5.3.4.1 Agp mutant folding of Agp mutant, DsbC, mutant of Agp, an AppA homologue, containing the AppA nonconsecutive disulfide bond Escherichia coli ? - ? 379171 5.3.4.1 alkaline protease inhibitor folding and rearrangement of alkaline protease inhibitor Streptomyces sp. ? - ? 378410 5.3.4.1 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 Streptomyces sp. ? - ? 378410 5.3.4.1 alkaline protease inhibitor folding and rearrangement of alkaline protease inhibitor Streptomyces sp. NCIM 5127 ? - ? 378410 5.3.4.1 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 Streptomyces sp. NCIM 5127 ? - ? 378410 5.3.4.1 alpha-globulin PDIL1-1 facilitates the oxidative folding of alpha-globulin Oryza sativa ? - ? 416553 5.3.4.1 alpha-synuclein - Humicola insolens ? - ? 444903 5.3.4.1 apolipoprotein B - Homo sapiens ? - ? 444912 5.3.4.1 apolipoprotein B100 the enzyme assists in the oxidative folding of apolipoprotein B100 Rattus norvegicus ? - ? 444212 5.3.4.1 beta-actin - Homo sapiens ? - ? 444277 5.3.4.1 bovine pancreatic trypsin inhibitor - Homo sapiens ? - ? 445282 5.3.4.1 carboxypeptidase Y maturation of carboxypeptidase Y Saccharomyces cerevisiae ? - ? 378644 5.3.4.1 cholera toxin reduced (but not oxidized) protein-disulfide isomerase displaces the cholera toxin A1 subunit from the holotoxin without unfolding the A1 subunit Bos taurus ? - ? 416771 5.3.4.1 citrate synthase DsbG suppresses aggregation of luciferase at 43°C, enzyme has both PDI and chaperone activity Escherichia coli stabilized citrate synthase - ? 368700 5.3.4.1 conotoxin lt14a - Conus caracteristicus ? - ? 445316 5.3.4.1 conotoxin lt14a - Conus coronatus ? - ? 445316 5.3.4.1 conotoxin lt14a - Conus ebraeus ? - ? 445316 5.3.4.1 conotoxin lt14a - Conus lividus ? - ? 445316 5.3.4.1 conotoxin lt14a - Conus miles ? - ? 445316 5.3.4.1 conotoxin lt14a - Conus quercinus ? - ? 445316 5.3.4.1 conotoxin lt14a - Conus striatus ? - ? 445316 5.3.4.1 conotoxin lt14a - Conus tessulatus ? - ? 445316 5.3.4.1 conotoxin lt14a - Conus textile ? - ? 445316 5.3.4.1 conotoxin lt14a - Conus varius ? - ? 445316 5.3.4.1 conotoxin lt14a - Conus vexillum ? - ? 445316 5.3.4.1 conotoxin lt14a - Conus planorbis ? - ? 445316 5.3.4.1 conotoxins sTx3.1 disulfide formation, macromolecular crowding has little effect on the protein disulfide isomerase-catalyzed oxidative folding and disulfide isomerization of conotoxin Conus marmoreus ? - ? 391684 5.3.4.1 conotoxins tx3a disulfide formation, macromolecular crowding has little effect on the protein disulfide isomerase-catalyzed oxidative folding and disulfide isomerization of conotoxin Conus marmoreus ? - ? 391685 5.3.4.1 creatine kinase 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 Homo sapiens ? - ? 379609 5.3.4.1 D-glyceraldehyde 3-phosphate dehydrogenase - Homo sapiens ? - ? 445401 5.3.4.1 degenerated RNase type III 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 Trypanosoma brucei ? - ? 379694 5.3.4.1 denatured D-glceraldehyde-3-phosphate dehydrogenase interaction of PDI with cyclophilin B increases its chaperone activity Bos taurus refolded D-glceraldehyde-3-phosphate dehydrogenase - ? 368727 5.3.4.1 denatured D-glyceraldehyde-3-phosphate dehydrogenase chaperone activity of PDI Homo sapiens refolded D-glyceraldehyde-3-phosphate dehydrogenase - ? 368724 5.3.4.1 denatured eclosion hormone PDI acts as a chaperone and refolds the insect neuropeptide eclosion hormone Bos taurus active eclosion hormon - ? 368722 5.3.4.1 denatured lysozyme PDI catalyzes the formation, rearrangement, and breakage of disulfide bonds, oxidative refolding by PDI almost completely restores lysozyme activity, overview Humicola insolens ? - ? 391811 5.3.4.1 denatured lysozyme - Conus caracteristicus native lysozyme - ? 445439 5.3.4.1 denatured lysozyme - Conus coronatus native lysozyme - ? 445439 5.3.4.1 denatured lysozyme - Conus ebraeus native lysozyme - ? 445439 5.3.4.1 denatured lysozyme - Conus lividus native lysozyme - ? 445439 5.3.4.1 denatured lysozyme - Conus miles native lysozyme - ? 445439 5.3.4.1 denatured lysozyme - Conus quercinus native lysozyme - ? 445439 5.3.4.1 denatured lysozyme - Conus striatus native lysozyme - ? 445439 5.3.4.1 denatured lysozyme - Conus tessulatus native lysozyme - ? 445439 5.3.4.1 denatured lysozyme - Conus textile native lysozyme - ? 445439 5.3.4.1 denatured lysozyme - Conus varius native lysozyme - ? 445439 5.3.4.1 denatured lysozyme - Conus vexillum native lysozyme - ? 445439 5.3.4.1 denatured lysozyme - Conus planorbis native lysozyme - ? 445439 5.3.4.1 denatured rhodanese interaction of PDI with cyclophilin B increases its chaperone activity Bos taurus refolded rhodanese - ? 368726 5.3.4.1 denatured rhodanese PDI exhibits chaperone activity with rhodanese Homo sapiens ? - ? 416876 5.3.4.1 denatured RNase A recombinant CYO1 renatures RNase A Arabidopsis thaliana ? - ? 391812 5.3.4.1 denatured Rnase A - Glycine max active Rnase A - ? 400830 5.3.4.1 denatured RNase A + GSH - Chlamydomonas reinhardtii renatured RNase A + GSSG - ? 427426 5.3.4.1 denatured-reduced lysozyme oxidase activity of PDI Entamoeba histolytica ? - ? 