlPDI-3
SwissProt
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
ERp27
SwissProt
Manually annotated by BRENDA team
ERp57
SwissProt
Manually annotated by BRENDA team
ERp72 or PDIA4, respecitvely
SwissProt
Manually annotated by BRENDA team
isoform ERdj5; isoform PDI
-
-
Manually annotated by BRENDA team
isoform pancreas-specific protein disulfide isomerase homolog, PDIp
-
-
Manually annotated by BRENDA team
isoform PDI
-
-
Manually annotated by BRENDA team
isoform procollagen-proline, 2-oxoglutarate-4-dioxygenase beta subunit
-
-
Manually annotated by BRENDA team
PDIA1
SwissProt
Manually annotated by BRENDA team
PDIA2 precursor
SwissProt
Manually annotated by BRENDA team
protein disulfide isomerase is identical to the beta-subunit of prolyl-4-hydroxylase
-
-
Manually annotated by BRENDA team
protein disulfide isomerase is identical to the beta-subunit of prolyl-4-hydroxylase; thyroid hormone binding protein is apparently identical to protein disulfide isomerase
-
-
Manually annotated by BRENDA team
recombinant enzyme obtained from Escherichia coli strain BL21
-
-
Manually annotated by BRENDA team
15 kDa isozyme, fragment
SwissProt
Manually annotated by BRENDA team
40 kDa isozyme, fragment
SwissProt
Manually annotated by BRENDA team
47 kDa isozyme, fragment
SwissProt
Manually annotated by BRENDA team
52 kDa isozyme
SwissProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
protein disulfide isomerase is identical to the beta-subunit of prolyl-4-hydroxylase
-
-
Manually annotated by BRENDA team
male Balb/c or CD1 mice
-
-
Manually annotated by BRENDA team
male C57BL/6 mice
-
-
Manually annotated by BRENDA team
PDIA3; C57BL/6 mice
UniProt
Manually annotated by BRENDA team
cultivar Kinmaze
UniProt
Manually annotated by BRENDA team
strain ANKA, isozyme PDI-8
SwissProt
Manually annotated by BRENDA team
strain ANKA, isozyme PDI-8
SwissProt
Manually annotated by BRENDA team
chabaudi
UniProt
Manually annotated by BRENDA team
chimeric PDI mutant containing Pichia pastoris signal sequence and ER retention sequence
AY919669
GenBank
Manually annotated by BRENDA team
strain 3D7
-
-
Manually annotated by BRENDA team
strain 3D7, isozymes PDI-8, PDI-9, PDI-11, and PDI-14
-
-
Manually annotated by BRENDA team
strains 3D7 and FcB1, isozyme PDI-22
-
-
Manually annotated by BRENDA team
strain H, isozyme PDI-8
SwissProt
Manually annotated by BRENDA team
Plasmodium knowlesi H
strain H, isozyme PDI-8
SwissProt
Manually annotated by BRENDA team
strain Sal1, isozyme PDI-8
SwissProt
Manually annotated by BRENDA team
Plasmodium vivax Sal1
strain Sal1, isozyme PDI-8
SwissProt
Manually annotated by BRENDA team
isozyme PDI-8
SwissProt
Manually annotated by BRENDA team
genes dsbA and dsbC
-
-
Manually annotated by BRENDA team
adult and newborn
-
-
Manually annotated by BRENDA team
Fischer 344 rats
-
-
Manually annotated by BRENDA team
glutathione-insulin transhydrogenase and protein disulfide-isomerase are both not catalyzed by a single enzyme species
-
-
Manually annotated by BRENDA team
Sprague Dawley rats
-
-
Manually annotated by BRENDA team
several strans, overview
-
-
Manually annotated by BRENDA team
strain trg1/TRG1
-
-
Manually annotated by BRENDA team
Saccharomyces cerevisiae trg1/TRG1
strain trg1/TRG1
-
-
Manually annotated by BRENDA team
-
D0QEL0
UniProt
Manually annotated by BRENDA team
precursor; strain KP1
UniProt
Manually annotated by BRENDA team
Schizosaccharomyces pombe KP1
precursor; strain KP1
UniProt
Manually annotated by BRENDA team
Sea urchin
-
-
-
Manually annotated by BRENDA team
NCIM 5127
-
-
Manually annotated by BRENDA team
Streptomyces sp. NCIM 5127
NCIM 5127
-
-
Manually annotated by BRENDA team
PDI-P5; isozymes PDIA3 and PDI-P5
UniProt
Manually annotated by BRENDA team
PDI-2; two PDI enzyme forms, which contain one or two double-cysteine redox-active sites and correspond to a single domain PDI and a class 1 PDI, i.e. PDI-1 and PDI-2
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
malfunction
-
PDI inhibition or silencing increases apoptosis and inhibits migration and adhesion of endothelial cells, overview
malfunction
-
functional inhibition of protein disulfide isomerase by S-nitrosylation may contribute to pathophysiology in both mutant superoxide dismutase 1-linked disease and sporadic amyotrophic lateral sclerosis
malfunction
-
the anomalous behavior of PDI during a key step in oxidative regeneration may contribute to misfolding in the endoplasmic reticulum, aggregation, and neurodegenerative disease
malfunction
-
mice lacking AGR2 are viable but are highly susceptible to colitis, indicating a critical role for AGR2 in protection from disease
malfunction
-
inhibition of cell surface PDI induces a marked increase in tissue factor procoagulant function
malfunction
Q53LQ0, Q67UF5
PDIL2-3 knockdown causes aberrant accumulation of prolamins in endoplasmic reticulum-derived type-I protein bodies whereas the oxidative folding of vacuole-targeted proteins, such as proglutelins and alpha-globulin, is hardly affected. PDIL2-3 knockdown inhibits the accumulation of Cys-rich 10-kD prolamin in the core of type-I protein bodies
metabolism
-
the close interdependence between Mnl1p and PDI suggests that these two proteins form a functional unit in the ER-associated degradation, ERAD, pathway
physiological function
-
the enzyme is involved in myocardial angiogenesis, overview
physiological function
-
the enzyme is involved in myocardial angiogenesis. Protein disulfide isomerase is highly upregulated in hypoxic myocardial capillary endothelial cells, chronic hypoxia increases the survival rate and reduces the infarct size in myocardial ischemia, overview
physiological function
Q13087
PDI is a multifunctional protein for catalyzing the formation, isomerization, and reduction of disulfide bonds
physiological function
E1CAJ6
physiological roles of PDIA3 and PDI-P5 in sperm maturation and fertilization, overview
physiological function
-
the enzyme plays a role in the formation of disulfide bonds in immunoglobulins, it is also involved in disulfide bond formation of the IgG4 subclass of antibody, but catalysis of disulfide bond formation is not rate limiting for IgG4 production
physiological function
-
endoplasmic reticulum stress is important in the formation of mutant superoxide dismutase 1 inclusions, and protein disulfide isomerase has an important function in ameliorating mutant superoxide dismutase 1 aggregation and toxicity
physiological function
D0QEL0, -
PDIA3 is an endoplasmic reticulum stress protein. It is induced by oxidative stress and plays a role in relation to stress regulation
physiological function
-
the substrate binding, but not catalytic, activity of PDI is essential for the degradation of MHC class I HC by human cytomegalovirus glycoprotein US2, but not by US11, since oxidative folding of US2 is required for US2 function in inducing degradation of MHC class I molecules, PDI catalyses the release of MHC class I molecules from US2, function for PDI in SPP-mediated ERAD pathway, overview
physiological function
-
PDI and other PDI family proteins are thought to play important roles in disulfide bond formation and isomerization in the endoplasmic reticulum
physiological function
-
PDI is a key enzyme involved in formation of correct pattern of disulfide bonds in proteins. PDI also plays an important role in the hypothalamic-pituitary-thyroid axis, mechanism, overview
physiological function
-
PDIp may function as a protein-folding catalyst for secretory digestive enzymes
physiological function
-
PDI is an abundant enzyme that forms, breaks, and isomerizes disulfide bonds and is therefore an important cellular defense against protein misfolding. PDI can be protective against mutant SOD1 aggregation and toxicity
physiological function
-
the enzyme is required for infection by Chlamydia species
physiological function
-
the protein disulfide isomerase AGR2 is essential for production of intestinal mucin MUC2, a large, cysteine-rich glycoprotein that forms the protective mucus gel lining the intestine
physiological function
-
FXIII-PDI activity may have a role in platelet function
physiological function
-
extracellular protein disulfide isomerase negatively regulates coagulation on endothelial cells through modulation of phosphatidylserine exposure
physiological function
-
protein disulfide isomerase blocks transcription factor C/EBP-alpha translation but not transcription
physiological function
-
PDI is required for cholera toxin intoxication but not for cholera toxin subunit A1 translocation
physiological function
Q53LQ0, Q67UF5
PDIL2-3 does not facilitate the oxidative folding of proglutelins; the a and a' domains of PDIL1-1 are both functional in the oxidative folding of proglutelins
physiological function
-
the DsbA coexpressed as whole cell bioconversion system can more efficiently detoxify high concentration of organophosphates than cells expressing methyl parathion hydrolase only. Overexpression of protein disulfide isomerase DsbA enhances detectability in the environment following degradation of pesticide residues
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
Agp mutant
?
show the reaction diagram
-
folding of Agp mutant, DsbC, mutant of Agp, an AppA homologue, containing the AppA nonconsecutive disulfide bond
-
-
?
alkaline protease inhibitor
?
show the reaction diagram
-
folding and rearrangement of alkaline protease inhibitor, folding and rearrangement of alkaline protease inhibitor, PDI contains 2 cysteine residues in the active site which are involved in rearrangement of disulfide bonds by function in thiol/disulfide exchange
-
-
?
alkaline protease inhibitor
?
show the reaction diagram
Streptomyces sp. NCIM 5127
-
folding and rearrangement of alkaline protease inhibitor, folding and rearrangement of alkaline protease inhibitor, PDI contains 2 cysteine residues in the active site which are involved in rearrangement of disulfide bonds by function in thiol/disulfide exchange
-
-
?
alpha-globulin
?
show the reaction diagram
Q53LQ0, Q67UF5
PDIL1-1 facilitates the oxidative folding of alpha-globulin
-
-
?
carboxypeptidase Y
?
show the reaction diagram
-
maturation of carboxypeptidase Y
-
-
?
cholera toxin
?
show the reaction diagram
-
reduced (but not oxidized) protein-disulfide isomerase displaces the cholera toxin A1 subunit from the holotoxin without unfolding the A1 subunit
-
-
-
citrate synthase
stabilized citrate synthase
show the reaction diagram
-
DsbG suppresses aggregation of luciferase at 43C, enzyme has both PDI and chaperone activity
-
?
conotoxins sTx3.1
?
show the reaction diagram
-, Q1HGL1
disulfide formation, macromolecular crowding has little effect on the protein disulfide isomerase-catalyzed oxidative folding and disulfide isomerization of conotoxin
-
-
?
conotoxins tx3a
?
show the reaction diagram
-, Q1HGL1
disulfide formation, macromolecular crowding has little effect on the protein disulfide isomerase-catalyzed oxidative folding and disulfide isomerization of conotoxin
-
-
?
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
-
-
?
degenerated RNase type III
?
show the reaction diagram
P12865, -
refolding of degenerated RNase type III, bovine pancreatic substrate, recombinant GST-tagged PDI, the coupled-assay method involves reduction of insulin in presence of DTT
-
-
?
dehydroascorbate
ascorbate
show the reaction diagram
-
PDI has dehydroascorbate reductase activity, PDI has dehydroascorbate reductase activity, PDI may play a role in the intraluminal dehydroascorbate reduction
-
?
denatured D-glceraldehyde-3-phosphate dehydrogenase
refolded D-glceraldehyde-3-phosphate dehydrogenase
show the reaction diagram
-
interaction of PDI with cyclophilin B increases its chaperone activity
-
?
denatured D-glyceraldehyde-3-phosphate dehydrogenase
refolded D-glyceraldehyde-3-phosphate dehydrogenase
show the reaction diagram
-
chaperone activity of PDI
-
?
denatured eclosion hormone
active eclosion hormon
show the reaction diagram
-
PDI acts as a chaperone and refolds the insect neuropeptide eclosion hormone
-
?
denatured lysozyme
?
show the reaction diagram
-
PDI catalyzes the formation, rearrangement, and breakage of disulfide bonds, oxidative refolding by PDI almost completely restores lysozyme activity, overview
-
-
?
denatured rhodanese
refolded rhodanese
show the reaction diagram
-
interaction of PDI with cyclophilin B increases its chaperone activity
-
?
denatured rhodanese
?
show the reaction diagram
-
PDI exhibits chaperone activity with rhodanese
-
-
?
denatured RNase A
?
show the reaction diagram
Q93YN0
recombinant CYO1 renatures RNase A
-
-
?
denatured Rnase A
active Rnase A
show the reaction diagram
-
-
-
-
?
denatured-reduced lysozyme
?
show the reaction diagram
-
oxidase activity of PDI
-
-
?
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
-
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, i.e. ERalpha, PDI colocalizes with ERalpha in MCF-7 nuclei, alters ERalpha conformation, enhances the ERalpha-estrogen response element interaction in the absence and presence of an oxidizing agent, influences the ability of ERalpha to mediate changes in gene expression, and associates with promoter regions of two endogenous estrogen-responsive genes, overview
-
-
?
folded cholera toxin
unfolded cholera toxin
show the reaction diagram
-
PDI binds in the reduced state to the A chain of cholera toxin, in the oxidized state it releases it, PDI may be involved in the retrograde protein transport into the cytosol
-
?
glycoprotein 120
glycoprotein 120
show the reaction diagram
-
PDI may play a role in HIV-1 infection by reducing HIV-1 envelope glycoprotein 120
-
?
GSSG
GSH
show the reaction diagram
-
disulfide reduction of GSSG, the disulfide reduction activity of both PDI-thioredoxin reductase and PDI-DTT is reduced
-
-
?
insulin
?
show the reaction diagram
-
-
-
-
?
insulin
?
show the reaction diagram
-
-
-
-
?
insulin
?
show the reaction diagram
A7YBW7, A7YBX0, A7YBX2, A7YBX4, -
-
-
-
?
insulin
?
show the reaction diagram
-
disulfide-bond reduction in substrate insulin, reduction activity by Holmgren's turbimetric method
-
-
-
insulin
?
show the reaction diagram
-
reduction of insulin, turbidometry assay including glutathione reduction and alkylation of 4-acetamido-4'-maleimidyl-stilbene-2,2'-disulfonate, as well as treatment with DTT and iodoacetamide or iodoacetate for subsequent insulin reduction, isomerase activity, overview
-
-
?
insulin
?
show the reaction diagram
-
bovine substrate, reduction of disulfide bonds
-
-
?
insulin
?
show the reaction diagram
Q93YN0
recombinant CYO1 accelerates disulfide bond reduction in the model substrate insulin
-
-
?
insulin
?
show the reaction diagram
-
reduction of disulfide bonds
-
-
?
insulin
?
show the reaction diagram
O13811, -
reduction of insulin disulfide bonds
-
-
-
insulin
?
show the reaction diagram
-
reduction of sidulfide bonds
-
-
?
insulin
?
show the reaction diagram
-
PDI exhibits reductase activity with insulin
-
-
?
insulin
?
show the reaction diagram
-
reductase activity of PDI
-
-
?
insulin
?
show the reaction diagram
Schizosaccharomyces pombe KP1
O13811
reduction of insulin disulfide bonds
-
-
-
insulin + DTT
?
show the reaction diagram
A0SHR2, -
bovine substrate, reductase activity with DTT
-
-
?
Insulin-(SS) + dithiothreitol
Insulin-(SH)2 + oxidized dithiothreitol
show the reaction diagram
-
-
-
-
Insulin-(SS) + GSH
Insulin-(SH)2 + GSSG
show the reaction diagram
-
-
-
-
Insulin-(SS) + GSH
Insulin-(SH)2 + GSSG
show the reaction diagram
-
-
-
-
Insulin-(SS) + GSH
Insulin-(SH)2 + GSSG
show the reaction diagram
-
-
-
-
-
Insulin-(SS) + GSH
Insulin-(SH)2 + GSSG
show the reaction diagram
-
-
-
-
Insulin-(SS) + GSH
Insulin-(SH)2 + GSSG
show the reaction diagram
-
-
-
-
Insulin-(SS) + GSH
Insulin-(SH)2 + GSSG
show the reaction diagram
-
-
-
-
Insulin-(SS) + GSH
Insulin-(SH)2 + GSSG
show the reaction diagram
-
-
-
-
kalata B1
?
show the reaction diagram
-
and derivatives, PDI dramatically enhanced the correct oxidative folding of linear and cyclic kalata B1 at physiological pH, determination of folding intermediates
-
-
?
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
-
-
?
luciferase
stabilized luciferase
show the reaction diagram
-
DsbG suppresses aggregation of luciferase at 43C, enzyme has both PDI and chaperone activity
-
?
lysozyme
aggregated lysozyme
show the reaction diagram
-
PDI has antichaperone activity facilitating protein aggregation
-
?
NRCSQGSCWN
NRCSQGSCWN
show the reaction diagram
-
-
-
?
NRCSQGSCWN
NRCSQGSCWN
show the reaction diagram
-
-
-
?
NRCSQGSCWN
?
show the reaction diagram
-
disulfide-bond formation within the thiol substrate peptide NRCSQGSCWN, oxidation activity requires GSH/GSSG
-
-
-
oxidized insulin + dithiothreitol
reduced insulin
show the reaction diagram
O97451, O97452, Q9U015
gPDI-2, low activity with gPDI-3, no activity with gPDI-1
-
?
oxidoreductase Ero1
?
show the reaction diagram
-
disulfide bond formation in the oxidoreductase Ero1, endoplasmic reticular protein interacts with PDILT
-
-
?
phytase
?
show the reaction diagram
-
folding of phytase, i.e. AppA, substrate from Escherichia coli, contains 3 consecutive and 1 nonconsecutive disulfide bonds, DsbC, no activity of DsbC with an AppA mutant C155S/C430S lacking the nonconsecutive disulfide bond
-
-
?
Pipe
?
show the reaction diagram
-
processing and targeting of Pipe, Pipe is an essential Golgi transmembrane-O-sulfotransferase, protein disulfide isomerase-related chaperone Wind is required for processing and correct targeting of the substrate, mapping of multiple substrate binding sites in Pipe, one enzyme site in vicinity of an exposed cluster of tyrosine residues within the thioredoxin fold domain is essential for activity, a second enzyme site in the enzyme's D-domain is also necessary for processing activity, but competitive to the thioredoxin fold domain residue, overview
-
-
?
