5.3.4.1: protein disulfide-isomerase
This is an abbreviated version!
For detailed information about protein disulfide-isomerase, go to the full flat file.
Reaction
catalyses the rearrangement of -S-S- bonds in proteins
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Synonyms
5'-MD, 58 kDa glucose regulated protein, 58 kDa microsomal protein, AGR2, anterior gradient homolog 2, BPA-binding protein, CaBP1, CaBP2, Cellular thyroid hormone binding protein, cotyledon-specific chloroplast biogenesis factor CYO1, CYO1, DbsG, disulfide bond isomerase, disulfide bond-forming enzyme, Disulfide interchange enzyme, disulfide isomerase, Disulfide isomerase ER-60, disulfide-bond isomerase, dithiol-disulfide isomerase, Dsb, DsbA, DsbB, DsbC, DsbD, DsbG, ECaSt/PDI, endoplasmic reticulum protein EUG1, Eps1p, ER protein 57, ER58, ER60, ERcalcistorin/protein-disulfide isomerase, ERdj5, Ero1, Erp, ERP-57, ERp-72 homolog, ERp18, ERp27, ERp28, ERp44, Erp46, ERp5, ERp57, ERP59, ERP60, ERp72, Eug1p, fibronectin, gPDI-1, gPDI-2, gPDI-3, HIP-70, HlPDI-1, HlPDI-2, HlPDI-3, Iodothyronine 5'-monodeiodinase, More, Mpd1p, Mpd2p, multifunctional protein disulfide isomerase, ncgl2478, P5, P55, P58, pancreas-specific protein disulfide isomerase, PDI, PDI A4, PDI I, PDI II, pdi-15, PDI-1a, pdi-40, pdi-47, pdi-52, PDI-A, PDI-M, PDI-P5, PDI-related protein, PDI1, PDI11, PDI2, PDI7, PDI8, PDIA1, PDIA2, PDIA3, PDIA4, PDIA6, PDIL-1, PDIL-2, PDIL1-1, PDIL1;1, PDIL1Aalpha, PDIL1B, PDIL2, PDIL2-3, PDIL3A, PDIL4D, PDIL5A, PDILT, PDIp, PDIr, protein disulfide isomerase, protein disulfide isomerase 1, protein disulfide isomerase 2, protein disulfide isomerase 3, protein disulfide isomerase A1, protein disulfide isomerase A3, protein disulfide isomerase A5, protein disulfide isomerase A6, protein disulfide isomerase associated 3, Protein disulfide isomerase P5, protein disulfide isomerase-1, protein disulfide isomerase-11, protein disulfide isomerase-2, protein disulfide isomerase-3, protein disulfide isomerase-8, protein disulfide isomerase-like protein of the testis, protein disulfide isomerase-P5, protein disulfide isomerase-related chaperone Wind, Protein disulfide isomerase-related protein, protein disulfide oxidoreductase, protein disulfide reductase/isomerase, protein disulfide-isomerase A4, Protein disulphide isomerase, Protein ERp-72, protein-disulfide isomerase, R-cognin, RB60, Rearrangease, Reduced ribonuclease reactivating enzyme, Retina cognin, S-S rearrangase, SSO0192, SsPDO, thiol-disulfide oxidoreductase, thiol-protein oxidoreductase, thioredoxin domain-containing protein 5, Thyroid hormone-binding protein, Thyroxine deiodinase, TXNDC5, yPDI
ECTree
Application
Application on EC 5.3.4.1 - protein disulfide-isomerase
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drug development
PDI constitutes a potential target for the development of alternative therapy strategies based on the inhibition of folding and chaperoning of exported proteins
industry
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PDI assists incorporation of cysteine-containing compounds (CCCs) into hair and wool substrates in order to generate milder methods to dye hair with longer lasting colour by creating new disulfide bonds between hair and peptide. PDI-assists promotion of the migration of CCCs (dyes), previously attached to keratin, along hair fibres, to avoid repetitive hair dyeing procedures. PDI induces controlled release of a CCC protein (e.g. reduced form of RNase A) from wool matrices
pharmacology
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protein disulfide isomerase is a potential therapeutic target in amyotrophic lateral sclerosis and (+-)-trans-1,2-bis(mercaptoacetamido)cyclohexane and other molecular mimics of protein disulfide isomerase could be of benefit in amyotrophic lateral sclerosis and other neurodegenerative diseases related to protein misfolding
analysis
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development of a method to determine quantitatively the redox state of active-site cysteines found in the Cys-Xaa-Xaa-Cys motif in living cells. Method is based on the alkylation of cysteines by methoxy polyethylene glycol 5000 maleimide. In vivo, protein disulfide isomerase is present in two semi-oxidized forms in which either the first active site in the a domain or the second active site in the a' domain is oxidized. In HEK-293 cells, about 50% of enzyme is fully reduced, in 18% a domain is oxidized, a' reduced, in 15%, the a domain is reduced, a' oxidized, and 16% of enzyme are fully oxidized
analysis
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study on the critical influence of reference genes used for data normalization, shown for protein disulfide isomerase
analysis
PDIA3 and C/EBP? may be valuable markers in fish for exposure and effect to environmental stress
biotechnology
overexpression of Plasmodium falciparum PDI isozymes A and B for production of a disulfide-rich transmission-blocking vaccine candidate Pfs25 in Pichia pastoris, the expression level is enhance by co-expression of the endogenous Pichia pastoris enzyme in Pfs25 3fold, production method evaluation
biotechnology
AY919669