416877 5.3.4.1 dieosin glutathione disulfide - Homo sapiens eosin glutathione sulfide - ? 445445 5.3.4.1 E2A homodimer 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 Homo sapiens E2A-basic helix-loop-helix protein heterodimer - ? 368698 5.3.4.1 envelope glycoprotein 120 i.e. human immunodeficiency virus gp120 Homo sapiens envelope glycoprotein 120 - ? 368711 5.3.4.1 estrogen receptor alpha 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 Homo sapiens ? - ? 390212 5.3.4.1 estrogen receptor alpha 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 Homo sapiens ? - ? 390212 5.3.4.1 folded cholera toxin 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 Saccharomyces cerevisiae unfolded cholera toxin - ? 368716 5.3.4.1 glutathione disulfide - Homo sapiens glutathione - ? 444336 5.3.4.1 glycoprotein 120 PDI may play a role in HIV-1 infection by reducing HIV-1 envelope glycoprotein 120 Bos taurus glycoprotein 120 - ? 368713 5.3.4.1 GSSG disulfide reduction of GSSG, the disulfide reduction activity of both PDI-thioredoxin reductase and PDI-DTT is reduced Bos taurus GSH - ? 379812 5.3.4.1 HED-SSM a mixed disulfide Corynebacterium glutamicum MSH + HED - ? 461612 5.3.4.1 HED-SSM a mixed disulfide Corynebacterium glutamicum LMG 3730 MSH + HED - ? 461612 5.3.4.1 HED-SSM a mixed disulfide Corynebacterium glutamicum BCRC 11384 MSH + HED - ? 461612 5.3.4.1 HED-SSM a mixed disulfide Corynebacterium glutamicum ATCC 13032 MSH + HED - ? 461612 5.3.4.1 HED-SSM a mixed disulfide Corynebacterium glutamicum JCM 1318 MSH + HED - ? 461612 5.3.4.1 HED-SSM a mixed disulfide Corynebacterium glutamicum NCIMB 10025 MSH + HED - ? 461612 5.3.4.1 HED-SSM a mixed disulfide Corynebacterium glutamicum DSM 20300 MSH + HED - ? 461612 5.3.4.1 insulin - Homo sapiens ? - ? 379955 5.3.4.1 insulin - Bos taurus ? - ? 379955 5.3.4.1 insulin - Populus trichocarpa x Populus deltoides ? - ? 379955 5.3.4.1 insulin - Leishmania amazonensis ? - ? 379955 5.3.4.1 insulin - Oryza sativa Japonica Group ? - ? 379955 5.3.4.1 insulin disulfide-bond reduction in substrate insulin, reduction activity by Holmgren's turbimetric method Pyrococcus furiosus ? - ? 379955 5.3.4.1 insulin 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 Bos taurus ? - ? 379955 5.3.4.1 insulin bovine substrate, reduction of disulfide bonds Plasmodium falciparum ? - ? 379955 5.3.4.1 insulin recombinant CYO1 accelerates disulfide bond reduction in the model substrate insulin Arabidopsis thaliana ? - ? 379955 5.3.4.1 insulin reduction of disulfide bonds Neospora caninum ? - ? 379955 5.3.4.1 insulin reduction of insulin disulfide bonds Schizosaccharomyces pombe ? - ? 379955 5.3.4.1 insulin reduction of sidulfide bonds Bos taurus ? - ? 379955 5.3.4.1 insulin PDI exhibits reductase activity with insulin Homo sapiens ? - ? 379955 5.3.4.1 insulin reductase activity of PDI Entamoeba histolytica ? - ? 379955 5.3.4.1 insulin reduction of insulin disulfide bonds Schizosaccharomyces pombe 972 ? - ? 379955 5.3.4.1 insulin - Rattus norvegicus reduced insulin - ? 445561 5.3.4.1 insulin - Homo sapiens reduced insulin - ? 445561 5.3.4.1 insulin + DTT bovine substrate, reductase activity with DTT Amblyomma variegatum ? - ? 392264 5.3.4.1 Insulin-(SS) + dithiothreitol - Dickeya chrysanthemi Insulin-(SH)2 + oxidized dithiothreitol - ? 1127 5.3.4.1 Insulin-(SS) + GSH - Mus musculus Insulin-(SH)2 + GSSG - ? 1126 5.3.4.1 Insulin-(SS) + GSH - Homo sapiens Insulin-(SH)2 + GSSG - ? 1126 5.3.4.1 Insulin-(SS) + GSH - Rattus norvegicus Insulin-(SH)2 + GSSG - ? 1126 5.3.4.1 Insulin-(SS) + GSH - Bos taurus Insulin-(SH)2 + GSSG - ? 1126 5.3.4.1 Insulin-(SS) + GSH - Oryctolagus cuniculus Insulin-(SH)2 + GSSG - ? 1126 5.3.4.1 Insulin-(SS) + GSH - Mesocricetus auratus Insulin-(SH)2 + GSSG - ? 1126 5.3.4.1 Insulin-(SS) + GSH - Humicola insolens Insulin-(SH)2 + GSSG - ? 1126 5.3.4.1 Insulin-(SS) + GSH - Leishmania major Insulin-(SH)2 + GSSG - ? 1126 5.3.4.1 Insulin-(SS) + GSH - Angiostrongylus cantonensis Insulin-(SH)2 + GSSG - ? 1126 5.3.4.1 Insulin-(SS) + GSH protein disulfide isomerase supports proinsulin folding as chaperone and isomerase Homo sapiens Insulin-(SH)2 + GSSG - ? 1126 5.3.4.1 Insulin-(SS) + GSH - Leishmania major MHOM/TN/94/GLC94 Insulin-(SH)2 + GSSG - ? 1126 5.3.4.1 integrin alphaIIb - Mesocricetus auratus ? - ? 445562 5.3.4.1 integrin alphaIIbbeta3 - Homo sapiens ? - ? 444339 5.3.4.1 integrin alphaMb2 - Homo sapiens ? - ? 444340 5.3.4.1 integrin alphaVb3 - Homo sapiens ? - ? 444341 5.3.4.1 integrin alphaVbeta3 - Homo sapiens ? - ? 444342 5.3.4.1 integrin beta3 - Mesocricetus auratus ? - ? 445563 5.3.4.1 integrin subunit alpha11 the enzyme activates integrin subunit alpha11 Homo sapiens ? - ? 444343 5.3.4.1 integrin subunit beta1 the enzyme activates integrin subunit beta1 Homo sapiens ? - ? 444344 5.3.4.1 kalata B1 and derivatives, PDI dramatically enhanced the correct oxidative folding of linear and cyclic kalata B1 at physiological pH, determination of folding intermediates Oldenlandia affinis ? - ? 392304 5.3.4.1 lactate dehydrogenase 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 Homo sapiens ? - ? 