Proteins
Proteins
show the reaction diagram
-
-
-
-
-
Proteins
Proteins
show the reaction diagram
-
-
-
-
-
Proteins
Proteins
show the reaction diagram
-
refolding of scrambled ribonuclease
with correct disulfide bonds
-
Proteins
Proteins
show the reaction diagram
-
refolding of scrambled ribonuclease
with correct disulfide bonds
-
Proteins
Proteins
show the reaction diagram
-
refolding of scrambled ribonuclease
with correct disulfide bonds
-
Proteins
Proteins
show the reaction diagram
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
-
Proteins
Proteins
show the reaction diagram
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
-
Proteins
Proteins
show the reaction diagram
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
-
Proteins
Proteins
show the reaction diagram
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
-
Proteins
Proteins
show the reaction diagram
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
-
Proteins
Proteins
show the reaction diagram
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
-
Proteins
Proteins
show the reaction diagram
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
-
Proteins
Proteins
show the reaction diagram
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
-
Proteins
Proteins
show the reaction diagram
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
-
Proteins
Proteins
show the reaction diagram
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
-
Proteins
Proteins
show the reaction diagram
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
-
Proteins
Proteins
show the reaction diagram
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
-
Proteins
Proteins
show the reaction diagram
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
-
Proteins
Proteins
show the reaction diagram
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
-
Proteins
Proteins
show the reaction diagram
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
-
Proteins
Proteins
show the reaction diagram
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
-
Proteins
Proteins
show the reaction diagram
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
-
Proteins
Proteins
show the reaction diagram
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
-
Proteins
Proteins
show the reaction diagram
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
-
Proteins
Proteins
show the reaction diagram
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
-
Proteins
Proteins
show the reaction diagram
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
-
Proteins
Proteins
show the reaction diagram
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
-
Proteins
Proteins
show the reaction diagram
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
-
Proteins
Proteins
show the reaction diagram
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
-
Proteins
Proteins
show the reaction diagram
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
-
Proteins
Proteins
show the reaction diagram
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
-
Proteins
Proteins
show the reaction diagram
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
-
Proteins
Proteins
show the reaction diagram
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
-
Proteins
Proteins
show the reaction diagram
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
-
Proteins
Proteins
show the reaction diagram
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
-
Proteins
Proteins
show the reaction diagram
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
-
Proteins
Proteins
show the reaction diagram
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
-
Proteins
Proteins
show the reaction diagram
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
-
Proteins
Proteins
show the reaction diagram
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
-
Proteins
Proteins
show the reaction diagram
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
-
Proteins
Proteins
show the reaction diagram
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
-
Proteins
Proteins
show the reaction diagram
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
-
Proteins
Proteins
show the reaction diagram
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
-
Proteins
Proteins
show the reaction diagram
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
-
Proteins
Proteins
show the reaction diagram
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
-
Proteins
Proteins
show the reaction diagram
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
-
Proteins
Proteins
show the reaction diagram
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
-
Proteins
Proteins
show the reaction diagram
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
-
Proteins
Proteins
show the reaction diagram
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
-
Proteins
Proteins
show the reaction diagram
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
-
Proteins
Proteins
show the reaction diagram
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
-
Proteins
Proteins
show the reaction diagram
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
-
Proteins
Proteins
show the reaction diagram
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
-
Proteins
Proteins
show the reaction diagram
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
-
Proteins
Proteins
show the reaction diagram
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
-
Proteins
Proteins
show the reaction diagram
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
-
Proteins
Proteins
show the reaction diagram
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
-
Proteins
Proteins
show the reaction diagram
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
-
Proteins
Proteins
show the reaction diagram
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
-
Proteins
Proteins
show the reaction diagram
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
-
Proteins
Proteins
show the reaction diagram
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
-
Proteins
Proteins
show the reaction diagram
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
-
Proteins
Proteins
show the reaction diagram
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
-
Proteins
Proteins
show the reaction diagram
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
-
Proteins
Proteins
show the reaction diagram
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
-
Proteins
Proteins
show the reaction diagram
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
-
Proteins
Proteins
show the reaction diagram
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
-
Proteins
Proteins
show the reaction diagram
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
-
Proteins
Proteins
show the reaction diagram
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
-
Proteins
Proteins
show the reaction diagram
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
-
Proteins
Proteins
show the reaction diagram
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
-
Proteins
Proteins
show the reaction diagram
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
-
Proteins
Proteins
show the reaction diagram
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
-
Proteins
Proteins
show the reaction diagram
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
-
Proteins
Proteins
show the reaction diagram
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
-
Proteins
Proteins
show the reaction diagram
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
-
Proteins
Proteins
show the reaction diagram
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
-
Proteins
Proteins
show the reaction diagram
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
-
Proteins
Proteins
show the reaction diagram
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
-
Proteins
Proteins
show the reaction diagram
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
-
Proteins
Proteins
show the reaction diagram
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
-
Proteins
Proteins
show the reaction diagram
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
-
Proteins
Proteins
show the reaction diagram
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
-
Proteins
Proteins
show the reaction diagram
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
-
Proteins
Proteins
show the reaction diagram
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
-
Proteins
Proteins
show the reaction diagram
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
-
Proteins
Proteins
show the reaction diagram
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
-
Proteins
Proteins
show the reaction diagram
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
-
Proteins
Proteins
show the reaction diagram
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
-
Proteins
Proteins
show the reaction diagram
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
-
Proteins
Proteins
show the reaction diagram
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
-
Proteins
Proteins
show the reaction diagram
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
-
Proteins
Proteins
show the reaction diagram
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
-
Proteins
Proteins
show the reaction diagram
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
-
Proteins
Proteins
show the reaction diagram
-
native, reduced or with wrong disulfide bonds
with correct disulfide bonds
-
Proteins
Proteins
show the reaction diagram
-
cosubstrate: DTT, 2-mercaptoethanol, GSH, or Cys
with correct disulfide bonds
-
Proteins
Proteins
show the reaction diagram
-
incorrectly disulfide-linked Bowman Birk soybean trypsin
with correct disulfide bonds
-
Proteins
Proteins
show the reaction diagram
-
eduction of insulin and oxidative folding of ribonuclease A
with correct disulfide bonds
-
Proteins
Proteins
show the reaction diagram
-
incorrectly disulfide-linked lysozyme
with correct disulfide bonds
-
Proteins
Proteins
show the reaction diagram
-
cosubstrate dithiothreitol can be replaced by GSH, cysteamine, 2-mercaptoethanol, thioglycollic acid or L-Cys, but at significantly higher concentrations
with correct disulfide bonds
-
Proteins
Proteins
show the reaction diagram
-
refolding of scrambled lysosyme
with correct disulfide bonds
-
Proteins
Proteins
show the reaction diagram
-
incorrectly disulfide-linked RNAse
with correct disulfide bonds
-
Proteins
Proteins
show the reaction diagram
-
incorrectly disulfide-linked RNAse
with correct disulfide bonds
-
Proteins
Proteins
show the reaction diagram
-
refolding and activation of human carbonic anhydrase IV, GSSG promotes the activation
with correct disulfide bonds
-
Proteins
Proteins
show the reaction diagram
-
incorrectly disulfide-linked bovine pancreatic ribonuclease
with correct disulfide bonds
-
Proteins
Proteins
show the reaction diagram
-
incorrectly disulfide-linked ribonuclease
with correct disulfide bonds
-
Proteins
?
show the reaction diagram
-
-
-
-
-
Proteins
?
show the reaction diagram
-
-
-
-
-
Proteins
?
show the reaction diagram
-
-
-
-
-
Proteins
?
show the reaction diagram
-
-
-
-
-
Proteins
?
show the reaction diagram
-
-
-
-
-
Proteins
?
show the reaction diagram
-
native, reduced or with wrong disulfide bonds
-
-
-
Proteins
?
show the reaction diagram
-
native, reduced or with wrong disulfide bonds
-
-
-
Proteins
?
show the reaction diagram
-
native, reduced or with wrong disulfide bonds
-
-
-
Proteins
?
show the reaction diagram
-
native, reduced or with wrong disulfide bonds
-
-
-
Proteins
?
show the reaction diagram
-
native, reduced or with wrong disulfide bonds
-
-
-
Proteins
?
show the reaction diagram
-
native, reduced or with wrong disulfide bonds
-
-
-
Proteins
?
show the reaction diagram
-
involved in the assembly of wheat storage proteins within the endoplasmic reticulum
-
-
-
Proteins
?
show the reaction diagram
-
proposed physiological role as catalyst of formation of native disulfide bonds in nascent and newly synthesized secretory proteins
-
-
-
Proteins
?
show the reaction diagram
-
facilitates the formation of the correct disulfide bonds within newly synthesized polypeptides
-
-
-
Proteins
?
show the reaction diagram
-
catalyzes disulfide cleavage in membrane-bound diphtheria toxin or the membrane-bound conjugate, iodotyramine conjugated with poly(D-Lys) via a 3,3'-dithiobis(propionic acid) spacer
-
-
-
Proteins
?
show the reaction diagram
-
enzyme may play a physiological role in the catalysis of S-S-bond formation in prolactin
-
-
-
Proteins
?
show the reaction diagram
-
enzyme may be involved in the formation of intra-chain and inter-chain disulfide bonds in procollagen
-
-
-
Proteins
?
show the reaction diagram
-
involved in cotranslational disulfide bond formation
-
-
-
Proteins
?
show the reaction diagram
-
may play a role in the formation of disulfide bonds in extracellular and periplasmic proteins
-
-
-
Proteins
?
show the reaction diagram
-
facilitates the formation of disulfides during the folding and processing of membrane and secretory proteins
-
-
-
Proteins
?
show the reaction diagram
-
catalysis of native disulfide bond formation
-
-
-
Proteins
?
show the reaction diagram
-
platelet enzyme may play a role in the various haemostatic and tissue remodelling processes in which platelets are involved
-
-
-
Proteins
?
show the reaction diagram
-
may play a role in retaining prolyl 4-hydroxylase in its native conformation
-
-
-
Proteins
?
show the reaction diagram
-
plays a role in the formation of disulfide bonds during biosynthesis of wheat storage proteins
-
-
-
Proteins
?
show the reaction diagram
-
implicated in the biosynthesis of secretory proteins
-
-
-
Proteins
?
show the reaction diagram
-
implicated in the biosynthesis of secretory proteins
-
-
-
Proteins
?
show the reaction diagram
-
implicated in the biosynthesis of secretory proteins
-
-
-
Proteins
?
show the reaction diagram
-
when present in large stoichiometric excess relative to an unfolded protein substrate, the enzyme can exhibit chaperone activity, inhibiting aggregation and increasing the recovery of native protein
-
-
-
reduced bovine pancreatic trypsin inhibitor
oxidized bovine pancreatic trypsin inhibitor
show the reaction diagram
O97451, O97452, Q9U015
gPDI-2, no cativity with gPDI-1 and gPDI-3
-
?
reduced ribonuclease
?
show the reaction diagram
-
refolding of reduced ribonuclease in presence of glutathione, isomerase activity of PDI
-
-
?
reduced RNase A
RNase A
show the reaction diagram
Q9GPH2
-
-
-
?
refolding of RNase
?
show the reaction diagram
-
renaturation of reduced RNase
-
-
?
rhodanese
?
show the reaction diagram
-
chaperone activity
-
-
?
rhodanese
?
show the reaction diagram
-
prevention of rhodanese degeneration, chaperone activity
-
-
?
rhodanese
?
show the reaction diagram
-
the protein substrate is devoid of disulfide bonds, chaperone activity
-
-
?
rhodanese
?
show the reaction diagram
Saccharomyces cerevisiae trg1/TRG1
-
prevention of rhodanese degeneration, 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
?
show the reaction diagram
-
refolding of ribonuclease, isomerase activity, renaturation of reduced ribonuclease, in presence of GSH and GSSG
-
-
?
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
-
-
?
ricin
?
show the reaction diagram
-
reductive activation of ricin and ricin A-chain immunotoxins, assay system involving thioredoxin reductase and NADPH, overview
-
-
?
ricin A-chain immunotoxins
?
show the reaction diagram
-
reductive activation of ricin and ricin A-chain immunotoxins, assay system involving thioredoxin reductase and NADPH, overview
-
-
?
RNase
?
show the reaction diagram
-
refolding of RNase, renaturation of reduced and of scrambled RNase with almost equal activity
-
-
?
RNase
?
show the reaction diagram
-
refolding of RNase, renaturation of reduced bovine pancreatic RNase
-
-
?
RNase A
?
show the reaction diagram
-
-
-
-
?
RNase A
?
show the reaction diagram
-
reduced and denatured substrate from bovine pancreas
-
-
?
RNase A
?
show the reaction diagram
-
reduced and denatured substrate, oxidase/isomerase activity on the refolding of the substrate
-
-
?
RNase A
?
show the reaction diagram
-
reconstitution of the Ero1-Lalpha/protein disulfide isomerase oxidative folding system in vitro. The a' domain of protein disulfide isomerase is much more active than the a domain in Ero1-Lalpha-mediated folding. The minimal element for binding to Ero1-Lalpha are core element b, linker x and the a domain
-
-
?
RNase A
?
show the reaction diagram
-
PDI catalyzes the refolding of denatured bovine RNase A. The protein disulfide isomerase exhibits a saturable, substrate binding site. NMR structural analysis of peptide binding pocket of b and b' domains, overview
-
-
-
RNase A
?
show the reaction diagram
-
oxidase activity of PDI
-
-
?
RNase A
?
show the reaction diagram
-
PDI exhibits isomerase activity with RNase A
-
-
?
RNase A + DTT
?
show the reaction diagram
A5LHV9, A5LHW0, A5LHW1, -
the enzyme contains a WCGHCK active site
-
-
?
RNase A + DTT
?
show the reaction diagram
A5LHV9, A5LHW0, A5LHW1, -
the enzyme contains a WCGHCQ active site
-
-
?
RNase B
?
show the reaction diagram
P30101
the ability of the ERp57-calnexin complex to mediate folding of 3H-labeled RNase B is completely dependent on a functional interaction between ERp57 and calnexin, overview
-
-
?
scrambled reoxidized lysozyme
?
show the reaction diagram
-
isomerase activity of PDI
-
-
?
scrambled RNAse
?
show the reaction diagram
A7YBW7, A7YBX0, A7YBX2, A7YBX4, -
-
-
-
?
scrambled RNase A
RNase A
show the reaction diagram
Q9GPH2
-
-
-
?
TAMRAX3CX4CX2-CONH2
?
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
-
PDI switches tissue factor from coagulation to signaling by targeting the allosteric Cys186-Cys209 disulfide, the tissue factor coagulant function is enhanced by protein-disulfide isomerase independent of oxidoreductase activity, the chaperone activity is sufficient, PDI enhances factor VIIa-dependent substrate factor X activation 5-10fold in the presence of wild-type, oxidized soluble TF but not TF mutants that contain an unpaired Cys186 or Cys209, PDI has no effect on fully active TF on either negatively charged phospholipids or in activating detergent, indicating that PDI selectively acts upon cryptic TF to facilitate ternary complex formation and macromolecular substrate turnover, overview, recombinant wild-type and mutant TFs expressed in Escherichia coli, PDI is a functional oxidoreductase and exhibits both protein disulfide isomerase and chaperone activity, PDI facilitates ternary complex formation and substrate Turnover, overview
-
-
?
tyramine-S-S-poly(D-lysine)
tyramine-SH + HS-poly(D-lysine)
show the reaction diagram
-
-
-
?
unfolded acidic phospholipase A2
refolded acidic phospholipase A2
show the reaction diagram
-
PDI at a molar ratio to acidic phospholipase A2 of 0.1 increases the reactivation of reduced and denatured acidic phospholipase A2 from 4% to 15%
-
?
unfolded bovine pancreatic ribonuclease A + oxidized glutathione
refolded bovine pancreatic ribonuclease A + reduced glutathione
show the reaction diagram
-
oxidative folding of RNase A, 12fold rate acceleration in the presence of PDI
-
?
unfolded bovine pancreatic trypsin inhibitor
refolded bovine pancreatic trypsin inhibitor
show the reaction diagram
-
-
-
?
unfolded bovine pancreatic trypsin inhibitor
refolded bovine pancreatic trypsin inhibitor + oxidized glutathione
show the reaction diagram
-
oxidative refolding of denatured bovine pancreatic trypsin inhibitor
-
?
unfolded bovine pancreatic trypsin inhibitor
folded bovine pancreatic trypsin inhibitor
show the reaction diagram
O97451, O97452, Q9U015
-
-
?
unfolded disulfide-bonded protein
refolded disulfide-bonded protein
show the reaction diagram
-
-
-
?
unfolded insulin
refolded insulin
show the reaction diagram
-
-
-
?
unfolded insulin
folded insulin
show the reaction diagram
O97451, O97452, Q9U015
-
-
?
unfolded insulin + reduced glutathione
refolded insulin + oxidized glutathione
show the reaction diagram
-
-
-
?
unfolded insulin beta-chain
refolded insulin beta-chain
show the reaction diagram
-
-
-
?
unfolded lysozyme
refolded lysozyme
show the reaction diagram
-
oxidative refolding of reduced and denatured lysozyme in glutathione redox buffer
-
?
unfolded mitochondrial malate dehydrogenase
refolded mitochondrial malate dehydrogenase
show the reaction diagram
-
maximum refolding when the PDI concentration is 20fold higher than the malate dehydrogenase concentration
-
?
unfolded pro-carboxypeptidase Y
refolded pro-carboxypeptidase Y
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
refolded RNase
show the reaction diagram
-
-
-
?
unfolded RNase
refolded RNase
show the reaction diagram
-
-
-
?
unfolded RNase
refolded RNase
show the reaction diagram
-
-
-
?
unfolded RNase
refolded RNase
show the reaction diagram
-
-
-
?
unfolded RNase
refolded RNase
show the reaction diagram
O97451, O97452, Q9U015
-
-
?
unfolded RNase
refolded RNase
show the reaction diagram
-
oxidative folding of RNase
-
?
unfolded RNase
refolded RNase
show the reaction diagram
P07237
PDI is a multifunctional enzyme that acts as a subunit in prolyl 4-hydroxylases and the microsomal triglyceride transfer protein, and as a chaperone that binds various peptides and assists their folding
-
?
unfolded RNase A
refolded RNase A
show the reaction diagram
-
-
-
?
unfolded RNase A
refolded RNase A
show the reaction diagram
-
-
-
?
unfolded RNase A
refolded RNase A
show the reaction diagram
-
-
-
?
unfolded RNase A
refolded RNase A
show the reaction diagram
-
-
-
?
unfolded RNase A
refolded RNase A
show the reaction diagram
-
all five consecutive PDI domains, a-b-b'-a'-c are necessary for PDI's disulfide isomerase and chaperone activity
-
?
unfolded RNase A
refolded RNase A
show the reaction diagram
-
PDI binds to DNA and may be involved in DNA-nuclear matrix anchoring
-
?
unfolded RNase A
refolded RNase A
show the reaction diagram
-
PDI catalyzes disulfide isomerization of misfolded, i.e. scrambled RNaseA into native RNase A
-
?
unfolded RNase A
refolded RNase A
show the reaction diagram
-
PDI catalyzes disulfide isomerization of misfolded, i.e. scrambled RNaseA into native RNase A
-
?
unfolded RNase A
refolded RNase A
show the reaction diagram
-
PDI functions in a plasma environment
-
?
unfolded RNase A
refolded RNase A
show the reaction diagram
-
reduced and denatured bovine pancreatic RNase A, glutathione redox buffer, PDI catalyzes the entire RNase A folding by enhancing the formation and reduction of mixed disulfides with glutathione and the formation of intramolecular disulfides
-
?
unfolded RNase A
refolded RNase A
show the reaction diagram
-
tyrosine and tryptophane residues in peptides are the recognition motifs for their binding
-
?
unfolded RNase A
refolded RNase
show the reaction diagram
-
-
-
?
unfolded RNase A + reduced glutathione
refolded RNase A + oxidized glutathione
show the reaction diagram
-
-
-
?
unfolded rRNaSe
refolded rRNase
show the reaction diagram
-
refolding of reduced rRNaSe
-
?
unofolded bovine pancreatic ribonuclease A + oxidized dithiothreitol
refolded bovine pancreatic ribonuclease A + reduced dithiothreitol
show the reaction diagram
-
oxidative folding of RNase A
-
?
vitronectin + thrombin + antithrombin
vitronectin-thrombin-antithrombin
show the reaction diagram
-
PDI catalyzes the formation of disulfide-linked complexes of vitronectin with thrombin-antithrombin
-
?
lysozyme
?
show the reaction diagram
-, Q1HGL1
PDI exhibits both chaperone and antichaperone activities when catalyzing the refolding of reduced/denatured lysozyme in HEPES buffer, effect of macromolecular crowding on the PDI-catalyzed folding, overview
-
-
?
additional information
?
-
-
-
-
-
-
additional information
?
-
-
3,3',5-triiodo-L-thyronine-binding activity
-
-
-
additional information
?
-
-
PDI is a subunit of the enzyme prolyl-4-hydroxylase, which catalyzes the formation of 4-hydroxyprolyl residues in nascent collagen-like polypeptides. PDI is also a subunit of a triacylglycerol transfer protein, which facilitates the incorporation of lipids into newly synthesized core lipoproteins within the endoplasmic reticulum. The function of PDI is to maintain the alpha-subunit of this enzyme in an active form
-
-
-
additional information
?
-
-
the enzyme has an essential role that is distinct from its function in formation of native disulphides
-
-
-
additional information
?
-
-
the enzyme acts as a thyroid-hormone binding protein
-
-
-
additional information
?
-
-
the enzyme may be significant in the action of triiodothyronine towards the target cells
-
-
-
additional information
?
-
-
protein disulfide isomerase serves as a subunit of at least two enzymes, the beta-subunit of the enzyme prolyl hydroxylase and an ER triglyceride transferase
-
-
-
additional information
?
-
-
both chaperone and isomerase functions of PDI are essential for acceleration of the oxidative refolding and reactivation of dimeric alkaline protease inhibitor API, PDI acts as isomerase/chaperone for a few monomeric proteins assisting in disulfide bond formation and rearrangement of secreted proteins
-
-
-
additional information
?
-
-
DsbA and DsbC are involved in disulfide bond formation and play an important role in the formation of extracellular enzymes, DsbA is important in lipase stability and excretion
-
-
-
additional information
?
-
-
DsbC resolves incorrect disulfides whose formation has been catalyzed by redox-active copper
-
-
-
additional information
?
-
-
essential enzyme for yeast cell growth, both oxidase and isomerase activities are required
-
-
-
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
?
-
-
modeling of disulfide formation, the enzyme catalyzes disulfide formation and isomerization and acts as a chaperone inhibiting aggregation, enzyme assists in the system of chaperones and folding catalysts to ensure proper connection of disulfides and protein folding without improper interactions, mechanism of incorrect disulfide recognition
-
-
-
additional information
?