overexpression of Plasmodium falciparum PDI isozymes A and B for production of a disulfide-rich transmission-blocking vaccine candidate Pfs25 in Pichia pastoris, the expression level is enhanced by co-expression of the endogenous Pichia pastoris enzyme in Pfs25 clone 3fold, production method evaluation
diagnostics
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the absence of PDIp expression in pancreatic adenocarcinoma may serve as an additional biomarker for pancreatic cancer
diagnostics
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the absence of PDIp expression in pancreatic adenocarcinoma may serve as an additional biomarker for pancreatic cancer
diagnostics
lung cancer patients with high Srx levels have significantly shorter survival and those with high TXNDC5 levels have longer survival. Cellular levels of Srx and TXNDC5 may be useful as biomarkers to predict the survival of individuals with lung cancer
medicine
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inhibition of isoform procollagen-proline, 2-oxoglutarate-4-dioxygenase beta subunit activity increases apoptosis in response to agents which induce ER-stress such as fenretinide and velcade
medicine
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lipopolysaccharide decreases protein disulfide isomerase protein expression by 33% in RAW 264.7 cells. Incubation of the cells with bacitracin significantly decreases tumor necrosis factor alpha gene expression and release. Downregulation of protein disulfide isomerase gene expression by siRNA correlates with a 3.2fold increase in tumor necrosis factor alpha release into the cell supernatant
medicine
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overexpression has significant effects on cell-cell fusion mediated by Newcastle disease virus. Overexpression results in increased membrane fusion, and enhanced production of free thiols in Newcastle disease virus fusion protein when expressed without hemagglutinin-neuraminidase protein but drecreased free thiols in Newcastle disease virus fusion protein expressed with hemagglutinin-neuraminidase protein. Overexpression favors a postfusion conformation of surface-expressed Newcastle disease virus fusion protein in the presence of hemagglutinin-neuraminidase protein
medicine
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PDI is required in vivo for both fibrin generation and platelet thrombus formation
medicine
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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. Patients with type II diabetes show increased levles of enzyme-containing microparticles in their plasma
medicine
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protein disulfide gene expression is significantly decreased by 28% and 69% at 20 h after cecal ligation and puncture or lipopolysaccharide infusion, respectively
medicine
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protein disulfide isomerase directly promotes initiator protein tissue factor-dependent fibrin production during thrombus formation in vivo. After endothelial denudation of carotid artery, enzyme is released at the injury site from adherent platelets and disrupted vessel walls. Inhibition of the enzyme decreases initiator protein tissue factor-triggered fibrin formation. Enzyme infusion increases fibrin generation at the injury site
medicine
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protein disulfide isomerase PDI directly interacts with thiol-containing fibrinogen receptor alphaIIbbeta3. PDI has greater ability to isomerize disulfide bonds than the alphaIIbbeta3 integrin. Anti-PDI antibodies inhibit signalling-independent activation of the thiol-containing fibrinogen receptor alphaIIbbeta3 by Mn2+
medicine
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PDI represents a potential drug target for anti-amebic therapy
medicine
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protein disulfide isomerase upregulation is e.g. associated with cancer, attention-deficite hyperactivity disorder, Alzheimer disease, amyotrophic lateral sclerosis, perinatal asphyxia, brain ischemia, sporadic Creutzfeldt-Jacob disease, major depression, brain injury, tuberous sclerosis, endothelial function, acute coronary syndrome, iscemic heart disease, hepatosteatosis, varioliform gastritis, preeclampsia, obesity, insulin resistance, diabetes, congenital hypothyroid goiter, Helicobacter pylori infection, peridontitis, dehydration, aging, or pregnancy
medicine
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the enzyme is a therapeutic target for preventing and treating inappropriate neutrophil sequestration
medicine
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the enzyme is a therapeutic target for preventing and treating inappropriate neutrophil sequestration
synthesis
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useful in facilitating the in vitro folding of proteins
synthesis
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useful in facilitating the in vitro folding of proteins
synthesis
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development of a versatile baculovirus expression and secretion system, using the enzyme as a fusion partner. Fusion improves the secretions and antibacterial activities of recombinant nuecin proteins and may be used for large-scale production of bioactive proteines