380043 5.3.4.1 luciferase DsbG suppresses aggregation of luciferase at 43°C, enzyme has both PDI and chaperone activity Escherichia coli stabilized luciferase - ? 368699 5.3.4.1 lysozyme PDI has antichaperone activity facilitating protein aggregation Rattus norvegicus aggregated lysozyme - ? 368707 5.3.4.1 lysozyme 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 Conus marmoreus ? - ? 392514 5.3.4.1 additional information - Bos taurus ? - ? 89 5.3.4.1 additional information 3,3',5-triiodo-L-thyronine-binding activity Bos taurus ? - ? 89 5.3.4.1 additional information PDI has dehydroascorbate reductase activity Rattus norvegicus ? - ? 89 5.3.4.1 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 eukaryota ? - ? 89 5.3.4.1 additional information the enzyme has an essential role that is distinct from its function in formation of native disulphides Saccharomyces cerevisiae ? - ? 89 5.3.4.1 additional information the enzyme acts as a thyroid-hormone binding protein eukaryota ? - ? 89 5.3.4.1 additional information the enzyme may be significant in the action of triiodothyronine towards the target cells Bos taurus ? - ? 89 5.3.4.1 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 Mammalia ? - ? 89 5.3.4.1 additional information PDI has dehydroascorbate reductase activity, PDI may play a role in the intraluminal dehydroascorbate reduction Rattus norvegicus ? - ? 89 5.3.4.1 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 Streptomyces sp. ? - ? 89 5.3.4.1 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 Pseudomonas aeruginosa ? - ? 89 5.3.4.1 additional information DsbC resolves incorrect disulfides whose formation has been catalyzed by redox-active copper Escherichia coli ? - ? 89 5.3.4.1 additional information essential enzyme for yeast cell growth, both oxidase and isomerase activities are required Saccharomyces cerevisiae ? - ? 89 5.3.4.1 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 Rattus norvegicus ? - ? 89 5.3.4.1 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 Bos taurus ? - ? 89 5.3.4.1 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 Homo sapiens ? - ? 89 5.3.4.1 additional information PDI plays a key role in catalyzing the folding of secretory proteins Saccharomyces cerevisiae ? - ? 89 5.3.4.1 additional information PDILT forms intermolecular disulfide bonds in testis Mus musculus ? - ? 89 5.3.4.1 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 Chlamydomonas reinhardtii ? - ? 89 5.3.4.1 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 Saccharomyces cerevisiae ? - ? 89 5.3.4.1 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 Escherichia coli ? - ? 89 5.3.4.1 additional information the enzyme is an essential catalyst of disulfide formation with two cysteines in the active site facilitating thiol-disulfide exchange Saccharomyces cerevisiae ? - ? 89 5.3.4.1 additional information the enzyme plays a crucial role in folding periplasmatically excreted proteins Escherichia coli ? - ? 89 5.3.4.1 additional information the organism is completely dependent on PDI activity for growth Saccharomyces cerevisiae ? - ? 89 5.3.4.1 additional information the single domain PDI-1 and the class 1 PDI-2 are not essential for the organism Trypanosoma brucei ? - ? 89 5.3.4.1 additional information all 5 domains of PDI are required for full catalytic activity Saccharomyces cerevisiae ? - ? 89 5.3.4.1 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 Escherichia coli ? - ? 89 5.3.4.1 additional information DsbC and DbsG also possess thioredoxin-like domains, substrate specificity of PDI Escherichia coli ? - ? 89 5.3.4.1 additional information Eug1p, Mpd1p, Mpd2p, and Eps1p partially compensate for PDI, substrate specificity of PDI Saccharomyces cerevisiae ? - ? 89 5.3.4.1 additional information isomerase activity is assayed using the insulin/glutathione coupled assay Homo sapiens ? - ? 89 5.3.4.1 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 Saccharomyces cerevisiae ? - ? 89 5.3.4.1 additional information PDI is a better thiol oxidant than a disulfide protein reductant Bos taurus ? - ? 89 5.3.4.1 additional information PDILT forms intermolecular disulfide bonds, but shows no intramolecular disulfide bonds Mus musculus ? - ? 89 5.3.4.1 additional information substrate disulfide bonds, overview, the AppA homologue Agp, a periplasmic phosphatase, lacks nonconsecutive disulfide bonds and is no substrate for DsbC Escherichia coli ? - ? 89 5.3.4.1 additional information substrate specificity of PDI Homo sapiens ? - ? 89 5.3.4.1 additional information substrate specificity of PDI Rattus norvegicus ? - ? 89 5.3.4.1 additional information substrate specificity of PDI Bos taurus ? - ? 89 5.3.4.1 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 Pyrococcus furiosus ? - ? 89 5.3.4.1 additional information the four domains a, b, b', and a' show cooperative properties in both isomerase and chaperone functions of PDi Homo sapiens ? - ? 89 5.3.4.1 additional information 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 Trypanosoma brucei ? - ? 89 5.3.4.1 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 Saccharomyces cerevisiae ? - ? 