-
-
modeling of disulfide formation, the enzyme catalyzes disulfide formation and isomerization and acts as a chaperone inhibiting aggregation, enzyme assists in the system of chaperones and folding catalysts to ensure proper connection of disulfides and protein folding without improper interactions, the pancreatic enzyme is responsible for folding of a subset of secreted pancreatic zymogens
-
-
-
additional information
?
-
-
PDI plays a key role in catalyzing the folding of secretory proteins
-
-
-
additional information
?
-
-
PDILT forms intermolecular disulfide bonds in testis
-
-
-
additional information
?
-
-
RB60 is an atypical PDI that functions as a member of a redox regulatory protein complex controlling translation in the chloroplast, the enzyme is essential in the endoplasmic reticulum
-
-
-
additional information
?
-
-
regulation of PDI and PDI homologues activities, in vivo isomerase activity depends only on full-length PDI, not on PDI-homologues, modeling of disulfide formation, the enzyme catalyzes disulfide formation and isomerization and acts as a chaperone inhibiting aggregation, enzyme assists in the system of chaperones and folding catalysts to ensure proper connection of disulfides and protein folding without improper interactions
-
-
-
additional information
?
-
-
the enzyme catalyzes disulfide formation and isomerization and acts as a chaperone inhibiting aggregation, enzyme assists in the system of chaperones and folding catalysts to ensure proper connection of disulfides and protein folding without improper interactions
-
-
-
additional information
?
-
-
the enzyme is an essential catalyst of disulfide formation with two cysteines in the active site facilitating thiol-disulfide exchange
-
-
-
additional information
?
-
-
the enzyme plays a crucial role in folding periplasmatically excreted proteins
-
-
-
additional information
?
-
-
the organism is completely dependent on PDI activity for growth
-
-
-
additional information
?
-
P12865, -
the single domain PDI-1 and the class 1 PDI-2 are not essential for the organism
-
-
-
additional information
?
-
-
all 5 domains of PDI are required for full catalytic activity
-
-
-
additional information
?
-
-
Cys98 and Cys101 form the reversible disulfide bond in the active site, the enzyme is active in reduced state which is stabilized by hydrogen bond interactions of the active cysteine residues with Thr94 and Thr182
-
-
-
additional information
?
-
-
DsbC and DbsG also possess thioredoxin-like domains, substrate specificity of PDI
-
-
-
additional information
?
-
-
Eug1p, Mpd1p, Mpd2p, and Eps1p partially compensate for PDI, substrate specificity of PDI
-
-
-
additional information
?
-
-
isomerase activity is assayed using the insulin/glutathione coupled assay
-
-
-
additional information
?
-
-
non-active site cysteines form a disulfide bridges which destabilizes the N-terminal active site disulfide rendering it a 18fold better oxidant by this way
-
-
-
additional information
?
-
-
PDI is a better thiol oxidant than a disulfide protein reductant
-
-
-
additional information
?
-
-
PDILT forms intermolecular disulfide bonds, but shows no intramolecular disulfide bonds
-
-
-
additional information
?
-
-
substrate disulfide bonds, overview, the AppA homologue Agp, a periplasmic phosphatase, lacks nonconsecutive disulfide bonds and is no substrate for DsbC
-
-
-
additional information
?
-
-
substrate specificity of PDI
-
-
-
additional information
?
-
-
the enzyme catalyzes dithiol-disulfide exchange reactions with an essential -C-P-Y-C- active site motif with catalytic C35 and C146, enzyme shows oxidative, reductive, and isomerase activities as well as ATPase activity, the latter being related to the enzyme's chaperone function
-
-
-
additional information
?
-
-
the four domains a, b, b', and a' show cooperative properties in both isomerase and chaperone functions of PDi
-
-
-
additional information
?
-
P12865, -
the single domain PDI-1 and the class 1 PDI-2 of the organism both posses isomerase activity, but only the single domain PDI has reducing activity
-
-
-
additional information
?
-
-
the yPDI enzyme family members Mpd1p, Mpd2p, and Eug1p show high chaperone activity, but low isomerase activity compared to PDI, isomerase activity is assayed using the insulin/glutathione coupled assay, chaperone activity is also measured utilizing mastoparan as substrate
-
-
-
additional information
?
-
P04785
cell-surface PDI is required for transnitrosation of metallothionein by S-nitroso-albumin in intact pulmonary vascular endothelial cells, overview
-
-
-
additional information
?
-
-
DsbB is an integral membrane protein responsible for the de novo synthesis of disulfide bonds in the Escherichia coli periplasm, disulfide bond formation is catalyzed by the DsbA/DsbB system, DsbA is critical for catalyzing disulfide bond formation in proteins in the bacterial periplasm, which it accomplishes by directly oxidizing substrate proteins via dithiol-disulfide exchange, DsbA donates its disulfide bond directly to substrate proteins, in the process of transferring electrons from DsbA to a tightly bound ubiquinone cofactor, DsbB undergoes an unusual spectral transition, DsbA must be reoxidized by an electron acceptor, mechanism, overview
-
-
-
additional information
?
-
A5LHV9, A5LHW0, A5LHW1, -
HlPDI-1 might be involved in tick blood feeding and Babesia parasite infection in ticks
-
-
-
additional information
?
-
A5LHV9, A5LHW0, A5LHW1, -
HlPDI-3 might be involved in tick blood feeding and Babesia parasite infection in ticks
-
-
-
additional information
?
-
-, Q1HGL1
in vivo, disulfide bond formation is mainly catalyzed by protein disulfide isomerase
-
-
-
additional information
?
-
A0SHR2, -
PDI has an important function in the correct folding of nascent polypeptides, which is a crucial step in the mechanism which delivers tick proteins to the secretion pathway important for blood feeding
-
-
-
additional information
?
-
-
PDI has two distinct functions: acting as a molecular chaperone to maintain properly folded proteins and regulating the redox state of proteins by catalyzing the thiol-disulfide exchange reaction through two thioredoxin-like domains
-
-
-
additional information
?
-
A3RMS2, -
PDI is a multifunctional protein required for many aspects of protein folding and transit through the endoplasmic reticulum, the PDI activity is essential for viability, collagen biogenesis and extracellular matrix formation, overview, all isozymes are synergistically essential for embryonic development in this nematode
-
-
-
additional information
?
-
A3RMS2, -
PDI is a multifunctional protein required for many aspects of protein folding and transit through the endoplasmic reticulum, the PDI activity is essential for viability, collagen biogenesis and extracellular matrix formation, PDI-2 is required for the normal function of prolyl 4-hydroxylase, a key collagen-modifying enzyme, overview, PDI-2 is required for normal post-embryonic development, all isozymes are synergistically essential for embryonic development in this nematode
-
-
-
additional information
?
-
-
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
?
-
O13811, -
PDI is involved in the cellular growth and response to nutritional and oxidative stress, regulation, overview
-
-
-
additional information
?
-
-
PDI oxidizes pairs of cysteines to form disulfide bonds and can also shuffle incorrect disulfides into their correct pairings, function and mechanism of PDI, bacterial machinery for disulfide formation and oxidative protein folding, overview
-
-
-
additional information
?
-
P30101
PDIis responsible for correct disulfide bond formation of proteins in the endoplasmic reticulum, it recognize unfolded proteins and can be selective for specific proteins or classes
-
-
-
additional information
?
-
-
RB60 is involved in the light-regulated translation of the psbA mRNA in the chloroplast of the unicellular alga Chlamydomonas reinhardtii, light controls the redox regulation of RB47 function via the coupling of RB47 and RB60 redox states, overview
-
-
-
additional information
?
-
-
sperm surface protein disulfide isomerase activity plays a role in gamete fusion and sperm-egg interaction, the enzyme mediates conformational changes by thiol-disulfide exchange in fusion-active proteins, participation of ERp57, overview
-
-
-
additional information
?
-
-
structure and mechanism of PDI in disulfide formation and oxidative protein folding, overview
-
-
-
additional information
?
-
P17967
structure and mechanism of PDI in disulfide formation and oxidative protein folding, overview
-
-
-
additional information
?
-
-
structure and mechanism of PDI in disulfide formation and oxidative protein folding, overview
-
-
-
additional information
?
-
Q93YN0
the cotyledon-specific chloroplast biogenesis factor CYO1 is a protein disulfide isomerase and has a chaperone-like activity required for thylakoid biogenesis in cotyledons, mutation of Cyo1 affects the photosynthesis in cotyledons, overview
-
-
-
additional information
?
-
-
the enzyme assists protein folding in malaria parasites
-
-
-
additional information
?
-
Q2XQR3
the enzyme assists protein folding in malaria parasites
-
-
-
additional information
?
-
-, Q2XQR5
the enzyme assists protein folding in malaria parasites
-
-
-
additional information
?
-
Q4Z2V7
the enzyme assists protein folding in malaria parasites
-
-
-
additional information
?
-
Q7RRT0
the enzyme assists protein folding in malaria parasites
-
-
-
additional information
?
-
P07237, P13667, P30101, Q13087
the enzyme is involved in correct disulfide bond formation in secretory proteins as a key step in endoplasmic reticulum quality control, ERp57 works in conjunction with the endoplasmic reticulum lectin-like chaperones calnexin and calreticulin via the noncatalytic b' domain of the enzyme, the b' domains of ERp57 and PDI are very different, overview
-
-
-
additional information
?
-
-
the enzyme is involved in diphtheria toxin sensitivity and is required for toxin entry, Chlamydia trachomatis or Chlamydia psittaci, intracellular pathogens of humans, require the enzyme for attachment to mammalian CHO6 cells, host cell invasion is obligatory for survival, growth and pathogenesis, overview
-
-
-
additional information
?
-
-
the enzyme is involved in the oxidative folding of cystine knot defense proteins and in in the biosynthesis of insecticidal cyclotides, overview, the Oldenlandia affinis plant accumulates knotted circular proteins called cyclotides
-
-
-
additional information
?
-
-
the enzyme mediates rapid delivery of NO signalling into human platelets from the S-nitrosothiol compound S-nitrosoglutathione, NO delivery is blocked by inhibition of PDI, overview
-
-
-
additional information
?
-
-
the enzyme plays important roles in the folding of nascent polypeptides and the formation of disulfide bonds in the endoplasmic reticulum, PDIS-1 associates with proglycinin, a precursor of the seed storage protein glycinin, in the cotyledon, seed-dependent aggregation of amyloid beta-peptide (1-40) monomers is inhibited by both PDIS-1 and PDIS-2, both are involved in seed development, overview
-
-
-
additional information
?
-
Q96DN0
ERp27 is non-catalytic and interacts with ERp57, ERp57 binds ERp27 by the Asp-Glu-Trp-Asp sequence in domain 2, reduced binding to R280A mutant ERp57, overview, it binds DELTA-somatostatin, the standard test peptide for protein disulfide isomerase-substrate binding, at its second domain, a significant conformational change in the b'-like domain of ERp27 occurs upon substrate binding, overview
-
-
-
additional information
?
-
P30101
ERp57 interacts with the lectin chaperone calnexin, binding structure, and active site structure, overview
-
-
-
additional information
?
-
-
kinetic cycle of DsbB, thew enzyme uses a tightly bound ubiquinone cofactor, which becomes oxidized to hydroquinone and is regenerated by the electron transport chain and O2, overview
-
-
-
additional information
?
-
-
PDI also functions as a dehydroascorbate reductase and a molecular chaperone besides its disulfide-isomerizing function
-
-
-
additional information
?
-
-
PDI has the ability to catalyze dithiol-disulfide exchange reactions, chaperone activity and propensity to form subunits of multi-enzyme complexes, overview
-
-
-
additional information
?
-
-
PDI interacts with the cyclotide precursor protein Oak1, PDi is a functional oxidoreductase and exhibits both protein disulfide isomerase and chaperone activity, properties of disulfide species, overview
-
-
-
additional information
?
-
-
PDI oxidizes pairs of cysteines to form disulfide bonds and can also shuffle incorrect disulfides into their correct pairings, function and mechanism of PDI, PDI has the ability to catalyze dithiol-disulfide exchange reactions, chaperone activity and propensity to form subunits of multi-enzyme complexes, overview
-
-
-
additional information
?
-
P17967
PDI oxidizes pairs of cysteines to form disulfide bonds and can also shuffle incorrect disulfides into their correct pairings, function and mechanism of PDI, PDI has the ability to catalyze dithiol-disulfide exchange reactions, chaperone activity and propensity to form subunits of multi-enzyme complexes, overview
-
-
-
additional information
?
-
-
PDI oxidizes pairs of cysteines to form disulfide bonds and can also shuffle incorrect disulfides into their correct pairings, function and mechanism of PDI, PDI has the ability to catalyze dithiol-disulfide exchange reactions, chaperone activity and propensity to form subunits of multi-enzyme complexes, overview
-
-
-
additional information
?
-
-
PDIS-1 and PDIS-2 show both an oxidative refolding activity of denatured ribonuclease A and a chaperone activity, PDIS-1 and PDIS-2 both possess a putative N-terminal secretory signal sequence and two tandem thioredoxin-like motifs, with a CGHC active site
-
-
-
additional information
?
-
-
RB60 binds to RB47 and modulates its activity via redox and phosphorylation events, RB60 attacks the disulfide bond Cys143-Cys259 of RB47, the redox states of the protein redox partners are coupled, overview, recombinant His-tagged RB47 expressed in Escherichia coli
-
-
-
additional information
?
-
P07237, P13667, P30101, Q13087
the enzyme catalyzes the oxidation, reduction, and isomerization of secretory proteins and plasma membrane proteins, substrate specificity, the enzyme contains a WCGHC active site, overview
-
-
-
additional information
?
-
-
the enzyme is a potent oxido-reductase and facilitates the disulfide-dependent conformational folding of EBA-175, the enzyme contain two CGHC active sites within two thioredoxin domains
-
-
-
additional information
?
-
Q2XQR3
the enzyme is a potent oxido-reductase and facilitates the disulfide-dependent conformational folding of EBA-175, the enzyme contain two CGHC active sites within two thioredoxin domains
-
-
-
additional information
?
-
-, Q2XQR5
the enzyme is a potent oxido-reductase and facilitates the disulfide-dependent conformational folding of EBA-175, the enzyme contain two CGHC active sites within two thioredoxin domains
-
-
-
additional information
?
-
Q4Z2V7
the enzyme is a potent oxido-reductase and facilitates the disulfide-dependent conformational folding of EBA-175, the enzyme contain two CGHC active sites within two thioredoxin domains
-
-
-
additional information
?
-
Q7RRT0
the enzyme is a potent oxido-reductase and facilitates the disulfide-dependent conformational folding of EBA-175, the enzyme contains two CGHC active sites within two thioredoxin domains
-
-
-
additional information
?
-
-
the enzyme mediates conformational changes by thiol-disulfide exchange
-
-
-
additional information
?
-
-
the enzyme shows disulfide exchange activity
-
-
-
additional information
?
-
-
the enzyme shows disulfide oxidase/isomerase, reductase, and chaperone activities, overview
-
-
-
additional information
?
-
-
the enzyme shows disulfide reduction and chaperone activities and contains a WCGHC active site, overview, tertiary structure and function analysis under pressure conditions above 100 MPa, overview
-
-
-
additional information
?
-
-
the enzyme shows disulfide reduction and chaperone activities, it facilitates the folding of secreted proteins with multiple disulfide bonds by catalyzing disulfide-bond rearrangement
-
-
-
additional information
?
-
A0SHR2, -
the enzyme shows dithiol-disulfide-oxidoreductase activity, and contains a conserved WCGHC active site and two thioredoxin domains
-
-
-
additional information
?
-
-
the enzyme shows hormone binding activity, e.g. of L-T3 and 17beta-estradiol hormones
-
-
-
additional information
?
-
-, Q1HGL1
the enzyme shows oxidase and isomerase activities, overview
-
-
-
additional information
?
-
-
enzyme is involved in the proper folding or quality control of storage proteins
-
-
-
additional information
?
-
-
PDI can function as a high-capacity intracellular 17beta-estradiol-binding protein that increases the concentration and accumulation of 17beta-estradiol in live cells. The intracellular PDI-bound 17beta-estradiol can be released from PDI upon a drop in 17beta-estradiol levels and the released 17beta-estradiol can augment estrogen receptor-mediated transcriptional activity and mitogenic actions in cultured cells. The binding of 17beta-estradiol by PDI also reduces the rate of metabolic disposition of this hormone
-
-
-
additional information
?
-
-
PDI is required in vivo for both fibrin generation and platelet thrombus formation
-
-
-
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
?
-
-
protein disulfide isomerase contributes to the activation of cryptic initiator protein tissue factoron microvesicles in vitro
-
-
-
additional information
?
-
-
protein disulfide isomerase directly promotes initiator protein tissue factor-dependent fibrin production during thrombus formation in vivo
-
-
-
additional information
?
-
-
protein disulfide isomerase PDI directly interacts with thiol-containing fibrinogen receptor alphaIIbbeta3. PDI has greater ability to isomerize disulfide bonds than the alphaIIbbeta3 integrin
-
-
-
additional information
?
-
A5LHV9, A5LHW0, A5LHW1, -
protein disulfide isomerases are involved in blood feeding, viability and oocyte development, probably by mediating the formation of disulfide bond-containing proteins of the ticks and the formation of basement membrane and cuticle components such as extracellular matrix
-
-
-
additional information
?
-
-
enzyme converts initiator protein tissue factor cysteine residues from glutathionylated to disulfide state
-
-
-
additional information
?
-
-
in vivo, protein disulfide isomerase is present in two semi-oxidized forms in which either the first active site in the a domain or the second active site in the a' domain is oxidized. In HEK-293 cells, about 50% of enzyme is fully reduced, in 18% a domain is oxidized, a' reduced, in 15%, the a domain is reduced, a' oxidized, and 16% of enzyme are fully oxidized
-
-
-
additional information
?
-
-
PDI enhances factor X activation by factor VIIa soluble tissue factor in a dose-dependent manner. The inclusion of annexin V or detergent abolishes the stimulation effect. The presence of 25 nM bovine PDI lowers the apparent Km of factor VIIa for factor X from far above 0.01 mM to 0.001-0.002 mM
-
-
-
additional information
?
-
-
presence of protein disulfide isomerase on the surface of platelet-derived microparticles. Enzyme is catalytically active and capable of both promoting platelet aggregation and disrupting insulin signaling. Platelet-derived microparticles increase the initial rates of aggregation by 4fold and the pro-aggregatory activity of micrparticles can be attenuated with an anti-PDI antibody. Anti-PDI antibodies are able to block the degradation of insulin, thereby restoring insulin signaling
-
-
?
additional information
?
-
-
protein disulfide isomerase has a concentration-dependent chaperone-activity and inhibits the aggregation of rhodanese, which has no disulfide bonds
-
-
-
additional information
?
-
-
recombinant human PDI does not influence factor X activation by factor VIIa soluble tissue factor
-
-
-
additional information
?
-
-
reduced protein disulfide isomerase activates initiator protein tissue factor by isomerzation of a mixed disulfide and a free thiol to an intramolecular disulfide
-
-
-
additional information
?
-
-
the nucleophilic C36 thiol of the protein disulfide isomerase a domain is positioned over the N-terminus of the alpha2 helix. The H38 amide in the reduced enzyme exhibits a maximum rate of exchange at pH 5 due to efficient general base catalysis by the neutral imidazole of its own side chain and suppression of its exchange by the ionization of the C36 thiol. Ionization of this thiol and deprotonation of the H38 side chain suppress the C39 amide hydroxide-catalyzed exchange by a million-fold. The electrostatic potential within the active site stabilizes the two distinct transition states that lead to substrate reduction and oxidation
-
-
-
additional information
?
-
Q13087
PDIp also shows chaperone activity in preventing the aggregation of reduced insulin B chain and denatured D-glyceraldehyde-3-phosphate dehydrogenase, PDIp can form stable complexes with thermal-denatured substrate proteins, e.g. MCF-7 cellular proteins, independently of their enzymatic activity. The b-b' fragment of PDIp, which does not contain the active sites and is devoid of enzymatic activity, still has chaperone activity
-
-
-
additional information
?
-
-
AGR2 is essential for production of intestinal mucin MUC2, but is not required for establishment of intestinal secretory epithelial cell lineages
-
-
-
additional information
?
-
-
ER protein 57, ERP-57, also known as PDIA3, has disulfide oxidoreductase and isomerase activity. ERP-57 interacts with calnexin, CANX, a chaperone protein and a lectin that binds glycoproteins through a transient oligosaccharide intermediate, thought to prevent a rapid degradation, as well as endoplasmic reticulum retention, of misfolded proteins, overview
-
-
-
additional information
?
-
-
GmPDIL-1 and GmPDIL-2 function as molecular chaperones, and prevent the aggregation of unfolded rhodanese, while GmPDIL-3a and GmPDIL-3b do not
-
-
-
additional information
?