89 5.3.4.1 additional information cell-surface PDI is required for transnitrosation of metallothionein by S-nitroso-albumin in intact pulmonary vascular endothelial cells, overview Rattus norvegicus ? - ? 89 5.3.4.1 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 Escherichia coli ? - ? 89 5.3.4.1 additional information HlPDI-1 might be involved in tick blood feeding and Babesia parasite infection in ticks Haemaphysalis longicornis ? - ? 89 5.3.4.1 additional information HlPDI-3 might be involved in tick blood feeding and Babesia parasite infection in ticks Haemaphysalis longicornis ? - ? 89 5.3.4.1 additional information in vivo, disulfide bond formation is mainly catalyzed by protein disulfide isomerase Conus marmoreus ? - ? 89 5.3.4.1 additional information 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 Amblyomma variegatum ? - ? 89 5.3.4.1 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 Homo sapiens ? - ? 89 5.3.4.1 additional information 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 Caenorhabditis elegans ? - ? 89 5.3.4.1 additional information 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 Caenorhabditis elegans ? - ? 89 5.3.4.1 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 Rattus norvegicus ? - ? 89 5.3.4.1 additional information PDI is involved in the cellular growth and response to nutritional and oxidative stress, regulation, overview Schizosaccharomyces pombe ? - ? 89 5.3.4.1 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 Escherichia coli ? - ? 89 5.3.4.1 additional information 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 Homo sapiens ? - ? 89 5.3.4.1 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 Chlamydomonas reinhardtii ? - ? 89 5.3.4.1 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 Mus musculus ? - ? 89 5.3.4.1 additional information structure and mechanism of PDI in disulfide formation and oxidative protein folding, overview Chlamydomonas reinhardtii ? - ? 89 5.3.4.1 additional information structure and mechanism of PDI in disulfide formation and oxidative protein folding, overview Arabidopsis thaliana ? - ? 89 5.3.4.1 additional information structure and mechanism of PDI in disulfide formation and oxidative protein folding, overview Homo sapiens ? - ? 89 5.3.4.1 additional information structure and mechanism of PDI in disulfide formation and oxidative protein folding, overview Saccharomyces cerevisiae ? - ? 89 5.3.4.1 additional information 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 Arabidopsis thaliana ? - ? 89 5.3.4.1 additional information the enzyme assists protein folding in malaria parasites Plasmodium falciparum ? - ? 89 5.3.4.1 additional information the enzyme assists protein folding in malaria parasites Plasmodium berghei ? - ? 89 5.3.4.1 additional information the enzyme assists protein folding in malaria parasites Plasmodium vivax ? - ? 89 5.3.4.1 additional information the enzyme assists protein folding in malaria parasites Plasmodium knowlesi ? - ? 89 5.3.4.1 additional information the enzyme assists protein folding in malaria parasites Plasmodium yoelii ? - ? 89 5.3.4.1 additional information 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 Homo sapiens ? - ? 89 5.3.4.1 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 Cricetulus griseus ? - ? 89 5.3.4.1 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 Oldenlandia affinis ? - ? 89 5.3.4.1 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 Homo sapiens ? - ? 89 5.3.4.1 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 Glycine max ? - ? 89 5.3.4.1 additional information 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 Homo sapiens ? - ? 89 5.3.4.1 additional information ERp57 interacts with the lectin chaperone calnexin, binding structure, and active site structure, overview Homo sapiens ? - ? 89 5.3.4.1 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 Escherichia coli ? - ? 89 5.3.4.1 additional information PDI also functions as a dehydroascorbate reductase and a molecular chaperone besides its disulfide-isomerizing function Humicola insolens ? - ? 89 5.3.4.1 additional information PDI has the ability to catalyze dithiol-disulfide exchange reactions, chaperone activity and propensity to form subunits of multi-enzyme complexes, overview Escherichia coli ? - ? 89 5.3.4.1 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 Oldenlandia affinis ? - ? 89 5.3.4.1 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 Chlamydomonas reinhardtii ? - ? 89 5.3.4.1 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 Arabidopsis thaliana ? - ? 89 5.3.4.1 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 Homo sapiens ? - ? 89 5.3.4.1 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 Saccharomyces cerevisiae ? - ? 89 5.3.4.1 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 Glycine max ? - ? 89 5.3.4.1 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 Chlamydomonas reinhardtii ? - ? 89 5.3.4.1 additional information 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 Homo sapiens ? - ? 