-
-
interactions between the C-terminal domain of Mnl1p and PDI, which include an intermolecular disulfide bond, are essential for subsequent introduction of a disulfide bond into the mannosidase homology domain of Mnl1p by PDI. This disulfide bond is essential for the ER-associated degradation activity of Mnl1p and in turn stabilizes the prolonged association of PDI with Mnl1p
-
-
-
additional information
?
-
-
PDI catalyzes disulfide bond formation in the endoplasmic reticulum
-
-
-
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
?
-
P55059
PDI is a major protein in the endoplasmic reticulum, operating as an essential folding catalyst and molecular chaperone for disulfide-containing proteins by catalyzing the formation, rearrangement, and breakage of their disulfide bridges
-
-
-
additional information
?
-
-
PDI is able to renature reduced-denatured RNase. Plasma transglutaminase-coagulation factor XIII, FXIII, also shows PDI activity with reduced-denatured RNase, its PDI activity is located on the A subunit
-
-
-
additional information
?
-
-
PDI specifically associates with signal peptide peptidase, SPP, independently of human cytomegalovirus glycoprotein US2, but not with Derlin-1
-
-
-
additional information
?
-
-
PDI specifically binds 3,3',5-triiodo-L-thyronine
-
-
-
additional information
?
-
-
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
?
-
P27773
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
?
-
E1CAJ6
PDIA3 shows chaperone activity to promote oxidative refolding of reduced denatured lysozyme, meanwhile PDI-P5 exhibits anti-chaperone activity to inhibit oxidative refolding of lysozyme at an equimolar ratio
-
-
-
additional information
?
-
-
the oxidoreductase chaperone PDI has an effect on the critical structure-forming step during the oxidative maturation of model disulfide-bond-containing proteins, it inhibits the conformational folding step of oxidative fold maturation and, therefore, has limited overall catalytic efficiency as an oxidoreductase chaperone, impact of rat PDI, null PDI and enzyme domains on the structure-forming step, overview. Detrimental impact of the oxidoreductase activity PDI during conformational folding include peptidyl prolyl isomerase which facilitates cis-trans isomerization of prolines
-
-
-
additional information
?
-
-
the PDI protein is necessary for Chlamydia attachment, but the bacteria apparently do not bind directly to cell-associated PDI, suggesting that Chlamydia attaches to a host protein(s) associated with PDI. PDI enzymatic activity is necessary for bacterial entry but not for attachment, cell surface PDI-mediated reduction triggers Chlamydia entry into cells, molecular mechanism, overview
-
-
-
additional information
?
-
-
a cysteine residue in the thioredoxin-like domain of AGR2 forms mixed disulfide bonds with MUC2, mutational analysis of the AGR2-MUC2 interaction, overview
-
-
-
additional information
?
-
P38659, -
ERp72 substrate specificity of ERp72, overview. Ep72 does not interact with calnexin
-
-
-
additional information
?
-
Q13087
formation of active RNase from rRNase and sRNase in the presence of PDIp. The pancreas-specific PDI homolog PDIp can function independently as a chaperone in vitro and in vivo
-
-
-
additional information
?
-
-
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
?
-
-
PDI first recognizes the C-terminal domain of Mnl1p containing Asp607, Glu627, and Trp636 , PDI forms an intermolecular disulfide bond with C5 or C6 of Mnl1p. PDI introduces a disulfide bond between C1 and C3 in the MHDof Mnl1p, the disulfide bond between C1 and C3 in turn stabilizes association of PDI with Mnl1p, and the intermolecular disulfide bond between PDI and C5 or C6 of Mnl1p is partially reduced,whereas maintaining association of PDI and Mnl1p
-
-
-
additional information
?
-
-
PDI forms mixed disulfides in substrate molecules, substrates are Ero1alpha, clusterin, or PTX3, analysis of PDI substrate specificity, comparison to other members of the protein disulfide isomerase family of oxidoreductases, overview
-
-
-
additional information
?
-
-
PDI is able to renature reduced-denatured bovine pancreas RNase A. Plasma transglutaminase-coagulation factor XIII, FXIII, a plasmatic pro-transglutaminase, also shows PDI activity with reduced-denatured RNase, its PDI activity is located on the A subunit. Both FXIII and tissue transglutaminase exhibit PDI activity sdespite the fact that they lack either the essential amino acid sequence, Cys-X-X-Cys, for PDI activity or its related sequences, Cys-Leu-His-Ser or Cys-Ile-His-Ser, which have been reported to impart such activity, overview
-
-
-
additional information
?
-
-
recombinant GmPDIL-3a and GmPDIL-3b do not function as oxidoreductases or as molecular chaperones in vitro, although a proportion of each protein formed complexes in both thiol-dependent and thiol-independent ways in the endoplasmic reticulum. GmPDIL-3a and GmPDIL-3b have no stimulatory effect on the oxidative refolding of RNase A by GmPDIL-1 and GmPDIL-2 when mixed together, further confirming that the functional properties of GmPDIL-3a and GmPDIL-3b are probably unique
-
-
-
additional information
?
-
-
the active-site cysteine residues of the functional domains, Trx-domains, are essential for catalysis of disulfide bond formation in polypeptides and proteins, such as the bacterial alkaline phosphatase
-
-
-
additional information
?
-
P55059
the enzyme has a modular structure with four thioredoxin-like domains, a, b, b', and a', along with a C-terminal extension. The homologous a and a' domains contain one cysteine pair in their active site directly involved in thiol-disulfide exchange reactions, while the b' domain putatively provides a primary binding site for unstructured regions of the substrate polypeptides, mechanistic model of PDI action, overview. The a' domain transfers its own disulfide bond into the unfolded protein accommodated on the hydrophobic surface of the substrate-binding region, which consequently changes into a closed form releasing the oxidized substrate, domain arrangements and redox behaviour, overview
-
-
-
additional information
?
-
-
the enzyme renatures denatured RNase A
-
-
-
additional information
?
-
-
the enzyme's isomerase activity comprises disulfide reduction, refolding, and oxidation of thiols requiring all four thioredoxin-folded domains in tandem link plus the C-terminal acidic extension
-
-
-
additional information
?
-
E1CAJ6
the isozymes catalyze refolding of reduced and denatured lysozyme
-
-
-
additional information
?
-
-
PDI behaves mainly as an oxidase/isomerase and exhibits chaperone-like activity
-
-
-
additional information
?
-
-
PDI catalyzes the isomerization of disulfide bonds on misfolded proteins
-
-
-
additional information
?
-
-
PDI directly interacts with calreticulin
-
-
-
additional information
?
-
Q53LQ0, Q67UF5
PDIL2-3 activity is dispensable in the oxidative folding of alpha-globulin
-
-
-
additional information
?
-
-
study on the interaction of disulfide dyes 2-[(2,4-dinitrophenyl)amino]-3-sulfanylpropanoic acid and 8-[[7,12-diammonio-2-(1H-imidazo[2,1-c][1,2,4]benzotriazin-10-ium-8-yl)-6,13-dioxo-5,14-dioxa-9,10-dithia-2-azahexadecan-16-yl](methyl)amino]-1H-imidazo[2,1-c][1,2,4]benzotriazin-10-ium
-
-
-
additional information
?
-
Q4Z2V7
the enzyme assists protein folding in malaria parasites, the enzyme is a potent oxido-reductase and facilitates the disulfide-dependent conformational folding of EBA-175, the enzyme contain two CGHC active sites within two thioredoxin domains
-
-
-
additional information
?
-
Streptomyces sp. NCIM 5127
-
both chaperone and isomerase functions of PDI are essential for acceleration of the oxidative refolding and reactivation of dimeric alkaline protease inhibitor API, PDI acts as isomerase/chaperone for a few monomeric proteins assisting in disulfide bond formation and rearrangement of secreted proteins
-
-
-
additional information
?
-
Chlamydomonas reinhardtii 2137a
-
RB60 is an atypical PDI that functions as a member of a redox regulatory protein complex controlling translation in the chloroplast, the enzyme is essential in the endoplasmic reticulum
-
-
-
additional information
?
-
Plasmodium knowlesi H
Q2XQR5
the enzyme assists protein folding in malaria parasites, the enzyme is a potent oxido-reductase and facilitates the disulfide-dependent conformational folding of EBA-175, the enzyme contain two CGHC active sites within two thioredoxin domains
-
-
-
additional information
?
-
Plasmodium vivax Sal1
Q2XQR3
the enzyme assists protein folding in malaria parasites, the enzyme is a potent oxido-reductase and facilitates the disulfide-dependent conformational folding of EBA-175, the enzyme contain two CGHC active sites within two thioredoxin domains
-
-
-
additional information
?
-
Saccharomyces cerevisiae trg1/TRG1
-
the organism is completely dependent on PDI activity for growth, the yPDI enzyme family members Mpd1p, Mpd2p, and Eug1p show high chaperone activity, but low isomerase activity compared to PDI, isomerase activity is assayed using the insulin/glutathione coupled assay, chaperone activity is also measured utilizing mastoparan as substrate
-
-
-
additional information
?
-
Schizosaccharomyces pombe KP1
O13811
PDI is involved in the cellular growth and response to nutritional and oxidative stress, regulation, overview
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
alkaline protease inhibitor
?
show the reaction diagram
Streptomyces sp., Streptomyces sp. NCIM 5127
-
folding and rearrangement of alkaline protease inhibitor
-
-
?
carboxypeptidase Y
?
show the reaction diagram
-
maturation of carboxypeptidase Y
-
-
?
dehydroascorbate
ascorbate
show the reaction diagram
-
PDI has dehydroascorbate reductase activity, PDI may play a role in the intraluminal dehydroascorbate reduction
-
?
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
-
?
Proteins
?
show the reaction diagram
-
-
-
-
-
Proteins
?
show the reaction diagram
-
-
-
-
-
Proteins
?
show the reaction diagram
-
-
-
-
-
Proteins
?
show the reaction diagram
-
-
-
-
-
Proteins
?
show the reaction diagram
-
-
-
-
-
Proteins
?
show the reaction diagram
-
native, reduced or with wrong disulfide bonds
-
-
-
Proteins
?
show the reaction diagram
-
native, reduced or with wrong disulfide bonds
-
-
-
Proteins
?
show the reaction diagram
-
native, reduced or with wrong disulfide bonds
-
-
-
Proteins
?
show the reaction diagram
-
native, reduced or with wrong disulfide bonds
-
-
-
Proteins
?
show the reaction diagram
-
native, reduced or with wrong disulfide bonds
-
-
-
Proteins
?
show the reaction diagram
-
native, reduced or with wrong disulfide bonds
-
-
-
Proteins
?
show the reaction diagram
-
involved in the assembly of wheat storage proteins within the endoplasmic reticulum
-
-
-
Proteins
?
show the reaction diagram
-
proposed physiological role as catalyst of formation of native disulfide bonds in nascent and newly synthesized secretory proteins
-
-
-
Proteins
?
show the reaction diagram
-
facilitates the formation of the correct disulfide bonds within newly synthesized polypeptides
-
-
-
Proteins
?
show the reaction diagram
-
catalyzes disulfide cleavage in membrane-bound diphtheria toxin or the membrane-bound conjugate, iodotyramine conjugated with poly(D-Lys) via a 3,3'-dithiobis(propionic acid) spacer
-
-
-
Proteins
?
show the reaction diagram
-
enzyme may play a physiological role in the catalysis of S-S-bond formation in prolactin
-
-
-
Proteins
?
show the reaction diagram
-
enzyme may be involved in the formation of intra-chain and inter-chain disulfide bonds in procollagen
-
-
-
Proteins
?
show the reaction diagram
-
involved in cotranslational disulfide bond formation
-
-
-
Proteins
?
show the reaction diagram
-
may play a role in the formation of disulfide bonds in extracellular and periplasmic proteins
-
-
-
Proteins
?
show the reaction diagram
-
facilitates the formation of disulfides during the folding and processing of membrane and secretory proteins
-
-
-
Proteins
?
show the reaction diagram
-
catalysis of native disulfide bond formation
-
-
-
Proteins
?
show the reaction diagram
-
platelet enzyme may play a role in the various haemostatic and tissue remodelling processes in which platelets are involved
-
-
-
Proteins
?
show the reaction diagram
-
may play a role in retaining prolyl 4-hydroxylase in its native conformation
-
-
-
Proteins
?
show the reaction diagram
-
plays a role in the formation of disulfide bonds during biosynthesis of wheat storage proteins
-
-
-
Proteins
?
show the reaction diagram
-
implicated in the biosynthesis of secretory proteins
-
-
-
Proteins
?
show the reaction diagram
-
implicated in the biosynthesis of secretory proteins
-
-
-
Proteins
?
show the reaction diagram
-
implicated in the biosynthesis of secretory proteins
-
-
-
Proteins
?
show the reaction diagram
-
when present in large stoichiometric excess relative to an unfolded protein substrate, the enzyme can exhibit chaperone activity, inhibiting aggregation and increasing the recovery of native protein
-
-
-
tissue factor
?
show the reaction diagram
-
PDI switches tissue factor from coagulation to signaling by targeting the allosteric Cys186-Cys209 disulfide, the tissue factor coagulant function is enhanced by protein-disulfide isomerase independent of oxidoreductase activity, the chaperone activity is sufficient, PDI enhances factor VIIa-dependent substrate factor X activation 5-10fold in the presence of wild-type, oxidized soluble TF but not TF mutants that contain an unpaired Cys186 or Cys209, PDI has no effect on fully active TF on either negatively charged phospholipids or in activating detergent, indicating that PDI selectively acts upon cryptic TF to facilitate ternary complex formation and macromolecular substrate turnover, overview
-
-
?
unfolded RNase
refolded RNase
show the reaction diagram
O97451, O97452, Q9U015
-
-
?
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
-
-
?
additional information
?
-
-
-
-
-
-
additional information
?
-
-
PDI is a subunit of the enzyme prolyl-4-hydroxylase, which catalyzes the formation of 4-hydroxyprolyl residues in nascent collagen-like polypeptides. PDI is also a subunit of a triacylglycerol transfer protein, which facilitates the incorporation of lipids into newly synthesized core lipoproteins within the endoplasmic reticulum. The function of PDI is to maintain the alpha-subunit of this enzyme in an active form
-
-
-
additional information
?
-
-
the enzyme has an essential role that is distinct from its function in formation of native disulphides
-
-
-
additional information
?
-
-
the enzyme acts as a thyroid-hormone binding protein
-
-
-
additional information
?
-
-
the enzyme may be significant in the action of triiodothyronine towards the target cells
-
-
-
additional information
?
-
-
protein disulfide isomerase serves as a subunit of at least two enzymes, the beta-subunit of the enzyme prolyl hydroxylase and an ER triglyceride transferase
-
-
-
additional information
?
-
-
both chaperone and isomerase functions of PDI are essential for acceleration of the oxidative refolding and reactivation of dimeric alkaline protease inhibitor API, PDI acts as isomerase/chaperone for a few monomeric proteins assisting in disulfide bond formation and rearrangement of secreted proteins
-
-
-
additional information
?
-
-
DsbA and DsbC are involved in disulfide bond formation and play an important role in the formation of extracellular enzymes, DsbA is important in lipase stability and excretion
-
-
-
additional information
?
-
-
DsbC resolves incorrect disulfides whose formation has been catalyzed by redox-active copper
-
-
-
additional information
?
-
-
essential enzyme for yeast cell growth, both oxidase and isomerase activities are required
-
-
-
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
?
-
-
modeling of disulfide formation, the enzyme catalyzes disulfide formation and isomerization and acts as a chaperone inhibiting aggregation, enzyme assists in the system of chaperones and folding catalysts to ensure proper connection of disulfides and protein folding without improper interactions, mechanism of incorrect disulfide recognition
-
-
-
additional information
?
-
-
modeling of disulfide formation, the enzyme catalyzes disulfide formation and isomerization and acts as a chaperone inhibiting aggregation, enzyme assists in the system of chaperones and folding catalysts to ensure proper connection of disulfides and protein folding without improper interactions, the pancreatic enzyme is responsible for folding of a subset of secreted pancreatic zymogens
-
-
-
additional information
?
-
-
PDI plays a key role in catalyzing the folding of secretory proteins
-
-
-
additional information
?
-
-
PDILT forms intermolecular disulfide bonds in testis
-
-
-
additional information
?
-
-
RB60 is an atypical PDI that functions as a member of a redox regulatory protein complex controlling translation in the chloroplast, the enzyme is essential in the endoplasmic reticulum
-
-
-
additional information
?
-
-
regulation of PDI and PDI homologues activities, in vivo isomerase activity depends only on full-length PDI, not on PDI-homologues, modeling of disulfide formation, the enzyme catalyzes disulfide formation and isomerization and acts as a chaperone inhibiting aggregation, enzyme assists in the system of chaperones and folding catalysts to ensure proper connection of disulfides and protein folding without improper interactions
-
-
-
additional information
?
-
-
the enzyme catalyzes disulfide formation and isomerization and acts as a chaperone inhibiting aggregation, enzyme assists in the system of chaperones and folding catalysts to ensure proper connection of disulfides and protein folding without improper interactions
-
-
-
additional information
?
-
-
the enzyme is an essential catalyst of disulfide formation with two cysteines in the active site facilitating thiol-disulfide exchange
-
-
-
additional information
?
-
-
the enzyme plays a crucial role in folding periplasmatically excreted proteins
-
-
-
additional information
?
-
-
the organism is completely dependent on PDI activity for growth
-
-
-
additional information
?
-
P12865, -
the single domain PDI-1 and the class 1 PDI-2 are not essential for the organism
-
-
-
additional information
?
-
P04785
cell-surface PDI is required for transnitrosation of metallothionein by S-nitroso-albumin in intact pulmonary vascular endothelial cells, overview
-
-
-
additional information
?
-
-
DsbB is an integral membrane protein responsible for the de novo synthesis of disulfide bonds in the Escherichia coli periplasm, disulfide bond formation is catalyzed by the DsbA/DsbB system, DsbA is critical for catalyzing disulfide bond formation in proteins in the bacterial periplasm, which it accomplishes by directly oxidizing substrate proteins via dithiol-disulfide exchange, DsbA donates its disulfide bond directly to substrate proteins, in the process of transferring electrons from DsbA to a tightly bound ubiquinone cofactor, DsbB undergoes an unusual spectral transition, DsbA must be reoxidized by an electron acceptor, mechanism, overview
-
-
-
additional information
?
-
A5LHV9, A5LHW0, A5LHW1, -
HlPDI-1 might be involved in tick blood feeding and Babesia parasite infection in ticks
-
-
-
additional information
?
-
A5LHV9, A5LHW0, A5LHW1, -
HlPDI-3 might be involved in tick blood feeding and Babesia parasite infection in ticks
-
-
-
additional information
?
-
-, Q1HGL1
in vivo, disulfide bond formation is mainly catalyzed by protein disulfide isomerase
-
-
-
additional information
?
-
A0SHR2, -
PDI has an important function in the correct folding of nascent polypeptides, which is a crucial step in the mechanism which delivers tick proteins to the secretion pathway important for blood feeding
-
-
-
additional information
?
-
-
PDI has two distinct functions: acting as a molecular chaperone to maintain properly folded proteins and regulating the redox state of proteins by catalyzing the thiol-disulfide exchange reaction through two thioredoxin-like domains
-
-
-
additional information
?
-
A3RMS2, -
PDI is a multifunctional protein required for many aspects of protein folding and transit through the endoplasmic reticulum, the PDI activity is essential for viability, collagen biogenesis and extracellular matrix formation, overview, all isozymes are synergistically essential for embryonic development in this nematode
-
-
-
additional information
?
-
A3RMS2, -
PDI is a multifunctional protein required for many aspects of protein folding and transit through the endoplasmic reticulum, the PDI activity is essential for viability, collagen biogenesis and extracellular matrix formation, PDI-2 is required for the normal function of prolyl 4-hydroxylase, a key collagen-modifying enzyme, overview, PDI-2 is required for normal post-embryonic development, all isozymes are synergistically essential for embryonic development in this nematode
-
-
-
additional information
?
-
-
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
?
-
O13811, -
PDI is involved in the cellular growth and response to nutritional and oxidative stress, regulation, overview
-
-
-
additional information
?
-
-
PDI oxidizes pairs of cysteines to form disulfide bonds and can also shuffle incorrect disulfides into their correct pairings, function and mechanism of PDI, bacterial machinery for disulfide formation and oxidative protein folding, overview
-
-
-
additional information
?
-
P30101
PDIis responsible for correct disulfide bond formation of proteins in the endoplasmic reticulum, it recognize unfolded proteins and can be selective for specific proteins or classes
-
-
-
additional information
?