89 5.3.4.1 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 Plasmodium falciparum ? - ? 89 5.3.4.1 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 Plasmodium berghei ? - ? 89 5.3.4.1 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 Plasmodium vivax ? - ? 89 5.3.4.1 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 Plasmodium knowlesi ? - ? 89 5.3.4.1 additional information 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 Plasmodium yoelii ? - ? 89 5.3.4.1 additional information the enzyme mediates conformational changes by thiol-disulfide exchange Mus musculus ? - ? 89 5.3.4.1 additional information the enzyme shows disulfide exchange activity Homo sapiens ? - ? 89 5.3.4.1 additional information the enzyme shows disulfide oxidase/isomerase, reductase, and chaperone activities, overview Plasmodium falciparum ? - ? 89 5.3.4.1 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 Bos taurus ? - ? 89 5.3.4.1 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 Escherichia coli ? - ? 89 5.3.4.1 additional information the enzyme shows dithiol-disulfide-oxidoreductase activity, and contains a conserved WCGHC active site and two thioredoxin domains Amblyomma variegatum ? - ? 89 5.3.4.1 additional information the enzyme shows hormone binding activity, e.g. of L-T3 and 17beta-estradiol hormones Rattus norvegicus ? - ? 89 5.3.4.1 additional information the enzyme shows oxidase and isomerase activities, overview Conus marmoreus ? - ? 89 5.3.4.1 additional information enzyme is involved in the proper folding or quality control of storage proteins Glycine max ? - ? 89 5.3.4.1 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 Homo sapiens ? - ? 89 5.3.4.1 additional information PDI is required in vivo for both fibrin generation and platelet thrombus formation Mus musculus ? - ? 89 5.3.4.1 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 Rattus norvegicus ? - ? 89 5.3.4.1 additional information protein disulfide isomerase contributes to the activation of cryptic initiator protein tissue factoron microvesicles in vitro Homo sapiens ? - ? 89 5.3.4.1 additional information protein disulfide isomerase directly promotes initiator protein tissue factor-dependent fibrin production during thrombus formation in vivo Mus musculus ? - ? 89 5.3.4.1 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 Homo sapiens ? - ? 89 5.3.4.1 additional information 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 Haemaphysalis longicornis ? - ? 89 5.3.4.1 additional information enzyme converts initiator protein tissue factor cysteine residues from glutathionylated to disulfide state Mus musculus ? - ? 89 5.3.4.1 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 Homo sapiens ? - ? 89 5.3.4.1 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 Bos taurus ? - ? 89 5.3.4.1 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 Homo sapiens ? - ? 89 5.3.4.1 additional information protein disulfide isomerase has a concentration-dependent chaperone-activity and inhibits the aggregation of rhodanese, which has no disulfide bonds Saccharomyces cerevisiae ? - ? 89 5.3.4.1 additional information recombinant human PDI does not influence factor X activation by factor VIIa soluble tissue factor Homo sapiens ? - ? 89 5.3.4.1 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 Homo sapiens ? - ? 89 5.3.4.1 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 Homo sapiens ? - ? 89 5.3.4.1 additional information 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 Homo sapiens ? - ? 89 5.3.4.1 additional information AGR2 is essential for production of intestinal mucin MUC2, but is not required for establishment of intestinal secretory epithelial cell lineages Mus musculus ? - ? 89 5.3.4.1 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 Homo sapiens ? - ? 89 5.3.4.1 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 Glycine max ? - ? 89 5.3.4.1 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 Saccharomyces cerevisiae ? - ? 89 5.3.4.1 additional information PDI catalyzes disulfide bond formation in the endoplasmic reticulum Homo sapiens ? - ? 89 5.3.4.1 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 Rattus norvegicus ? - ? 89 5.3.4.1 additional information 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 Humicola insolens ? - ? 89 5.3.4.1 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 Bos taurus ? - ? 89 5.3.4.1 additional information PDI specifically associates with signal peptide peptidase, SPP, independently of human cytomegalovirus glycoprotein US2, but not with Derlin-1 Homo sapiens ? - ? 89 5.3.4.1 additional information PDI specifically binds 3,3',5-triiodo-L-thyronine Mus musculus ? - ? 89 5.3.4.1 additional information PDI specifically binds 3,3',5-triiodo-L-thyronine Homo sapiens ? - ? 89 5.3.4.1 additional information PDI specifically binds 3,3',5-triiodo-L-thyronine Rattus norvegicus ? - ? 89 5.3.4.1 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 Rattus norvegicus ? - ? 89 5.3.4.1 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 Mus musculus ? - ? 89 5.3.4.1 additional information 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 Sus scrofa ? - ? 89 5.3.4.1 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 Rattus norvegicus ? - ? 89 5.3.4.1 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 Cricetulus griseus ? - ? 89 5.3.4.1 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 Homo sapiens ? - ? 89 5.3.4.1 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 Mus musculus ? - ? 89 5.3.4.1 additional information ERp72 substrate specificity of ERp72, overview. Ep72 does not interact with calnexin Rattus norvegicus ? - ? 89 5.3.4.1 additional information 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 Homo sapiens ? - ? 89 5.3.4.1 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 Rattus norvegicus ? - ? 89 5.3.4.1 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 Saccharomyces cerevisiae ? - ? 89 5.3.4.1 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 Homo sapiens ? - ? 89 5.3.4.1 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 Bos taurus ? - ? 89 5.3.4.1 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 Glycine max ? - ? 89 5.3.4.1 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 Entamoeba histolytica ? - ? 89 5.3.4.1 additional information 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 Humicola insolens ? - ? 89 5.3.4.1 additional information the enzyme renatures denatured RNase A Rattus norvegicus ? - ? 89 5.3.4.1 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 Mus musculus ? - ? 89 5.3.4.1 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 Homo sapiens ? - ? 89 5.3.4.1 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 Rattus norvegicus ? - ? 89 5.3.4.1 additional information the isozymes catalyze refolding of reduced and denatured lysozyme Sus scrofa ? - ? 89 5.3.4.1 additional information PDI behaves mainly as an oxidase/isomerase and exhibits chaperone-like activity Entamoeba histolytica ? - ? 89 5.3.4.1 additional information PDI catalyzes the isomerization of disulfide bonds on misfolded proteins Bos taurus ? - ? 89 5.3.4.1 additional information PDI directly interacts with calreticulin Homo sapiens ? - ? 89 5.3.4.1 additional information PDIL2-3 activity is dispensable in the oxidative folding of alpha-globulin Oryza sativa ? - ? 89 5.3.4.1 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 Bos taurus ? - ? 89 5.3.4.1 additional information the enzyme has a single E2-binding site Homo sapiens ? - ? 89 5.3.4.1 additional information the enzyme has three catalytic activities including thiol-disulfide oxireductase, disulfide isomerase, and redox-dependent chaperone Homo sapiens ? - ? 89 5.3.4.1 additional information isoform PDI-A shows no activity with insulin, NADPH thioredoxin reductase , NADP malate dehydrogenase, peroxiredoxin, or RNase A Populus trichocarpa x Populus deltoides ? - ? 89 5.3.4.1 additional information the enzyme has oxidative folding activity Arabidopsis thaliana ? - ? 89 5.3.4.1 additional information TXNDC5 directly interacts with Srx through its thioredoxin-like domains, binding and in vivo complexing analysis. The Srx-TXNDC5 interaction is not affected by the treatment of cells with exogenous H2O2 Homo sapiens ? - - 89 5.3.4.1 additional information NCgl2478 reduces S-mycothiolated mixed disulfides and intramolecular disulfides via a monothiol-disulfide and a dithiol-disulfide exchange mechanism, respectively. NCgl2478 lacks oxidase activity. HED-SSM is a mixed disulfide between monothiol-disulfide (MSH) and 2-hydroxyethyl disulfide (HED) and a substrate of the enzyme. The enzyme performs reduction of insulin occurred via a dithiol mechanism Corynebacterium glutamicum ? - - 89 5.3.4.1 additional information NCgl2478 reduces S-mycothiolated mixed disulfides and intramolecular disulfides via a monothiol-disulfide and a dithiol-disulfide exchange mechanism, respectively. NCgl2478 lacks oxidase activity. HED-SSM is a mixed disulfide between monothiol-disulfide (MSH) and 2-hydroxyethyl disulfide (HED) and a substrate of the enzyme. The enzyme performs reduction of insulin occurred via a dithiol mechanism Corynebacterium glutamicum LMG 3730 ? - - 89 5.3.4.1 additional information the enzyme assists protein folding in malaria parasites Plasmodium berghei ANKA ? - ? 89 5.3.4.1 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 Plasmodium berghei ANKA ? - ? 89 5.3.4.1 additional information NCgl2478 reduces S-mycothiolated mixed disulfides and intramolecular disulfides via a monothiol-disulfide and a dithiol-disulfide exchange mechanism, respectively. NCgl2478 lacks oxidase activity. HED-SSM is a mixed disulfide between monothiol-disulfide (MSH) and 2-hydroxyethyl disulfide (HED) and a substrate of the enzyme. The enzyme performs reduction of insulin occurred via a dithiol mechanism Corynebacterium glutamicum BCRC 11384 ? - - 89 5.3.4.1 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 Streptomyces sp. NCIM 5127 ? - ? 89 5.3.4.1 additional information the enzyme has a single E2-binding site Homo sapiens ATCC 6706839 ? - ? 89 5.3.4.1 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 Chlamydomonas reinhardtii 2137a ? - ? 