-
-
RB60 is involved in the light-regulated translation of the psbA mRNA in the chloroplast of the unicellular alga Chlamydomonas reinhardtii, light controls the redox regulation of RB47 function via the coupling of RB47 and RB60 redox states, overview
-
-
-
additional information
?
-
-
sperm surface protein disulfide isomerase activity plays a role in gamete fusion and sperm-egg interaction, the enzyme mediates conformational changes by thiol-disulfide exchange in fusion-active proteins, participation of ERp57, overview
-
-
-
additional information
?
-
-
structure and mechanism of PDI in disulfide formation and oxidative protein folding, overview
-
-
-
additional information
?
-
P17967
structure and mechanism of PDI in disulfide formation and oxidative protein folding, overview
-
-
-
additional information
?
-
-
structure and mechanism of PDI in disulfide formation and oxidative protein folding, overview
-
-
-
additional information
?
-
Q93YN0
the cotyledon-specific chloroplast biogenesis factor CYO1 is a protein disulfide isomerase and has a chaperone-like activity required for thylakoid biogenesis in cotyledons, mutation of Cyo1 affects the photosynthesis in cotyledons, overview
-
-
-
additional information
?
-
-
the enzyme assists protein folding in malaria parasites
-
-
-
additional information
?
-
Q2XQR3
the enzyme assists protein folding in malaria parasites
-
-
-
additional information
?
-
-, Q2XQR5
the enzyme assists protein folding in malaria parasites
-
-
-
additional information
?
-
Q4Z2V7
the enzyme assists protein folding in malaria parasites
-
-
-
additional information
?
-
Q7RRT0
the enzyme assists protein folding in malaria parasites
-
-
-
additional information
?
-
P07237, P13667, P30101, Q13087
the enzyme is involved in correct disulfide bond formation in secretory proteins as a key step in endoplasmic reticulum quality control, ERp57 works in conjunction with the endoplasmic reticulum lectin-like chaperones calnexin and calreticulin via the noncatalytic b' domain of the enzyme, the b' domains of ERp57 and PDI are very different, overview
-
-
-
additional information
?
-
-
the enzyme is involved in diphtheria toxin sensitivity and is required for toxin entry, Chlamydia trachomatis or Chlamydia psittaci, intracellular pathogens of humans, require the enzyme for attachment to mammalian CHO6 cells, host cell invasion is obligatory for survival, growth and pathogenesis, overview
-
-
-
additional information
?
-
-
the enzyme is involved in the oxidative folding of cystine knot defense proteins and in in the biosynthesis of insecticidal cyclotides, overview, the Oldenlandia affinis plant accumulates knotted circular proteins called cyclotides
-
-
-
additional information
?
-
-
the enzyme mediates rapid delivery of NO signalling into human platelets from the S-nitrosothiol compound S-nitrosoglutathione, NO delivery is blocked by inhibition of PDI, overview
-
-
-
additional information
?
-
-
the enzyme plays important roles in the folding of nascent polypeptides and the formation of disulfide bonds in the endoplasmic reticulum, PDIS-1 associates with proglycinin, a precursor of the seed storage protein glycinin, in the cotyledon, seed-dependent aggregation of amyloid beta-peptide (1-40) monomers is inhibited by both PDIS-1 and PDIS-2, both are involved in seed development, overview
-
-
-
additional information
?
-
-
enzyme is involved in the proper folding or quality control of storage proteins
-
-
-
additional information
?
-
-
PDI can function as a high-capacity intracellular 17beta-estradiol-binding protein that increases the concentration and accumulation of 17beta-estradiol in live cells. The intracellular PDI-bound 17beta-estradiol can be released from PDI upon a drop in 17beta-estradiol levels and the released 17beta-estradiol can augment estrogen receptor-mediated transcriptional activity and mitogenic actions in cultured cells. The binding of 17beta-estradiol by PDI also reduces the rate of metabolic disposition of this hormone
-
-
-
additional information
?
-
-
PDI is required in vivo for both fibrin generation and platelet thrombus formation
-
-
-
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
?
-
-
protein disulfide isomerase contributes to the activation of cryptic initiator protein tissue factoron microvesicles in vitro
-
-
-
additional information
?
-
-
protein disulfide isomerase directly promotes initiator protein tissue factor-dependent fibrin production during thrombus formation in vivo
-
-
-
additional information
?
-
-
protein disulfide isomerase PDI directly interacts with thiol-containing fibrinogen receptor alphaIIbbeta3. PDI has greater ability to isomerize disulfide bonds than the alphaIIbbeta3 integrin
-
-
-
additional information
?
-
A5LHV9, A5LHW0, A5LHW1, -
protein disulfide isomerases are involved in blood feeding, viability and oocyte development, probably by mediating the formation of disulfide bond-containing proteins of the ticks and the formation of basement membrane and cuticle components such as extracellular matrix
-
-
-
additional information
?
-
Q13087
PDIp also shows chaperone activity in preventing the aggregation of reduced insulin B chain and denatured D-glyceraldehyde-3-phosphate dehydrogenase, PDIp can form stable complexes with thermal-denatured substrate proteins, e.g. MCF-7 cellular proteins, independently of their enzymatic activity. The b-b' fragment of PDIp, which does not contain the active sites and is devoid of enzymatic activity, still has chaperone activity
-
-
-
additional information
?
-
-
AGR2 is essential for production of intestinal mucin MUC2, but is not required for establishment of intestinal secretory epithelial cell lineages
-
-
-
additional information
?
-
-
ER protein 57, ERP-57, also known as PDIA3, has disulfide oxidoreductase and isomerase activity. ERP-57 interacts with calnexin, CANX, a chaperone protein and a lectin that binds glycoproteins through a transient oligosaccharide intermediate, thought to prevent a rapid degradation, as well as endoplasmic reticulum retention, of misfolded proteins, overview
-
-
-
additional information
?
-
-
GmPDIL-1 and GmPDIL-2 function as molecular chaperones, and prevent the aggregation of unfolded rhodanese, while GmPDIL-3a and GmPDIL-3b do not
-
-
-
additional information
?
-
-
interactions between the C-terminal domain of Mnl1p and PDI, which include an intermolecular disulfide bond, are essential for subsequent introduction of a disulfide bond into the mannosidase homology domain of Mnl1p by PDI. This disulfide bond is essential for the ER-associated degradation activity of Mnl1p and in turn stabilizes the prolonged association of PDI with Mnl1p
-
-
-
additional information
?
-
-
PDI catalyzes disulfide bond formation in the endoplasmic reticulum
-
-
-
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
?
-
P55059
PDI is a major protein in the endoplasmic reticulum, operating as an essential folding catalyst and molecular chaperone for disulfide-containing proteins by catalyzing the formation, rearrangement, and breakage of their disulfide bridges
-
-
-
additional information
?
-
-
PDI is able to renature reduced-denatured RNase. Plasma transglutaminase-coagulation factor XIII, FXIII, also shows PDI activity with reduced-denatured RNase, its PDI activity is located on the A subunit
-
-
-
additional information
?
-
-
PDI specifically associates with signal peptide peptidase, SPP, independently of human cytomegalovirus glycoprotein US2, but not with Derlin-1
-
-
-
additional information
?
-
-
PDI specifically binds 3,3',5-triiodo-L-thyronine
-
-
-
additional information
?
-
-
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
?
-
P27773
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
?
-
E1CAJ6
PDIA3 shows chaperone activity to promote oxidative refolding of reduced denatured lysozyme, meanwhile PDI-P5 exhibits anti-chaperone activity to inhibit oxidative refolding of lysozyme at an equimolar ratio
-
-
-
additional information
?
-
-
the oxidoreductase chaperone PDI has an effect on the critical structure-forming step during the oxidative maturation of model disulfide-bond-containing proteins, it inhibits the conformational folding step of oxidative fold maturation and, therefore, has limited overall catalytic efficiency as an oxidoreductase chaperone, impact of rat PDI, null PDI and enzyme domains on the structure-forming step, overview. Detrimental impact of the oxidoreductase activity PDI during conformational folding include peptidyl prolyl isomerase which facilitates cis-trans isomerization of prolines
-
-
-
additional information
?
-
-
the PDI protein is necessary for Chlamydia attachment, but the bacteria apparently do not bind directly to cell-associated PDI, suggesting that Chlamydia attaches to a host protein(s) associated with PDI. PDI enzymatic activity is necessary for bacterial entry but not for attachment, cell surface PDI-mediated reduction triggers Chlamydia entry into cells, molecular mechanism, overview
-
-
-
additional information
?
-
Q4Z2V7
the enzyme assists protein folding in malaria parasites
-
-
-
additional information
?
-
Streptomyces sp. NCIM 5127
-
both chaperone and isomerase functions of PDI are essential for acceleration of the oxidative refolding and reactivation of dimeric alkaline protease inhibitor API, PDI acts as isomerase/chaperone for a few monomeric proteins assisting in disulfide bond formation and rearrangement of secreted proteins
-
-
-
additional information
?
-
Chlamydomonas reinhardtii 2137a
-
RB60 is an atypical PDI that functions as a member of a redox regulatory protein complex controlling translation in the chloroplast, the enzyme is essential in the endoplasmic reticulum
-
-
-
additional information
?
-
Plasmodium knowlesi H
Q2XQR5
the enzyme assists protein folding in malaria parasites
-
-
-
additional information
?
-
Plasmodium vivax Sal1
Q2XQR3
the enzyme assists protein folding in malaria parasites
-
-
-
additional information
?
-
Saccharomyces cerevisiae trg1/TRG1
-
the organism is completely dependent on PDI activity for growth
-
-
-
additional information
?
-
Schizosaccharomyces pombe KP1
O13811
PDI is involved in the cellular growth and response to nutritional and oxidative stress, regulation, overview
-
-
-
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
ATP
-
for the ATPase activity, binding of ATP does not alter the enzyme's conformation, binding structure
DTT
A5LHV9, A5LHW0, A5LHW1, -
-
glutathione
Q96DN0
reduced and oxidized
glutathione
-
at physiological concentrations of GSSG, the rate-limiting step for the oxidation of the active site of PDI by GSSG is the nucleophilic attack by the C-terminal active-site cysteine on the reduced glutathione (GSH)-PDI mixed disulfide
GSH
-
for oxidative folding
GSSG
-
for reduction activity
thioredoxin
-
the enzymes PDI, P5, ERp72, ERp46 and ERp18 contains a thioredoxin binding site and the CGHC active site
ubiquinone
-
tightly bound ubiquinone cofactor, which becomes oxidized to hydroquinone and is regenerated by the electron transport chain and O2PDI contains four transmembrane helices that surround the bound ubiquinone cofactor, overview
additional information
-
glutathione is used in vitro as redox system
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ag+
-
PDI binds Ag+
Ca2+
-
enzyme binds 19 mol Ca2+ per mol of protein with low affinity, which is reduced by increasing the ionic strength. Ca2+ induces conformational changes
Ca2+
-
major calcium binding protein of the endoplasmic reticulum
Ca2+
-
recombinant ECaST/PDI binds 26 mol of Ca2+/mol of protein with a Kd of 2.8 mM, 1-5 mM Ca2+ augments the reactivation of rBPTI
Ca2+
-
1-5 mM Ca2+ augments the reactivation of reduced bovine pancreatic trypsin inhibitor
Ca2+
Sea urchin
-
enzyme binds 23 mol Ca2+ at low affinity
Ca2+
-
can partially substitute for Mg2+
Ca2+
-
possibly bound at the C-terminal extension
Co2+
-
can partially substitute for Mg2+
Cu2+
-
PDI binds a maximum of 4 mol Cu2+ and is able to reduce it to Cu+, the bound Cu+ is surface-exposed
Cu2+
-
only 40% as effective as Mg2+
Mg2+
-
for the ATPase activity, best divalent cation
Mg2+
E1CAJ6
-
Mg2+
-
-
Mn2+
-
only 30% as effective as Mg2+
Zn2+
-
required for enzyme dimerization and oligomerization
Mn2+
-
modulates the thiol isomerase activity of protein disulfide isomerase that is bound to integrin alphaVbeta3 and induces its transition to the ligand-competent state
additional information
-
enzyme requires divalent cations for ATPase activity, with descending specificity for Mg2+, Co2+, Ca2+, Cu2+, and Mn2+
additional information
-
Ca2+ and Mg2+ have no effect on the enzyme and do not influence Zn2+ effects
additional information
P27773
no effect by Ca2+
additional information
-
no effect by Ca2+
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1,1-bis(4-hydroxyphenyl)ethane
-
i.e.bisphenol E, 15% inhibition at 0.0125 mM
1,3-diphenylpropane
-
8% inhibition at 0.0125 mM
12-O-Tetradecanoylphorbol 13-acetate
-
binds to and moderately inhibits PDI
2',3,3',4',5'-pentachlorobiphenyl
-
strong inhibition of PDI 3,3',5-triiodo-L-thyronine-binding activity
2',3,3',5,5',6'-hexachlorobiphenyl
-
strong inhibition of PDI 3,3',5-triiodo-L-thyronine-binding activity
2,2-bis(4-hydroxyphenyl)propane
-
i.e. bisphenol A, 30% inhibition at 0.0125 mM
2-(2-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
-
and analogs
3,3',5-triiodo-L-thyronine
-
30% inhibition at 0.0125 mM
3,3',5-triiodo-L-thyronine
-
inhibits PDI isomerase activity
3,3',5-triiodothyronine
-
-
3,4-dichlorophenol
-
inhibits PDI 3,3',5-triiodo-L-thyronine binding activity
4,4'-diisothiocyano-2,2'-stilbene disulfonic acid
-
considerably more effective after preincubation with DTT
4,4'-methylenebisphenol
-
12% inhibition at 0.0125 mM
4-alpha-cumylphenol
-
18% inhibition at 0.0125 mM
4-amino-phenylarsine oxide
-
0.0058 mM, 50% inhibition of tyramine-S-S-poly(D-lysine) reduction
4-chloromercuribenzoic acid
-
-
4-chloromercuribenzoic acid
A7YBW7, A7YBX0, A7YBX2, A7YBX4, -
-
4-hydroxy-2-nonenal
-
44% inhibition at 0.03 mM
4-nonylphenol
-
inhibits PDI 3,3',5-triiodo-L-thyronine binding activity
4-octylphenol
-
inhibits PDI 3,3',5-triiodo-L-thyronine binding activity
5,5'-dithiobis(2-nitrobenzoic acid)
-
0.0049 mM, 50% inhibition of tyramine-S-S-poly(D-lysine) reduction
5-(3-carboxy-4-nitro-phenyl) sulfonyl-2-nitrobenzoic acid
-
i.e. NSC695265. Molecular docking simulation into the redox-active site, residues C37, G38, H39, C40. Inhibitor binds to hydrophobic amino acidsA34, W36, C37, C40, H39, T68 and F80. The redox inhibitory conformations are energetically and statistically favored
8-azido-ATP
-
for the ATPase activity, binds at the same site as ATP
acrolein
-
79% inhibition at 0.03 mM
anti-PDI Fab fragments
-
-
-
Bacitracin
-
-
Bacitracin
A7YBW7, A7YBX0, A7YBX2, A7YBX4, -
-
Bacitracin
-
inhibition of protein disulfide isomerase results in enhanced stress response and apoptosis
Bacitracin
-
inhibition of protein disulfide isomerase. Treatment of Mn2+-treated endothelial cells abolishes the conversion of integrin alphaVbeta to the ligand-competent high-affinity state
Bacitracin
-
infusion of blood vessels inhibits platelet thrombus formation and fibrin generation
Bacitracin
-
a PDI-specific inhibitor
Bacitracin
-
-
Bacitracin
-
commercial bacitracin consists of 65% bacitracin A and B
Bacitracin A
-
-
Bacitracin A
-
-
bacitracin B
-
-
-
bacitracin F
-
-
-
bacitracin H
-
-
-
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. Inhibits also PDI family members ERp57 and ERp72
bisphenol A
-
i.e. 2,2-bis(4-hydroxyphenyl)propane, an endocrine disrupting chemical, inhibiting the enzyme's 3,3',5-triiodo-L-thyronine binding activity, its chaperone activity, and its isomerase activity, structural requirements, overview
Ca2+
-
1 mM, 40% inhibition
deoxycholate
-
-
Diazobenzene sulfonic acid
-
considerably more effective after preincubation with DTT
Dithionitrobenzoic acid
-
molecular docking simulation into the redox-active site, residues C37, G38, H39, C40. Inhibitor binds to hydrophobic amino acidsA34, W36, C37, C40, H39, T68 and F80. The redox inhibitory conformations are energetically and statistically favored
dithiothreitol
-
treatment decreases the content of 52 kDa isoform by half
E-64
-
0.01 mM, 11% inhibition after treatment with 0.01 mM DTT. No inhibition without DTT
Estrogens
-
-
-
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
-
-
iodoacetamide
-
incubation after pretreatment with DTT or GSH
iodoacetamide
-
pH-dependent inactivation
iodoacetamide
Q13087
alkylation of PDIp by iodoacetamide fully abolishes its enzymatic activity while it still retains most of its chaperone activity
iodoacetate
-
1 mM, almost complete inhibition after reduction with 0.01 mM DTT. No inhibition in absence of DTT
iodoacetate
-
inactivation by alkylation follows pseudo-first-order kinetics
iodoacetate
-
-
kanamycin
-
analysis of binding and dissociation constants with PDI and PDI domain deletion mutants
MA3 018
-
inhibition of protein disulfide isomerase. Treatment of Mn2+-treated endothelial cells abolishes the conversion of integrin alphaVbeta to the ligand-competent high-affinity state
-
MA3 019
-
inhibition of protein disulfide isomerase. Treatment of Mn2+-treated endothelial cells abolishes the conversion of integrin alphaVbeta to the ligand-competent high-affinity state
-
methyl-methanethiosulfonate
-
abolishes PDI oxidoreductase but not chaperone activity
N-acetylated-triiodothyronine
-
0.07 mM, 50% inhibition of tyramine-S-S-poly(D-lysine) reduction
N-ethylmaleimide
-
pH-independent inactivation within the range of pH 6.3-7.0
N-ethylmaleimide
-
abolishes PDI oxidoreductase but not chaperone activity
N-Iodoacetyl-N'-(5-sulfo)-1-naphthyl-diaminoethane
-
incubation after pretreatment with DTT or GSH
NEM
-
incubation after pretreatment with DTT or GSH
neomycin
-
analysis of binding and dissociation constants with PDI and PDI domain deletion mutants
nitazoxanide
-
a broad-spectrum anti-parasitic drug
nitazoxanide thiazolide derivatives
-
PDI is inhibited by those thiazolides that also affected parasite proliferation
-
paromomycin
-
analysis of binding and dissociation constants with PDI and PDI domain deletion mutants
Pentachlorophenol
-
inhibits PDI 3,3',5-triiodo-L-thyronine binding activity
Peptides
-
study of the inhibition of enzyme catalyzed reduction of insulin by GSH by peptides of various length and amino acid composition
Phenylarsine oxide
-
complete inhibition at 0.01-0.1 mM in vivo
protein DS61
-
-
-
ribostamycin
-
aminoglycoside antibiotic, inhibits the chaperone activity of PDI, isomerase activity is not inhibited
ribostamycin
-
analysis of binding and dissociation constants with PDI and PDI domain deletion mutants
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
tert-2-hexenal
-
32% inhibition at 1 mM
-
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
tizoxanide
-
deacetylated metabolite of nitazoxanide
tocinoic acid
-
-
Vancomycin
-
analysis of binding and dissociation constants with PDI and PDI domain deletion mutants
Vincristine
-
inhibits chaperone activity but not isomerase activity of both isoforms PDI and P5 in vitro. A 100:1 molar ratio of vincristine to enzyme is sufficient to almost completely inhibit chaperone activity
zinc bacitracin
A5LHV9, A5LHW0, A5LHW1, -
specific inhibition; specific inhibition; specific inhibition
Zn2+
-
1 mM, 70% inhibition
Mg2+
-
1 mM, 20% inhibition
additional information
-
malonaldehyde bis(diethyl acetal) is a poor inhibitor, pH-dependency of inhibition by alkylating inhibitors and SH-reagents
-
additional information
-
in absence of DTT, the enzyme, at a concentration above 0.001 mM, inhibits reactivation of creatinine kinase involving Cys36 and Cys295 of PDI
-
additional information
-
inhibition by PDI-specific antibodiy RL90
-
additional information
-
pressure conditions at 400 MPa decrease the enzyme isomerase activity
-
additional information
-
in presence of light, the level of protein disulfide isomerase protein decreases by 80%
-
additional information
-
functional inhibition of protein disulfide isomerase by S-nitrosylation
-
additional information
P27773
no inhibition of CxPR2 activity by treatment with cysteine and serine protease inhibitors E-64 and DCI
-
additional information
-
CxRP2 activity is partially depleted by immobilized RNK-16 granule proteins, no inhibition of CxPR2 activity by treatment with cysteine and serine protease inhibitors E-64 and DCI
-
additional information
-
no effects of nonhydroxylated biphenyls on 3,3',5-triiodo-L-thyronine binding
-
additional information
-
no inhibition of PDI oxido-reductase activity with di(o-aminobenzyl)-labeled oxidized glutathione by DELTA-somatostatin
-
additional information
-
both GmPDIL-3a and GmPDIL-3b are resistant to protease treatment in the absence of detergent, and are degraded when detergent is added
-
additional information
-
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
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
calnexin
P30101
interacts with the enzyme via the b and b' domains, binding site and structure, overview
-
cCMP
A7YBW7, A7YBX0, A7YBX2, A7YBX4, -
-
dichlorophenyl-1,1-dimethylurea
-
blocks the reduction of plastoquinone, resulting in 1.5- to 2fold increase in PDI content
-
DsbA
-
disulfide bond formation is catalyzed by the DsbA/DsbB system, DsbA is critical for catalyzing disulfide bond formation in proteins in the bacterial periplasm, which it accomplishes by directly oxidizing substrate proteins via dithiol-disulfide exchange, DsbA donates its disulfide bond directly to substrate proteins, in the process of transferring electrons from DsbA to a tightly bound ubiquinone cofactor, DsbA must be reoxidized by an electron acceptor, overview
-
DTT
-
the disulfide reduction activity of PDI-DTT is reduced
DTT
P12865
required for activity
DTT
-
absolutely required for activity
DTT
-
required for activity
GSH
-
required for activity
GSH
A7YBW7, A7YBX0, A7YBX2, A7YBX4, -
-
GSSG
-
promotes the activation of carbonic anhydrase IV
GSSG
-
required for oxidation activity
GSSG
-
required for activity
NADPH
-, Q1HGL1
-
phosphate
-
treatment of plants results in 1.5- to 2fold increase in PDI content
GSSG
A7YBW7, A7YBX0, A7YBX2, A7YBX4, -
-
additional information
-
thioredoxin reductase activates PDI at pH 7.4, 37C involving glutathione reduction and NADPH, the disulfide reduction activity of PDI-thioredoxin reductase is reduced
-
additional information
-
PDI1 gene expression is stress-induced by over 2.5fold in response to e.g. reducing agents such as DTT, or to thiol-specific oxidizing agents such as diamide, other PDI gene homologues are also stress-induced
-
additional information
P07237, P13667, P30101, Q13087
the enzyme is stress-inducible; the enzyme is stress-inducible; the enzyme is stress-inducible
-
additional information
-
PDIS-1, but not PDIS-2, is induced under endoplasmic reticulum-stress conditions
-
additional information
A5LHV9, A5LHW0, A5LHW1, -
blood feeding induces the expression of HlPDI-1 in both partially fed nymphs and adults, overview; blood feeding induces the expression of HlPDI-3 in both partially fed nymphs and adults, overview
-
additional information
O13811
oxidaive stress by H2O2, and glucose deprivation or nitrogen starvation induce PDI enzyme expression
-
additional information
-
light controls the redox regulation of RB47 function via the coupling of RB47 and RB60 redox states
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.2
-
2-mercaptoethanol
-
with scrambled ribonuclease as substrate
0.8
-
2-mercaptoethanol
-
with scrambled ribonuclease as substrate
1
-
Cys
-
with scrambled ribonuclease as substrate
3
-
Cys
-
glutathione, with scrambled ribonuclease as substrate
3
-
Cys
-
GSH, with scrambled ribonuclease as substrate
0.0253
-
denatured-reduced lysozyme
-
pH 7.0, temperature not specified in the publication
-
0.003
-
dithiothreitol
-
with scrambled ribonuclease as substrate
0.0054
-
dithiothreitol
-
-
5
-
GSH
-
with scrambled ribonuclease as substrate
2.026
-
Insulin
-
pH 7.0, temperature not specified in the publication
-
0.0011
-
ribonuclease
-
scrambled
-
0.002
-
ribonuclease
-
scrambled
-
0.002
-
ribonuclease
-
dithiothreitol, with scrambled ribonuclease as substrate
-
0.0033
-
ribonuclease
-
scrambled
-
0.01
-
ribonuclease
-
scrambled, with dithiothreitol as substrate
-
0.02
-
ribonuclease
-
scrambled, with dithiothreitol as substrate
-
0.028
-
RNase
-
refolding of RNase
-
0.063
-
RNase
-
refolding of RNase
-
0.007
-
RNAse A
-
wild-type PDI
-
0.036
-
RNAse A
-
mutant PDI without Cys in domain a'
-
0.05
-
RNAse A
-
mutant PDI without two Cys in domains a' and a
-
0.0116
-
scrambled reoxidized lysozyme
-
pH 7.0, temperature not specified in the publication
-
0.005
-
insulin-(SS)
-
-
-
additional information
-
additional information
-
Km for scrambled ribonuclease: 0.023 mg/ml
-
additional information
-
additional information
-
light scattering and fluorescence measurement kinetics of wild-type PDI and mutant abb'a' lacking the C-terminal domain c, overview
-
additional information
-
additional information
-
redox equilibrium measurements of wild-type and mutant C90A/C97A enzymes, determination of oxidase and isomerase activities
-
additional information
-
additional information
-
kinetics and kinetic mechanism of DsbB, overview
-
additional information
-
additional information
-
folding kinetics of linear and cyclic kalata B1
-
additional information
-
additional information
-
refolding reaction obeys almost first-order kinetics with respect to PDI concentration
-
additional information
-
additional information
A7YBW7, A7YBX0, A7YBX2, A7YBX4, -
kinetics; kinetics; kinetics; kinetics
-
additional information
-
additional information
-
kinetic analysis of the RB60-RB47 complex, overview
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2.8e-05
-
RNase
-
refolding of RNase
-
0.0011
-
RNase
-
refolding of RNase
-
0.017
-
sRNase
-
-
-
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.447
-
acrolein
-
pH 6.3, 38C
0.311
-
iodoacetamide
-
pH 6.3, 38C
0.124
-
N-ethylmaleimide
-
pH 6.3, 38C
0.179
-
iodoacetate
-
pH 6.3, 38C
additional information
-
additional information
-
pseudo-first-order and second-order kinetics
-
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.07
-
Bacitracin
-
commercial bacitracin, in 100 mM potassium phosphate and 1 mm EDTA (pH 7.4), at 22C
0.172
-
Bacitracin
-
using denatured-reduced lysozyme as substrate, at pH 7.0, temperature not specified in the publication
0.334
-
Bacitracin
-
using scrambled reoxidized lysozyme as substrate, at pH 7.0, temperature not specified in the publication
1.137
-
Bacitracin
-
using insulin as substrate, at pH 7.0, temperature not specified in the publication
0.59
-
Bacitracin A
-
in 100 mM potassium phosphate and 1 mm EDTA (pH 7.4), at 22C
1.05
-
bacitracin B
-
in 100 mM potassium phosphate and 1 mm EDTA (pH 7.4), at 22C
-
0.02
-
bacitracin F
-
in 100 mM potassium phosphate and 1 mm EDTA (pH 7.4), at 22C
-
0.04
-
bacitracin H
-
in 100 mM potassium phosphate and 1 mm EDTA (pH 7.4), at 22C
-
0.43
-
protein DS61
-
isozyme PDI-22
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
ATPase activity, Holmgren's turbimetric method for reductive activity measurement utilizing bovine insulin
additional information
-
-
-
additional information
-
A5LHV9, A5LHW0, A5LHW1, -
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
2.5
-
-
assay at with substrate AppA, DsbC
4.5
-
-
assay at with substrate Agp mutant, DsbC
6.5
-
-
substrate NRCSQGSCWN
6.5
-
-
R120Q mutant shows 59% of wild-type activity at pH 7.5
6.5
-
A0SHR2, -
assay at
6.5
-
-
pH optimum for the reductase activity of recombinant PDI
7
-
-
assay at
7
-
-
assay at, oxidoreductase and isomerase activity
7
-
-
assay at
7
-
-
assay at
7
-
Q96DN0
assay at
7
-
-
assay at
7.4
-
-
assay at
7.4
-
-
assay at
7.5
7.8
-
-
7.5
9
-
-
7.5
-
-
-
7.5
-
-
assay at
7.5
-
-
assay at
7.5
-
-, Q1HGL1
isomerase activity assay at
7.5
-
-
assay at
7.5
-
O13811
assay at
7.5
-
P27773
assay at
7.5
-
-
assay at
7.5
-
-
assay at
7.5
-
D0EJL8
assay at
7.5
-
-
assay at
8
8.2
-
assay at
8
-
-
-
8
-
-
assay at
8
-
-
assay at
8
-
-, Q1HGL1
refolding activity assay at
8
-
A7YBW7, A7YBX0, A7YBX2, A7YBX4, -
assay at; assay at; assay at; assay at
8
-
Q13087
isomerase assay at
8
-
-
pH optimum for the oxidase activity of recombinant PDI
8.6
-
E1CAJ6
assay at
10
-
-
ATPase activity
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
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4.5
7.5
-
approx. 50% of maximal activity at pH 5.5, approx. 75% of maximal activity at pH 7.5
5
7
-
approx. 50% of maximal activity at pH 5.5, approx. 80% of maximal activity at pH 7.0, oxidation of NRCSQGSCWN
7
10.5
-
ATPase activity is maximal at basic pH
7
9
-
pH 7: about 50% of maximal activity, pH 9: about 60% of maximal activity
7.2
8
-
activities are greater than 50% in this range
7.5
9
-
pH 7.5: about 20% of maximal activity, pH 9.0: about 80% of maximal activity
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
22
-
-
assay at room temprature
25
-
-
assay at
25
-
-
assay at
25
-
-
assay at
25
-
-
assay at
25
-
-
assay at
25
-
Q13087
isomerase assay at
25
-
-
assay at
25
-
-
assay at
30
-
-
-
30
-
-
assay at, oxidoreductase and isomerase activity
30
-
A5LHV9, A5LHW0, A5LHW1, -
assay at; assay at; assay at
37
-
-
assay at
37
-
-
assay at
37
-
-
in vivo assay at
37
-
E1CAJ6
assay at
37
-
-
assay at
38
-
-
assay at
45
-
-
assay at
90
-
-
ATPase activity
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
45
75
-
for the oxidation activity
45
90
-
for the ATPase activity
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.6
-
-
PDI C-terminal extension domain, isoelectric focusing
6.64
-
A0SHR2, -
isoelectric focusing
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
the thiol-containing form of PDI increases in the platelet surface with platelet activition
Manually annotated by BRENDA team
-
time-dependent decrease in in PDI expression in thrombi following injury. Infusion of monoclonal antibodies against PDI into the circulation of mice lacking the G protein-coupled platelet receptor Par4 prior to vessel wall injury inhibits fibrin generation
Manually annotated by BRENDA team
-
activities in adult tissues are only 10-40% of those found in newborn
Manually annotated by BRENDA team
Q96DN0
expression of ERp27
Manually annotated by BRENDA team
-
lowest activity of the tissues tested
Manually annotated by BRENDA team
-
activities in adult tissues are only 10-40% of those found in newborn; lowest activity of the tissues tested
Manually annotated by BRENDA team
P07237, P13667, P30101, Q13087
inducible
Manually annotated by BRENDA team
-
distribution to the endoplasmic reticulum and protein storage vacuoles, PDIS-1 levels, but not PDIS-2 levels, are increased in cotyledons
Manually annotated by BRENDA team
-
expression of GmPDIL-3a and GmPDIL-3b in soybean cotyledons during maturation, overview
Manually annotated by BRENDA team
A5LHV9, A5LHW0, A5LHW1, -
female tick, highest expression level of HlPDI-1
Manually annotated by BRENDA team
-
transcription is more than 7fold enriched in L1 state compared to eggs
Manually annotated by BRENDA team
Q53LQ0, Q67UF5
;
Manually annotated by BRENDA team
-
low expression level of PDIp
Manually annotated by BRENDA team
D0QEL0, -
very low expression level of PDIA3
Manually annotated by BRENDA team
A5LHV9, A5LHW0, A5LHW1, -
female tick
Manually annotated by BRENDA team
A0SHR2, -
cells of the acini type II and III of salivary gland
Manually annotated by BRENDA team
-
cultured, confluent; lung
Manually annotated by BRENDA team
-
a pituitary tumor cell line
Manually annotated by BRENDA team
-
a pituitary carcinoma celll line
Manually annotated by BRENDA team
A0SHR2, -
male tick
Manually annotated by BRENDA team
-
activities in adult tissues are only 10-40% of those found in newborn
Manually annotated by BRENDA team
-
transiently transfected with human wild-type US2, wild-type US11, or different cysteine mutants of US2 and US11
Manually annotated by BRENDA team
A5LHV9, A5LHW0, A5LHW1, -
female tick
Manually annotated by BRENDA team
-
PDIp is exclusively expressed in Paneth cells
Manually annotated by BRENDA team
-
; intestinal secretory epithelial cell
Manually annotated by BRENDA team
-
activities in adult tissues are only 10-40% of those found in newborn
Manually annotated by BRENDA team
Q96DN0
expression of ERp27
Manually annotated by BRENDA team
A5LHV9, A5LHW0, A5LHW1, -
-
Manually annotated by BRENDA team
-
trifoliolate leaves
Manually annotated by BRENDA team
-
52 kDa isoform
Manually annotated by BRENDA team
-
trifoliolate center leaves
Manually annotated by BRENDA team
-
highest activity of tissues tested
Manually annotated by BRENDA team
-
activities in adult tissues are only 10-40% of those found in newborn; highest activity of tissues tested
Manually annotated by BRENDA team
D0QEL0, -
primary expression of PDIA3
Manually annotated by BRENDA team
-
low expression level of PDIp
Manually annotated by BRENDA team
-
activities in adult tissues are only 10-40% of those found in newborn
Manually annotated by BRENDA team
Q96DN0
expression of ERp27
Manually annotated by BRENDA team
-
enzyme activity increases in response to polyclonal activation by bacterial lipopolysaccharide. Induction of the enzyme is closely coupled to the final stages of differentiation to plasma cells
Manually annotated by BRENDA team
-
activities in adult tissues are only 10-40% of those found in newborn
Manually annotated by BRENDA team
-
; NS0/2N2 cell; NS0/40 cell
Manually annotated by BRENDA team
A5LHV9, A5LHW0, A5LHW1, -
-
Manually annotated by BRENDA team
A5LHV9, A5LHW0, A5LHW1, -
female tick, high expression of HlPDI-1
Manually annotated by BRENDA team
-
tissue-specific expression of PDI
Manually annotated by BRENDA team
Q96DN0
high expression of ERp27
Manually annotated by BRENDA team
Q13087
pancreas-specific enzyme
Manually annotated by BRENDA team
-
pancreas-specific protein disulfide isomerase, PDIp, specific expression in pancreatic acinar cells, high expression level of PDIp
Manually annotated by BRENDA team
-
on the extracellular surface of both nonactivated and thrombin-activated platelets. Enzyme is released by vesiculation from activated platelets
Manually annotated by BRENDA team
D0QEL0, -
low expression level of PDIA3
Manually annotated by BRENDA team
-
an NK cell-like leukemia cell line
Manually annotated by BRENDA team
A5LHV9, A5LHW0, A5LHW1, -
female tick, high expression of HlPDI-1; female tick, high expression of HlPDI-2; female tick, high expression of HlPDI-3
Manually annotated by BRENDA team
-
changes in the levels of PDIS-1 and PDIS-2 during seed development, overview
Manually annotated by BRENDA team
-
52 kDa isoform
Manually annotated by BRENDA team
-
activities in adult tissues are only 10-40% of those found in newborn
Manually annotated by BRENDA team
-
cultured, confluent
Manually annotated by BRENDA team
D0QEL0, -
low expression level of PDIA3
Manually annotated by BRENDA team
E1CAJ6
epididymal caput, corpus, and cauda sperm, isozymes PDIA3 and PDI-P5. PDI-P5 is downregulated from the epididymal corpus to cauda sperm, while PDIA3 is constitutively expressed
Manually annotated by BRENDA team
-
lumbar, segments
Manually annotated by BRENDA team
-
activities in adult tissues are only 10-40% of those found in newborn
Manually annotated by BRENDA team
Q96DN0
expression of ERp27
Manually annotated by BRENDA team
-
low expression level of PDIp
Manually annotated by BRENDA team
-
52 kDa isoform
Manually annotated by BRENDA team
-
specific expression of PDIp in gastric chief cells, high expression level of PDIp
Manually annotated by BRENDA team
-
activities in adult tissues are only 10-40% of those found in newborn
Manually annotated by BRENDA team
-
testis-specific isozyme PDILT
Manually annotated by BRENDA team
Q96DN0
expression of ERp27
Manually annotated by BRENDA team
A0SHR2, -
male ticks
Manually annotated by BRENDA team
-
high expression level of PDIp
Manually annotated by BRENDA team
D0QEL0, -
very low expression level of PDIA3
Manually annotated by BRENDA team
-
SV40 transformed, cultured, confluent, weak activity
Manually annotated by BRENDA team
A5LHV9, A5LHW0, A5LHW1, -
female tick
Manually annotated by BRENDA team
additional information
P12865
developmentally regulated expression of both PDI enzyme forms, the enzymes are not essential for growth of trypanosomes
Manually annotated by BRENDA team
additional information
P07237, P13667, P30101, Q13087
ubiquitous tissue expression; ubiquitous tissue expression; ubiquitous tissue expression
Manually annotated by BRENDA team
additional information
-
PDI expression during parasite development, overview
Manually annotated by BRENDA team
additional information
A3RMS2, -
PDI-2 is required for normal post-embryonic development
Manually annotated by BRENDA team
additional information
-
no expression in oocytes
Manually annotated by BRENDA team
additional information
A0SHR2, -
the PDI expression levels in salivary gland is uniform in unfed ticks and ticks fed for different time intervals, no differences in enzyme expression between female and male ticks, PDI tissue distribution analysis, overview
Manually annotated by BRENDA team
additional information
A5LHV9, A5LHW0, A5LHW1, -
the isozymes are present in all the developmental stages of the tick, immunihistochemic and quantitative expression analysis, overview; the isozymes are present in all the developmental stages of the tick, immunohistochemic and quantitative expression analysis, overview; the isozymes are present in all the developmental stages of the tick, immunohistochemic and quantitative expression analysis, overview
Manually annotated by BRENDA team
additional information
-
stage-specific expression and cellular localization of isozymes, overview, isozyme PDI-8 is expressed during all stages of parasite life cycle
Manually annotated by BRENDA team
additional information
-
no detection of protein of the 52 kDa isoform in root
Manually annotated by BRENDA team
additional information
-
ubiquitous expression in soybean tissues
Manually annotated by BRENDA team
additional information
-
transcription is more than 7fold enriched in L1 state compared to eggs, and displays a dramatic decrease in L3. Following an increase in the L5 stage, there is again a decrease in the adult worm
Manually annotated by BRENDA team
additional information
D0QEL0, -
differential expression of PDIA3 mRNA in salmon tissues
Manually annotated by BRENDA team
additional information
-
GmPDIL-3a and GmPDIL-3b are ubiquitously expressed in the plant body
Manually annotated by BRENDA team
additional information
-, Q5UAH0
propagation in mice
Manually annotated by BRENDA team
additional information
-
no activity of PDIp in pancreatic adenocarcinoma cells
Manually annotated by BRENDA team
additional information
-
no or poor expression of PDIp in colon, cecum, and duodenum. PDIp shows a cell-type specific expression in various mouse tissues, in the digestive organs, such as the stomach and pancreas, very high levels of PDIp are selectively expressed in the digestive enzyme-secreting cells
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
RB60 contains an N-terminal sequence of 50 amino acids that are sufficient for chloroplast and enodplasmic reticulum targeting, after translocation to the ER the leader sequence is cleaved while it remains intact after import into chloroplasts
Manually annotated by BRENDA team
-
in presence of light, level of protein disulfide isomerase protein decreases by 80%. The effect of chemical treatments coincides with the effect of the light/dark cycle
Manually annotated by BRENDA team
Chlamydomonas reinhardtii 2137a
-
RB60 contains an N-terminal sequence of 50 amino acids that are sufficient for chloroplast and enodplasmic reticulum targeting, after translocation to the ER the leader sequence is cleaved while it remains intact after import into chloroplasts
-
Manually annotated by BRENDA team
-
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
-
loosely associated with the luminal surface
Manually annotated by BRENDA team
-
the enzyme is among the most abundant proteins within the endoplasmic reticulum of developing grains
Manually annotated by BRENDA team
-
lumen; surface-associated
Manually annotated by BRENDA team
O97451, O97452, Q9U015
ER retention/retrieval signal KQRL; gPDI-3 has a ER retention/retrieval signal KQRL, gPDI-2 has a KRKK motif; KRKK motif
Manually annotated by BRENDA team
-
the enzyme contains a C-terminal endoplasmic reticulum retention signal, RB60 contains an N-terminal leader sequence of 50 amino acids that are sufficient for chloroplast and enodplasmic reticulum targeting, after translocation to the ER the leader sequence is cleaved while it remains intact after import into chloroplasts
Manually annotated by BRENDA team
-, Q1HGL1
the enzyme contains an N-terminal ER retention signal sequence
Manually annotated by BRENDA team
-
PDIS-1 and PDIS-2 lack the C-terminal, endoplasmic reticulum-retrieval signal, KDEL
Manually annotated by BRENDA team
A0SHR2, -
PDI contains an endoplasmic reticulum-retention KEEL signal
Manually annotated by BRENDA team
A5LHV9, A5LHW0, A5LHW1, -
PDI contains an endoplasmic reticulum-retention DEL signal; PDI contains an endoplasmic reticulum-retention EEL signal; PDI contains an endoplasmic reticulum-retention VEL signal