89 5.3.4.1 additional information NCgl2478 reduces S-mycothiolated mixed disulfides and intramolecular disulfides via a monothiol-disulfide and a dithiol-disulfide exchange mechanism, respectively. NCgl2478 lacks oxidase activity. HED-SSM is a mixed disulfide between monothiol-disulfide (MSH) and 2-hydroxyethyl disulfide (HED) and a substrate of the enzyme. The enzyme performs reduction of insulin occurred via a dithiol mechanism Corynebacterium glutamicum ATCC 13032 ? - - 89 5.3.4.1 additional information the enzyme assists protein folding in malaria parasites Plasmodium knowlesi H ? - ? 89 5.3.4.1 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 Plasmodium knowlesi H ? - ? 89 5.3.4.1 additional information PDI is involved in the cellular growth and response to nutritional and oxidative stress, regulation, overview Schizosaccharomyces pombe 972 ? - ? 89 5.3.4.1 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 Mus musculus C57BL/6 ? - ? 89 5.3.4.1 additional information NCgl2478 reduces S-mycothiolated mixed disulfides and intramolecular disulfides via a monothiol-disulfide and a dithiol-disulfide exchange mechanism, respectively. NCgl2478 lacks oxidase activity. HED-SSM is a mixed disulfide between monothiol-disulfide (MSH) and 2-hydroxyethyl disulfide (HED) and a substrate of the enzyme. The enzyme performs reduction of insulin occurred via a dithiol mechanism Corynebacterium glutamicum JCM 1318 ? - - 89 5.3.4.1 additional information the enzyme assists protein folding in malaria parasites Plasmodium vivax Sal1 ? - ? 89 5.3.4.1 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 Plasmodium vivax Sal1 ? - ? 89 5.3.4.1 additional information NCgl2478 reduces S-mycothiolated mixed disulfides and intramolecular disulfides via a monothiol-disulfide and a dithiol-disulfide exchange mechanism, respectively. NCgl2478 lacks oxidase activity. HED-SSM is a mixed disulfide between monothiol-disulfide (MSH) and 2-hydroxyethyl disulfide (HED) and a substrate of the enzyme. The enzyme performs reduction of insulin occurred via a dithiol mechanism Corynebacterium glutamicum NCIMB 10025 ? - - 89 5.3.4.1 additional information the organism is completely dependent on PDI activity for growth Saccharomyces cerevisiae trg1/TRG1 ? - ? 89 5.3.4.1 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 Saccharomyces cerevisiae trg1/TRG1 ? - ? 89 5.3.4.1 additional information NCgl2478 reduces S-mycothiolated mixed disulfides and intramolecular disulfides via a monothiol-disulfide and a dithiol-disulfide exchange mechanism, respectively. NCgl2478 lacks oxidase activity. HED-SSM is a mixed disulfide between monothiol-disulfide (MSH) and 2-hydroxyethyl disulfide (HED) and a substrate of the enzyme. The enzyme performs reduction of insulin occurred via a dithiol mechanism Corynebacterium glutamicum DSM 20300 ? - - 89 5.3.4.1 NADP malate dehydrogenase substrate for isoform PDI-M only Populus trichocarpa x Populus deltoides ? - ? 445743 5.3.4.1 NADPH oxidase A - Botrytis cinerea ? - ? 444376 5.3.4.1 NADPH thioredoxin reductase - Populus trichocarpa x Populus deltoides ? - ? 445744 5.3.4.1 neuronal nitric oxide synthase the enzyme catalyzes neuronal nitric oxide synthase dimerization Mus musculus ? - ? 444380 5.3.4.1 NRCSQGSCWN - Homo sapiens NRCSQGSCWN - ? 368705 5.3.4.1 NRCSQGSCWN - Arabidopsis thaliana ? - ? 380137 5.3.4.1 NRCSQGSCWN disulfide-bond formation within the thiol substrate peptide NRCSQGSCWN, oxidation activity requires GSH/GSSG Pyrococcus furiosus ? - ? 380137 5.3.4.1 oxidized insulin - Arabidopsis thaliana reduced insulin - ? 445776 5.3.4.1 oxidized insulin + dithiothreitol gPDI-2, low activity with gPDI-3, no activity with gPDI-1 Giardia intestinalis reduced insulin - ? 368733 5.3.4.1 oxidoreductase Ero1 disulfide bond formation in the oxidoreductase Ero1, endoplasmic reticular protein interacts with PDILT Mus musculus ? - ? 380179 5.3.4.1 peroxiredoxin - Populus trichocarpa x Populus deltoides ? - ? 445786 5.3.4.1 phytase 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 Escherichia coli ? - ? 380208 5.3.4.1 Pipe 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 Drosophila melanogaster ? - ? 380209 5.3.4.1 procollagen I - Homo sapiens ? - ? 445833 5.3.4.1 procollagen III - Homo sapiens ? - ? 445832 5.3.4.1 protein-(SSG)2n - Homo sapiens protein(SS)n + n(GSSG) - ? 444392 5.3.4.1 Proteins - Gallus gallus Proteins - ? 1125 5.3.4.1 Proteins - Bacteria Proteins - ? 1125 5.3.4.1 Proteins - eukaryota Proteins - ? 1125 5.3.4.1 Proteins - Escherichia coli Proteins - ? 1125 5.3.4.1 Proteins - Homo sapiens Proteins - ? 1125 5.3.4.1 Proteins - Rattus norvegicus Proteins - ? 1125 5.3.4.1 Proteins - Saccharomyces cerevisiae Proteins - ? 1125 5.3.4.1 Proteins - Bos taurus Proteins - ? 1125 5.3.4.1 Proteins - Oryctolagus cuniculus Proteins - ? 1125 5.3.4.1 Proteins - Trypanosoma brucei Proteins - ? 1125 5.3.4.1 Proteins refolding of scrambled ribonuclease Homo sapiens Proteins with correct disulfide bonds ? 1125 5.3.4.1 Proteins refolding of scrambled ribonuclease Saccharomyces cerevisiae Proteins with correct disulfide bonds ? 