Manually annotated by BRENDA team
-
the enzyme contains a C-terminal endoplasmic reticulum retrieval signal, SEEL
Manually annotated by BRENDA team
Q96DN0
ERp27 contains a putative secretory pathway signal sequence and a putative endoplasmic reticulum-retention signal, overview
Manually annotated by BRENDA team
-
; expression is up-regulated in ER-stress conditions
Manually annotated by BRENDA team
-
enzyme exists as an interconvertible mixture of monomers and dimers
Manually annotated by BRENDA team
-
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
Manually annotated by BRENDA team
-
exclusively in human umbilical vein endothelial cells. In endothelium, PDI remains exclusively localized in the endoplasmic reticulum, both at steady state and after thrombin stimulation
Manually annotated by BRENDA team
Chlamydomonas reinhardtii 2137a
-
the enzyme contains a C-terminal endoplasmic reticulum retention signal, RB60 contains an N-terminal leader sequence of 50 amino acids that are sufficient for chloroplast and enodplasmic reticulum targeting, after translocation to the ER the leader sequence is cleaved while it remains intact after import into chloroplasts
-
Manually annotated by BRENDA team
Saccharomyces cerevisiae trg1/TRG1, Streptomyces sp. NCIM 5127
-
lumen
-
Manually annotated by BRENDA team
-
GmPDIL-3a and GmPDIL-3b form protein complexes in the endoplasmic reticulum
Manually annotated by BRENDA team
-
of the P2 fraction
Manually annotated by BRENDA team
-
integral, the catalytic reaction takes place on the periplasmic side, PDI contains four transmembrane helices that surround the bound ubiquinone cofactor, overview
Manually annotated by BRENDA team
-
rough. The enzyme associates with the membrane via electrostatic interactions between the acidic enzyme and the basic groups on the membrane
-
Manually annotated by BRENDA team
-
rough and smooth
-
Manually annotated by BRENDA team
-
located on both sides of the membrane. The inside-located enzyme is immunochemically different from the outside-located enzyme
-
Manually annotated by BRENDA team
Chlamydomonas reinhardtii 2137a
-
-
-
-
Manually annotated by BRENDA team
Q53LQ0, Q67UF5
PDIL1-1 is uniformly distributed in the lumen; PDIL2-3 is localized mainly on the surface of the endoplasmic reticulum
Manually annotated by BRENDA team
-
cell surface protein
-
Manually annotated by BRENDA team
Chlamydomonas reinhardtii 2137a
-
-
-
Manually annotated by BRENDA team
-
protein storage vacuoles
Manually annotated by BRENDA team
-
presence of isoforms P5 and Erp57. P5 localizes to the inner side of the inner membrane
Manually annotated by BRENDA team
additional information
P12865
both enzyme forms co-localized with markers of the endocytic pathway and concentrate at the posterior end of the cell between the nucleus and the kinetoplast
-
Manually annotated by BRENDA team
additional information
-
dual localization of RB60 via two different conserved transport mechanisms, overview
-
Manually annotated by BRENDA team
additional information
P04785
cullular enzyme distribution, immunohistochemic detection, overview
-
Manually annotated by BRENDA team
additional information
-
PDIS-1 and PDIS-2 both possess a putative N-terminal secretory signal sequence and two tandem thioredoxin-like motifs, with a CGHC active site
-
Manually annotated by BRENDA team
additional information
-
stage-specific expression and cellular localization of isozymes, overview
-
Manually annotated by BRENDA team
additional information
Q96DN0
subcellular localization study with wild-type and mutant enzyme, overview
-
Manually annotated by BRENDA team
additional information
-
presence of protein disulfide isomerase on the surface of platelet-derived microparticles. Enzyme is catalytically active and capable of both promoting platelet aggregation and disrupting insulin signaling. Platelet-derived microparticles increase the initial rates of aggregation by 4fold and the pro-aggregatory activity of micrparticles can be attenuated with an anti-PDI antibody. Anti-PDI antibodies are able to block the degradation of insulin, thereby restoring insulin signaling
-
Manually annotated by BRENDA team
additional information
-
semiquantitative analysis of the endogenous PDI distribution, overview
-
Manually annotated by BRENDA team
additional information
Chlamydomonas reinhardtii 2137a
-
dual localization of RB60 via two different conserved transport mechanisms, overview
-
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Neisseria meningitidis serogroup B (strain MC58)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Salmonella typhimurium
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
12650
-
O97451, O97452, Q9U015
gPDI-3, deduced from nucleotide sequence
17770
-
-
MALDI mass spectrometry
21100
-
-
gel filtration
25850
-
O97451, O97452, Q9U015
gPDI-1, deduced from nucleotide sequence
50430
-
O97451, O97452, Q9U015
deduced from nucleotide sequence; gPDI-2, deduced from nucleotide sequence
58000
-
-
SDS-PAGE, immunoblot
62000
-
-
gel filtration
69000
-
-
light scattering
100000
-
-
gel filtration
107000
-
-
gel filtration
107000
-
-
analytical ultrafiltration
108000
-
-
gel filtration
108000
-
-
gel filtration
110000
-
-
gel filtration
114800
-
-
gel filtration
116000
-
-
gel filtration, the C-terminal fragment comprising residues 441-491 contributes to the anomalous molecular mass determination by gel filtration
120000
-
-
gel filtration
120000
-
-
gel filtration
120000
-
-
gel filtration
120000
-
-
gel filtration
122000
-
-
gel filtration
130000
300000
-
GmPDIL-3a-GmPDIL-3b protein complexes
140000
-
-
gel filtration
140000
-
-
gel filtration
208000
-
Q53LQ0, Q67UF5
PDIL2-3, gel filtration
220000
-
-
PAGE
326000
-
-
gel filtration, in presence of 1 mM Zn2+
additional information
-
-
Zn2+ induces formation of larger enzyme aggregates with MW up to 600 kDa and above
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 61200, SDS-PAGE under reducing conditions
?
-
x * 58900, SDS-PAGE under reducing conditions, other bands with MW 53800 and 55200 represent proteolytic degradation products of the 58900 MW protein
?
-
x * 55000, SDS-PAGE, another band with MW 45000 represents a proteolytic degradation product
?
-
x * 62000, SDS-PAGE
?
-
x * 54300, calculation from nucleotide sequence
?
-
x * 57000, SDS-PAGE
?
-
x * 57000, SDS-PAGE
?
-
x * 55114, calculation from nucleotide sequence
?
-
x * 25910, calculation from nucleotide sequence
?
-
x * 55000, SDS-PAGE
?
-
x * 57000, SDS-PAGE, immunoprecipitation
?
-
x * 58000, recombinant ECaSt/PDI, SDS-PAGE
?
P12865
x * 45000, recombinant PDI-1, SDS-PAGE, x * 80000, recombinant PDI-2, SDS-PAGE
?
-
x * 65000, recombinant mature PDILT without signal sequence, SDS-PAGE
?
-
x * 55000
?
-
x * 55000, SDS-PAGE
?
-
x * 53000, SDS-PAGE
?
-
x * 52000, native enzyme, SDS-PAGE, x * 55000, recombinant His-tagged enzyme, SDS-PAGE
?
A0SHR2, -
x * 55000, SDS-PAGE
?
A5LHV9, A5LHW0, A5LHW1, -
x * 47850, sequence calculation; x * 53680, sequence calculation; x * 54890, sequence calculation
?
Q96DN0
x * 27700, ERp27, SDS-PAGE
?
-
x * 55000, recombinant His-tagged enzyme, SDS-PAGE
?
O13811
x * 39490, sequece calculation
?
-
x * 55000, SDS-PAGE
?
A7YBW7, A7YBX0, A7YBX2, A7YBX4, -
x * 15000, isozyme pdi-15, SDS-PAGE; x * 40000, isozyme pdi-40, SDS-PAGE; x * 47000, isozyme pdi-47, SDS-PAGE; x * 52000, isozyme pdi-52, SDS-PAGE
?
-
x * 60000 and x * 63000, SDS-PAGE; x * 72000, SDS-PAGE
?
E1CAJ6
x * 48074, PDI-P5, sequence calculation, x * 56859, PDIA3, sequence calculation
?
-
x * 54000, ERP-57
?
-, Q5UAH0
x * 55000, recombinant PDI, SDS-PAGE, x * 85000, recombinant GST-tagged PDI, SDS-PAGE
?
-
x * 53100, oxidized enzyme, calculated from amino acid sequence; x * 58800, reduced enzyme, small-angle X-ray scattering; x * 66400, oxidized enzyme, small-angle X-ray scattering
?
-
x * 55000, SDS-PAGE
?
Schizosaccharomyces pombe KP1
-
x * 39490, sequece calculation
-
?
Streptomyces sp. NCIM 5127
-
x * 55000
-
dimer
-
2 * 57000, SDS-PAGE under reducing and nonreducing conditions, association between subunits is noncovalent
dimer
-
2 * 55000, SDS-PAGE
dimer
-
2 * 63000, SDS-PAGE
dimer
-
2 * 60000, SDS-PAGE
dimer
-
2 * 57000, SDS-PAGE
dimer
-
2 * 60000, SDS-PAGE
dimer
-
-
dimer
-
2 * 70000, SDS-PAGE
dimer
-
DsbC contains an N-terminal dimerization domain followed by a linker helix both involved in protein dimerization, the linker helix helps separate the C-terminal catalytic domains
dimer
-
DsbC dimerizes to form a protein binding site flanked by two catalytic thioredoxin domains
dimer
-
2 * 22000, DsbA, SDS-PAGE, 2 * 25000, DsbC, SDS-PAGE
dimer
-
DsbG is a homodimer with an N-terminal dimerization domain on each subunit, crystal structure
dimer
-
2 * 55000, about, sequence calculation, 2 * 52000, analytical ultrafiltration
dimer
-
V-shaped homodimeric modular structures of the dimerization domains and dimer interface of DsbC and DsbG, the dimerization domains fold independently of the catalytic portions of the full-length molecules, overview, each dimeric molecule contains two separate C-terminal thioredoxin-fold domains, joined by hinged helical stalks to a single N-terminal dimerization domain formed from the N-terminal 67 residues of each monomer
dimer
-
and monomer. 2 * 62000, gel filtration, 2 * 56000, calculated
dimer
-
crystallization data
homotetramer
Q53LQ0, Q67UF5
4 * 72397, PDIL2-3, calculated from amino acid sequence
monomer
-
1 * 64000, analytical ultracentrifugation
monomer
-
predominantly, isozyme PDI-22, SDS-PAGE and gel filtration
monomer
-
and dimer. 1 * 62000, gel filtration, 1 * 56000, calculated
multimer
-
x * 52000 + x * ?, SDS-PAGE
oligomer
-
x * 62000, gel filtration, x * 56000, calculated
monomer
-
1 * 21100, estimated from amino acid sequence
additional information
-
PDI is a multifunctional enzyme that acts as beta subunit in prolyl 4-hydroxylases and as a subunit in the microsomal triglyceride transfer protein
additional information
-
PDI consist of 2 catalytically active domains, a and a', and two inactive ones b and b', all four domains have a thioredoxin fold, domain b' contains he primary peptide binding site
additional information
-
PDI domain organization, overview
additional information
-
PDI domain organization, domains a, b, b', a', PDI and P5 contain both two thioredoxin-like domains, domains a and a', at the N-terminus and the C-terminus, respectively, are homologous to thioredoxin and both have an independent active site, each active site contains 2 cysteine residues within the sequence WCGHCK, overview
additional information
-
PDI domain organization, 5 domains a, b, b', a', and c, 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
-
PDI domain organization, Eug1p, Mpd1p, Mpd2p, and Eps1p have only one catalytic domain with 2 cysteines, overview
additional information
-
domain arrangement: two catalytically inactive thioredoxin domains inserted between two catalytically active thioredoxin domains and an acidic C-terminal tail, the four thioredoxin domains form the shape of a twisted U with the active sites facing each other across the long sides, the inside surface is enriched in hydrophobic residues facilitating interactions with misfolded proteins, all 5 domains of PDI are required for full catalytic activity
additional information
-
protein disulfide isomerase-related chaperone Wind contains a thioredoxin fold domain and a C-terminal D-domain unique in PDI-D proteins
additional information
-
PDI domain organization, 5 domains a, b, b', a', and c, the acidic C-terminal domain c, residues 463-491, stabilizes the chaperone function of the enzyme
additional information
-
the catalytic domains a and a' are responsible for the oxidase and the isomerase activity, respectively
additional information
-
non-active site cysteines form a disulfide bridge that is stable even under very reducing environment destabilizing the N-terminal active site disulfide which becomes a 18fold better oxidant by this way
additional information
-
the four domains a, b, b', and a' are arranged in an annular manner
additional information
-
the catalytic domain, residues 88-231, shows a thioredoxin fold with a helical insert
additional information
P07237, P13667, P30101, Q13087
domain structure of isozymes, comparison, overview; domain structure of isozymes, comparison, overview; domain structure of isozymes, comparison, overview; domain structure of isozymes, comparison, overview
additional information
-
a multidomain protein, tertiary structure and function analysis under pressure conditions above 100 MPa, overview
additional information
A3RMS2, -
isozyme domain structure, overview; isozyme domain structure, overview
additional information
-
the enzyme structure contains two thioredoxin-like domains, a and a', and an ERp29c domain, determination by peptide mapping with either trypsin or V8 protease, domain structures, overview
additional information
A0SHR2, -
domain organization of PDI, overview
additional information
Q4Z2V7
structural analysis and comparison of PDIs from different Plasmodium species
additional information
-
structural analysis and comparison of PDIs from different Plasmodium species
additional information
Q2XQR5
structural analysis and comparison of PDIs from different Plasmodium species
additional information
-, Q2XQR3
structural analysis and comparison of PDIs from different Plasmodium species
additional information
Q7RRT0
structural analysis and comparison of PDIs from different Plasmodium species
additional information
Q96DN0
ERp27 is a two-domain protein homologous to the non-catalytic b and b' domains of protein disulfide isomerase, domain structure, thioredoxin site structure and involved residues, overview
additional information
-
primary and secondary PDi structure analysis, overview
additional information
-
tryptic peptide preparation and analysis by MALDI-MS/MS and LC-ESI-MS/MS methods, peptide mapping and amino acid sequence determination, sequence comparison, overview
additional information
Q93YN0
CYO1 has a C4-type zinc finger domain, putative enzyme topology, overview
additional information
P30101
determination and analysis of the crystal structure of the bb domains of ERp57, overview
additional information
-
PDI domain structure, overview
additional information
P17967
PDI domain structure, overview
additional information
-
PDIp exists predominantly as monomer under reducing conditions, but the dimeric form is significantly increased following the removal of the reducing agent, due to the formation of an inter-subunit disulfide bond. The oxidized PDIp exposes more hydrophobic patches and is more sensitive to protease digestion. The formation of the inter-subunit disulfide bond is mainly contributed by its non-active cysteine residue C4. The formation of the inter-subunit disulfide bond is redox-dependent and is favored under oxidizing conditions. PDIp can function as a chaperone to form stable complexes with various non-native cellular proteins, particularly under oxidizing conditions
additional information
-
in solution at low concentration, enzyme comprises mainly monomers. At increasing concentrations, fractions of dimers and higher order oligomers are observed. Oligomerization is not driven by formation of intermolecular disulfide bonds, but by non-covalent interactions
additional information
-
isoform PDIL-1 associates with the precursor of a seed storage protein, proglycinin, and with the alpha' subunit of the seed storage protein beta-conglycinin; isoform PDIL-2 associates with the precursor of a seed storage protein, proglycinin, and with the alpha' subunit of the seed storage protein beta-conglycinin
additional information
-
reconstitution of the Ero1-Lalpha/protein disulfide isomerase oxidative folding system in vitro. The a' domain of protein disulfide isomerase is much more active than the a domain in Ero1-Lalpha-mediated folding. The minimal element for binding to Ero1-Lalpha are core element b, linker x and the a domain
additional information
-
PDI can directly interact with estrogen receptor alpha, but it does not interact with estrogen receptor beta
additional information
Q13087
the two catalytic domains of PDIp, a and a', which contain the WCGHC and WCTHC motifs, respectively, may be responsible for its enzymatic activity, whereas the two non-catalytic domains, b and b', may be involved in substrate-binding
additional information
D0QEL0, -
the PDIA3 sequence contains two PDI-typical thioredoxin active sites of WCGHC
additional information
-
the protein disulfide isomerase exhibits a saturable, substrate binding site. NMR structural analysis of peptide binding pocket of b and b' domains, and interaction analysis of b and b' domains of PDI, the b' domain tends to form dimers, while the b domain moderates the tendency of the b' domain to dimerize and significantly slows interconversion, overview
additional information
-
GmPDIL-3a and GmPDIL-3b are plant endoplasmic reticulum PDI family proteins containing the nonclassic redox center motif CXXS? C
additional information
-, Q5UAH0
structure determination and molecular modeling, overview
additional information
-
the enzyme molecule has four domains a,a', b, and b', each possessing a thioredoxin fold, the domain a and a' show catalytic sites with the Cys-Gly-His-Cys motif, the b and b' domains possess substrate binding sites, domains b' and a' are linked via linker x, and the enbzyme also posseses a C-terminal acidic alpha-helix containing the endoplasmic reticulum retention signal, domain structure, overview
additional information
-
the enzyme molecule has four domains a,a', b, and b', each possessing a thioredoxin fold, the domain a and a' show catalytic sites with the Cys-Gly-His-Cys motif, the b and b' domains possess substrate binding sites, domains b' and a' are linked via linker x, and the enzyme also posseses a C-terminal acidic alpha-helix containing the endoplasmic reticulum retention signal, domain structure, overview
additional information
P55059
the enzyme has a modular structure with four thioredoxin-like domains, a, b, b', and a', along with a C-terminal extension. The homologous a and a' domains contain one cysteine pair in their active site directly involved in thiol-disulfide exchange reactions, while the b' domain putatively provides a primary binding site for unstructured regions of the substrate polypeptides, structure determination and analysis by NMR and small-angle X-ray scattering methods, domain arrangements and redox behaviour, overview
additional information
P38659, -
comparison of structures of b and b' domains and the bb' fragments of ERp57 and ERp72, modelling, overview
additional information
Plasmodium berghei ANKA, Plasmodium knowlesi H, Plasmodium vivax Sal1
-
structural analysis and comparison of PDIs from different Plasmodium species
-
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
glycoprotein
-
very small carbohydrate content, 0.5-1.0%
glycoprotein
-
-
no glycoprotein
-
-
no glycoprotein
-
-
glycoprotein
-
-
glycoprotein
-
PDILT contains 9 putative glycosylation sites
glycoprotein
AY919669, -
O-glycosylation
no glycoprotein
-
-
glycoprotein
-
-
glycoprotein
-
the enzyme has 5 N-glycosylation sites all modified in vivo
glycoprotein
-
PDI is N-glycosylated
glycoprotein
-
expression in Bombyx mori results in production of mostly non-N-glycosylated and some N-glycosylated recombinant protein
glycoprotein
-
-
glycoprotein
P12865
both enzyme forms are N-glycosylated, PDI-1 contains 2 N-glycosylation sites, PDI-2 contains 12 sites
glycoprotein
-
isoform PDIL-1 is N-glycosylated
additional information
-
in vivo, protein disulfide isomerase is present in two semi-oxidized forms in which either the first active site in the a domain or the second active site in the a' domain is oxidized. In HEK-293 cells, about 50% of enzyme is fully reduced, in 18% a domain is oxidized, a' reduced, in 15%, the a domain is reduced, a' oxidized, and 16% of enzyme are fully oxidized
additional information
-
PDIp exists predominantly as monomer under reducing conditions, but the dimeric form is significantly increased following the removal of the reducing agent, due to the formation of an inter-subunit disulfide bond. The oxidized PDIp exposes more hydrophobic patches and is more sensitive to protease digestion. The formation of the inter-subunit disulfide bond is mainly contributed by its non-active cysteine residue C4. The formation of the inter-subunit disulfide bond is redox-dependent and is favored under oxidizing conditions. PDIp can function as a chaperone to form stable complexes with various non-native cellular proteins, particularly under oxidizing conditions
glycoprotein
Saccharomyces cerevisiae trg1/TRG1
-
the enzyme has 5 N-glycosylation sites all modified in vivo
-
additional information
-
autophosphorylation in the central domain
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
crystal structure of reduced and oxidized enzyme
-
purified native and selenomethionine-labeled DsbG in oxidized and in redox-mixed state, DsbG is oxidized by 1.7 mM (1,10-phenanthroline)Cu(II), crystallization in 20% PEG 4000, 0.1 M sodium citrate, pH 3.8-4.2, and 0.2 M ammonium sulfate, X-ray diffraction structure determination and analysis at 1.7-2.0 A resolution
-
purified recombinant His6-tagged DsbC and DsbG dimerization domains, sitting drop vapour-diffusion method, 4-6 mg/ml protein in 25 mM HEPES, pH 7.5, 150 mM NaCl, 0.001 ml of protein and of reservoir solution, containing 2.0 M Li2SO4, 0.1 M MgSO4 and 5% 2-propanol, pH 4.5, are mixed, for crystallization of DsbG also addition of 0.2 M CdCl2 and 33% MPD, X-ray diffraction structure determination and analysis at 2.0 and 1.9 A, respectively
-
purified recombinant reduced DsbC, hanging drop vapour diffusion method, the reservoir solution contains 0.2 M Li2SO4, o.1 M Tris, pH8.4, and 20% PEG 4000, 0.0015 ml of protein and of reservoir solution are mixed, X-ray diffraction reduced structure determination and analysis at 2.5 A resolution
-
ERp57 and its isolated bb' and b' domains in complex with the lectin chaperone calnexin, hanging drop vapour diffusion method, equilibration of 14 mg/ml protein in 50 mM Tris-HCl, 0.15 M NaCl, 1 mM DTT, pH 7.5, against 30% w/v PEG 3350, 0.1 M (NH4)2SO4, 0.1 M HEPES buffer, pH 7.5, for 1-3 days at 20C, X-ray diffraction structure determination and analysis at 2.0 A resoution
P30101
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)
P13667
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
-
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, 20C, X-ray diffraction structure determination and analysis at 1.9 A resolution, overview
P38659, -
purified recombinant residues 23-522 of PDI1, X-ray diffraction structure determination and analysis at 2.4 A resolution, modeling
-
to 3.7 A resolution. PDI is a highly flexible molecule with its catalytic domains, a and a', representing two mobile arms connected to a more rigid core composed of the b and b' domains. The linker between the a domain and the core is more susceptible to degradation than that connecting the a' domain to the core. Molecular flexibility is essential for the enzymatic activity in vitro and in vivo
-
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5
-
-
unstable
5
-
-
stable
10
-
-
1 h, 0C or 37C, highest stability
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
-
-
t1/2: 9 days
25
-
-
t1/2: 27 days
50
-
-
pH 7.5, 1 h, stable up to
50
-
-
15 min, partially purified enzyme, stable
57
-
-
15 min, partially purified enzyme, 25% loss of activity
60
-
-
pH 7.5, 1 h, about 45% loss of activity
62
-
-
15 min, partially purified enzyme, 50% loss of activity
70
75
P27773
CxRP2 is heat sensitive losing substantial activity after 30 min at 70-75C, overview
70
75
-
CxRP2 is heat sensitive losing substantial activity after 30 min at 70-75 C, overview
70
-
-
stable above
80
-
-
pH 7.5, 1 h, about 70% loss of activity
additional information
-
-
the enzyme is highly thermostable
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
unstable to 0.2 M guanidine hydrochloride
-
reduced enzyme is more stable than oxidized enzyme
-
stable to 0.2 M guanidine hydrochloride
-
enzyme stability is considerably higher in endosperm isolated 40 days after anthesis than in mature wheat
-
OXIDATION STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
PDI active site can be reduced by glutathion
-
652503
PDI can be reduced by dithiothreitol
-
650995
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-20C, freeze-dried enzyme, 30% loss of activity after 9 months
-
-20C, freeze-dried form, stable for at least 1 year
-
-20C, stable for several months
-
-20C, enzyme concentrated to 1.5-2 mg/ml, stable for at least 6 months
-
-20C, indefinitely stable
-
4C, 1 mM phenylmethylsulfonyl fluoride, 0.5 mM DTT, 20% w/v glycerol, half-life: 20 days
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
recombinant GST-tagged or His-tagged enzyme from Escherichia coli strain BL21(DE3) by glutathione or nickel affinity chromatography, respectively, native enzyme partially by isoelectric focusing/2D PAGE
A0SHR2, -
from liver
-
native enzyme
-
ox; protein disulfide isomerase activity and glutathione-insulin transhydrogenase activity, EC 1.8.4.2, are catalyzed by a single enzyme protein
-
partial
-
recombiant enzyme from Escherichia coli to homogeneity and over 95% purity
-, Q1HGL1
recombinant His6-tagged wild-type and mutant Wind from Escherichia coli strain XL 1-Blue by nickel affinity chromatography
-
Ni-NTA-agarose column chromatography, gel filtration
-
recombinant DsbC from strain BL21(DE3) by anion exchange chromatography
-
recombinant His6-tagged DsbC by nickel affinity chromatography
-
recombinant His6-tagged isolated dimerization domains of DsbC and DsbG from strain BL21 (DE3) by nickel affinity chromatography and gel filtration
-
partial
-
protein disulfide-isomerase is identical with the beta-subunit of the prolyl 4-hydroxylase tetramer, alpha2beta2
-
gPDI-2-GST fusion protein, glutathione-agarose; gPDI-3-GST fusion protein, glutathione-agarose; gPDI-GST fusion proteins, glutathion-agarose
O97451, O97452, Q9U015
recombinant mature GmPDIL-3a (Thr24-Leu520) and GmPDIL-3b (Ser27-Leu523), excluding the putative signal peptides, from Escherichia coli strain BL21(DE3)
-
from platelet
-
glutathione-Sepharose resin column chromatography and gel filtration
P13667
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
Q96DN0
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 expressed in Escherichia coli
-
recombinant wild-type and mutant enzymes from Escherichia coli
Q13087
chelating Sepharose column chromatography and Resource Q column chromatography
-
native enzyme from tachyzoit extracts by tizoxanide affinity chromatography, recombinant His-tagged enzyme from Escherichia coli by Co2+ affinity chromatography
-
recombinant His-tagged PDI from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration
-
recombinant His-tagged PDI from Escherichia coli by nickel affinnity chromatography
-
recombinant His-tagged DsbA and DsbC from Escherichia coli strain BL(DE3) by nickel affinity chromatography
-
recombinant wild-type and mutant enzyme from Escherichia coli strain BL21(DE3) by heat precipitation at 80C, gel filtration, and anion exchange chromatography
-
native enzyme from brain by anion exchange and bisphenyl A affinity chromatography, recombinant His-tagged enzyme from Escherichia coli by nickel affinity chromatography
-
recombinant b and b' domains and the bb' fragments of ERp57 and ERp72 from Escherichia coli
P38659, -
recombinant PDI
-
recombinant wild-type and mutant PDI from Escherichia coli to homogeneity
-
GST-PDI fusion protein
-
recombinant His-tagged enzyme from Escherichia coli strain AD494(DE3) by nickel affinity chromatography
-
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
-
recombinant His-tagged wild-type PDI and mutant PDI defective in the a' domain from Escherichia coli by nickel affnity chromatography
-
recombinant protein
-
-
Sea urchin
-
recombinant His-tagged mature isozymes PDIA3 and PDI-P5 from Escherichia coli strain HMS174 (DE3) by nickel affinity chromatography and anion exchange chromatography, the His-tag of PDI-P5 is cleaved off
E1CAJ6
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
cloning from RNA by 3' race RT-PCR, DNA and amino acid sequence determination and analysis, sequence comparison, expression as GST-tagged or His-tagged enzyme in Escherichia coli strain BL21(DE3)
A0SHR2, -
gene cyo1, isolation of CYO1 from the cyo1 mutant strain by T-DNA tagging, DNA and amino acid sequence determination and analysis, functional complementation by the wild-type cyo1 gene, cyo1 expression analysis, overview
Q93YN0
expression using baculovirus system
-
functional and mutational analysis of a conserved family of three PDIs in Caenorhabditis elegans; functional and mutational analysis of a conserved family of three PDIs in Caenorhabditis elegans
A3RMS2, -
expression of GFP- or ORF-tagged RB60, wild-type and deletion mutants, in vitro protein synthesis using the T3 TNT-coupled reticulocyte lysate system
-
DNA and amino acid sequence determination and anaylsis, phylogenetic tree, expression in Escherichia coli as a soluble cytoplasmic protein
-, Q1HGL1
expression of enzymatically nonfunctional PDI can restore Chlamydia sp. attachment but not entry into mutant CHO6 cells, while expression of functional PDI restores the complete Chlamydia infection, overview
-
PDI cloning from CHO-K1 cells, expression as N-terminally HA-tagged enzyme in GP2-293 cells, complementation by expression of full-length PDI restores Chlamydia trachomatis binding and infectivity in the enzyme-deficient CHO-6 mutant cell line, as wellas to diphtheria toxin sensitivity, PDI might complement an endoplasmic reticulum transport function, or other indirect functions, resulting in the change of phenotype for chlamydial susceptibility, overview
-
DNA sequence determination, expression of GFP-tagged wild-type enzyme and mutants Y53S and K84D in COS-7 cells, expression of C-terminally or N-terminally His6-tagged wild-type and mutant Wind in Escherichia coli strain XL 1-Blue and in Vero cells, the affinity for substrate Pipe is higher with the N-terminally His-tagged enzyme compared to the C-terminally tagged one
-
expressed in Escherichia coli XL1-Blue MRF' cells
-
in addition to a dsbA-like gene, a dsnC gene, coding for a periplasmic protein with disulfide isomerase activity
-
enzyme form DsbD
-
expressed in Escherichia coli BL21(DE3) cells
-
expression of His6-tagged DsbC
-
expression of His6-tagged isolated dimerization domains of DsbC and DsbG in strain BL21 (DE3)
-
overexpression of DsbC in strain BL21(DE3)
-
-
O97451, O97452, Q9U015
expression in Escherichia coli
-
genes PDIS-1 and PDIS-2, DNA and amino acid sequence determination and anaylsis, expression in Escherichia coli as soluble folded proteins
-
GmPDIL-3a and GmPDIL-3b isozymes, cloning of mature GmPDIL-3a (Thr24-Leu520) and GmPDIL-3b (Ser27-Leu523), excluding the putative signal peptides, expression in Escherichia coli strain BL21(DE3)
-
gene HlPDI-1, DNA and amino acid sequence determination and anaylsis, phylogenetic tree, functional expression in Escherichia coli strain BL21 (DE3); gene HlPDI-2, DNA and amino acid sequence determination and anaylsis, phylogenetic tree, functional expression in Escherichia coli strain BL21 (DE3); gene HlPDI-3, DNA and amino acid sequence determination and anaylsis, phylogenetic tree, functional expression in Escherichia coli strain BL21 (DE3)
A5LHV9, A5LHW0, A5LHW1, -
baculovirus expression system
-
cloning of cDNA
-
cloning of the a and a' domain, expression in Escherichia coli
-
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 and Sf9 insect cells
-
expression of enzyme form PDIp in Escherichia coli
-
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)
P30101
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
-
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
Q13087
sequence comparison; sequence comparison; sequence comparison; sequence comparison
P07237, P13667, P30101, Q13087
the gene encoding ERp27 is located at 14,958,24114,982,750 bp on chromosome 12 and has 7 exons, DNA and amino acid sequence determination and anaylsis, sequence comparison, expression of GFP-fusion ERp27 in COS-7 cell endoplasmic reticulum, expression of N-terminally His-tagged wild-type and mutant ERp57, and of PDI a, b, and b' domains, in Escherichia coli strain BL21(DE3)
Q96DN0
transfection of EA.hy926 cells
-
wild-type and/or mutant PDI overexpression in vascular smooth muscle cells and in HEK-293T cells
-
expressed in Escherichia coli BL21(DE3) cells
-
expression in Bacillus brevis
-
overexpression in Bacillus brevis, secretion to the cell medium
-
gene pdi, DNA and amino avid sequence determination and analysis, expression of PDI in Pichia pastoris strain overexpressing the Plasmodium falciparum disulfide-rich, transmission-blocking vaccine candidate protein Pfs25, isozymes A and B, the co-expression results in 3fold enhanced levels of the Pfs25 isozymes A and B as well as in enhaced PpPDI expression, overview; overexpression of endogenous PDI in clone Pfs25
Q9C1Z8
isozyme pdi-15, DNA and amino acid sequence determination and analysis, sequence comparison with other Leishmania species, overview; isozyme pdi-40, DNA and amino acid sequence determination and analysis, sequence comparison with other Leishmania species, overview; isozyme pdi-47, DNA and amino acid sequence determination and analysis, sequence comparison with other Leishmania species, overview; isozyme pdi-52, DNA and amino acid sequence determination and analysis, sequence comparison with other Leishmania species, overview
A7YBW7, A7YBX0, A7YBX2, A7YBX4, -
cDNA cloning from library, DNA and amino acid sequence determination and analysis, genetic structure comparison and phylogenetic tree
C0JBY4, -
coexpression of wild-type or mutant AGR2 with cysteine-rich regions of MUC2
-
DNA sequence determination of testis-specific PDILT, expression in HeLa cells endoplasmic reticulum as Myc-tagged protein
-
PDI, quantitative expression analysis, overexpression in CHO and in NS0/2N2 cells
-
expression of His-tagged enzyme in Escherichia coli
-
gene pdi, DNA and amino acid sequence determination and analysis, His-tagged PDI is co-expressed with the cyclotide precursor protein Oak1 in Escherichia coli strain BL21(DE3) using the pREP4 helper plasmid
-
expressed in Escherichia coli; expressed in Escherichia coli
Q53LQ0, Q67UF5
DNA and amino acid sequence determination and analysis, sequence comparison and phylogenetic analysis, expression of the enzyme fused to the human tissue plasminogen activator signal sequence in Escherichia coli strain DH10B
Q4Z2V7
PDI, DNA sequence determination and analysis
-, Q5UAH0
expression of His-tagged PDI in Escherichia coli periplasmic space
-
gene pdi, DNA and amino avid sequence determination and anaylsis, expression of PDI in Pichia pastoris strain overexpressing the Plasmodium falciparum disulfide-rich, transmission-blocking vaccine candidate protein Pfs25, isozymes A and B, the co-expression results in enhanced levels of the Pfs25 isozymes A and B as well as enhanced PfPDI expression, overview; overexpression of wild-type isozymes A and B and of the chimeric PDI mutant in Pichia pastoris using the PFs25 clone, co-expression of Pichia pastoris PDI in Pfs25
AY919669, -
isozymes PDI-8, PDI-9, PDI-11, and PDI-14, localization on chromosome-8, chromosome-9, chromosome-11, and chromosome-14, respectively, DNA and amino acid sequence determination and analysis, sequence comparison and phylogenetic analysis, expression of the enzyme fused to the human tissue plasminogen activator signal sequence in Escherichia coli, strain DH10B
-
DNA and amino acid sequence determination and analysis, sequence comparison and phylogenetic analysis, expression of the enzyme fused to the human tissue plasminogen activator signal sequence in Escherichia coli strain DH10B
-, Q2XQR5
DNA and amino acid sequence determination and analysis, sequence comparison and phylogenetic analysis, expression of the enzyme fused to the human tissue plasminogen activator signal sequence in Escherichia coli strain DH10B
-, Q2XQR3
DNA and amino acid sequence determination and analysis, sequence comparison and phylogenetic analysis, expression of the enzyme fused to the human tissue plasminogen activator signal sequence in Escherichia coli strain DH10B
Q7RRT0
genes dsbA and dsbC, DNA sequence determination and analysis, expression of His-tagged DsbA and DsbC in Escherichia coli strain BL(DE3)
-
overexpression of wild-type and mutant enzyme in Escherichia coli strain BL21(DE3)
-
DNA and amino acid sequence determination, expression of His-tagged enzyme in Escherichia coli strain DH5alpha
-
expression in Escherichia coli
-
expression of b and b' domains and the bb' fragments of ERp57 and ERp72 in Escherichia coli
P38659, -
expression of wild-type and mutant PDI in Escherichia coli strain BL21(DE3)
-
overexpression in Escherichia coli
-
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 in Escherichia coli
-
expression in Bombyx mori pupae
-
expression in Escherichia coli
-
expression of GST-PDI fusion protein in Escherichia coli
-
expression of His-tagged enzyme in Escherichia coli strain AD494(DE3)
-
expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
-
expression of His-tagged wild-type PDI and mutant PDI defective in the a' domain, which bears the isomerase activity, in Escherichia coli
-
expression of residues 23-522 of PDI1
-
PDIA3, DNA and amino acid sequence determination and analysis, quantitative expression analysis, genetic structure and phylogenetic analysis
D0QEL0, -
gene PDI, DNA and amino acid sequence determination and analysis, restriction mapping, expression in Escherichia coli strain MV1184
O13811
gene PDI2, DNA and amino acid sequence determination and analysis, cloning into the Escherichia coli-yeast shuttle vector pRS316 to generate the recombinant plasmid pYPDI2 in Escherichia coli strain strain MV1184, which is recombinantly introduced in Schizosaccharomyces pombe cells, that show up to 2.73fold increased PDI enzyme activity, with significantly higher activity in the stationary phase than in the exponential phase
D0EJL8
isozymes PDIA3 and PDI-P5 precursors, DNA and amino acid sequence determination and analysis, expression of His-tagged mature isozymes in Escherichia coli strain HMS174 (DE3)
E1CAJ6
DNA sequence determination of PDI-1 and PDI-2, which show low overall identity, genomic organization and expression analysis in Trypanosoma brucei, expression of both enzyme forms as GST-tagged proteins in Escherichia coli
P12865
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expression of GmPDIL-3a and GmPDIL-3b in the cotyledon increases during seed maturation when synthesis of storage proteins is initiated
-
the enzyme is upregulated in amyotrophic lateral sclerosis
-
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
-
protein disulfide isomerase is highly upregulated in hypoxic myocardial capillary endothelial cells
-
PDI is induced by unfolded protein response, UPR, signaling transduction pathways activated by protein misfolding in the endoplasmic reticulum, overview. PDI is upregulated before symptom onset in spinal cords of mutant SOD1G93A mice
-
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
-
oxidative stress, hypoxia, and toxic perfluorooctane sulfonate exposure induce PDIA3, PDIA3 is significantly increased in the liver of Atlantic salmon exposed to hyperoxic water during smoltification
D0QEL0, -
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
C24S
-
site-directed mutagenesis, unaltered Pipe processing efficiency compared to the wild-type enzyme
C27S
-
site-directed mutagenesis, unaltered Pipe processing efficiency compared to the wild-type enzyme
D29N
-
site-directed mutagenesis, unaltered Pipe processing efficiency compared to the wild-type enzyme
D31N
-
site-directed mutagenesis, unstable protein that still dimerizes but then aggregates, unaltered Pipe processing efficiency compared to the wild-type enzyme
D31N/R41S
-
site-directed mutagenesis, monomeric mutant, slightly decreased Pipe processing efficiency compared to the wild-type enzyme
D50A
-
site-directed mutagenesis, inactive mutant, normal dimerization
D50N
-
site-directed mutagenesis, decreased Pipe processing efficiency compared to the wild-type enzyme
D50S
-
site-directed mutagenesis, altered Pipe targeting compared to the wild-type enzyme, normal dimerization
D85N
-
site-directed mutagenesis, unaltered Pipe processing efficiency compared to the wild-type enzyme
E32K
-
site-directed mutagenesis, unaltered Pipe processing efficiency compared to the wild-type enzyme
E60A
-
site-directed mutagenesis, unaltered Pipe processing and targeting efficiency compared to the wild-type enzyme
E60Q
-
site-directed mutagenesis, decreased Pipe processing efficiency compared to the wild-type enzyme
E60Y
-
site-directed mutagenesis, unaltered Pipe processing and targeting efficiency compared to the wild-type enzyme
E88K
-
site-directed mutagenesis, unaltered Pipe processing efficiency compared to the wild-type enzyme
E88Q
-
site-directed mutagenesis, unaltered Pipe processing efficiency compared to the wild-type enzyme
E90R
-
site-directed mutagenesis, unaltered Pipe processing efficiency comp