1125 5.3.4.1 Proteins refolding of scrambled ribonuclease Humicola insolens Proteins with correct disulfide bonds ? 1125 5.3.4.1 Proteins native, reduced or with wrong disulfide bonds Gallus gallus Proteins with correct disulfide bonds ? 1125 5.3.4.1 Proteins native, reduced or with wrong disulfide bonds Mammalia Proteins with correct disulfide bonds ? 1125 5.3.4.1 Proteins native, reduced or with wrong disulfide bonds Bacteria Proteins with correct disulfide bonds ? 1125 5.3.4.1 Proteins native, reduced or with wrong disulfide bonds eukaryota Proteins with correct disulfide bonds ? 1125 5.3.4.1 Proteins native, reduced or with wrong disulfide bonds Chlamydomonas reinhardtii Proteins with correct disulfide bonds ? 1125 5.3.4.1 Proteins native, reduced or with wrong disulfide bonds Mus musculus Proteins with correct disulfide bonds ? 1125 5.3.4.1 Proteins native, reduced or with wrong disulfide bonds Escherichia coli Proteins with correct disulfide bonds ? 1125 5.3.4.1 Proteins native, reduced or with wrong disulfide bonds Homo sapiens Proteins with correct disulfide bonds ? 1125 5.3.4.1 Proteins native, reduced or with wrong disulfide bonds Rattus norvegicus Proteins with correct disulfide bonds ? 1125 5.3.4.1 Proteins native, reduced or with wrong disulfide bonds Saccharomyces cerevisiae Proteins with correct disulfide bonds ? 1125 5.3.4.1 Proteins native, reduced or with wrong disulfide bonds Bos taurus Proteins with correct disulfide bonds ? 1125 5.3.4.1 Proteins native, reduced or with wrong disulfide bonds Triticum aestivum Proteins with correct disulfide bonds ? 1125 5.3.4.1 Proteins native, reduced or with wrong disulfide bonds Oryctolagus cuniculus Proteins with correct disulfide bonds ? 1125 5.3.4.1 Proteins native, reduced or with wrong disulfide bonds Ovis aries Proteins with correct disulfide bonds ? 1125 5.3.4.1 Proteins native, reduced or with wrong disulfide bonds Aspergillus niger Proteins with correct disulfide bonds ? 1125 5.3.4.1 Proteins native, reduced or with wrong disulfide bonds Glycine max Proteins with correct disulfide bonds ? 1125 5.3.4.1 Proteins native, reduced or with wrong disulfide bonds Klebsiella aerogenes Proteins with correct disulfide bonds ? 1125 5.3.4.1 Proteins native, reduced or with wrong disulfide bonds Pseudomonas aeruginosa Proteins with correct disulfide bonds ? 1125 5.3.4.1 Proteins native, reduced or with wrong disulfide bonds Pseudomonas stutzeri Proteins with correct disulfide bonds ? 1125 5.3.4.1 Proteins native, reduced or with wrong disulfide bonds Canis lupus familiaris Proteins with correct disulfide bonds ? 1125 5.3.4.1 Proteins native, reduced or with wrong disulfide bonds Proteus mirabilis Proteins with correct disulfide bonds ? 1125 5.3.4.1 Proteins native, reduced or with wrong disulfide bonds Ricinus communis Proteins with correct disulfide bonds ? 1125 5.3.4.1 Proteins native, reduced or with wrong disulfide bonds Dickeya chrysanthemi Proteins with correct disulfide bonds ? 1125 5.3.4.1 Proteins native, reduced or with wrong disulfide bonds Schistosoma mansoni Proteins with correct disulfide bonds ? 1125 5.3.4.1 Proteins native, reduced or with wrong disulfide bonds Methylophilus methylotrophus Proteins with correct disulfide bonds ? 1125 5.3.4.1 Proteins native, reduced or with wrong disulfide bonds Providencia sp. Proteins with correct disulfide bonds ? 1125 5.3.4.1 Proteins native, reduced or with wrong disulfide bonds Humicola insolens Proteins with correct disulfide bonds ? 1125 5.3.4.1 Proteins cosubstrate: DTT, 2-mercaptoethanol, GSH, or Cys Saccharomyces cerevisiae Proteins with correct disulfide bonds ? 1125 5.3.4.1 Proteins cosubstrate: DTT, 2-mercaptoethanol, GSH, or Cys Bos taurus Proteins with correct disulfide bonds ? 1125 5.3.4.1 Proteins incorrectly disulfide-linked Bowman Birk soybean trypsin Glycine max Proteins with correct disulfide bonds ? 1125 5.3.4.1 Proteins eduction of insulin and oxidative folding of ribonuclease A Rattus norvegicus Proteins with correct disulfide bonds ? 1125 5.3.4.1 Proteins incorrectly disulfide-linked lysozyme Glycine max Proteins with correct disulfide bonds ? 1125 5.3.4.1 Proteins cosubstrate dithiothreitol can be replaced by GSH, cysteamine, 2-mercaptoethanol, thioglycollic acid or L-Cys, but at significantly higher concentrations Bos taurus Proteins with correct disulfide bonds ? 1125 5.3.4.1 Proteins refolding of scrambled lysosyme Humicola insolens Proteins with correct disulfide bonds ? 1125 5.3.4.1 Proteins incorrectly disulfide-linked RNAse Rattus norvegicus Proteins with correct disulfide bonds ? 1125 5.3.4.1 Proteins incorrectly disulfide-linked RNAse Glycine max Proteins with correct disulfide bonds ? 1125 5.3.4.1 Proteins refolding and activation of human carbonic anhydrase IV, GSSG promotes the activation Escherichia coli Proteins with correct disulfide bonds ? 1125 5.3.4.1 Proteins incorrectly disulfide-linked bovine pancreatic ribonuclease Gallus gallus Proteins with correct disulfide bonds ? 1125 5.3.4.1 Proteins incorrectly disulfide-linked ribonuclease Bos taurus Proteins with correct disulfide bonds ? 1125 5.3.4.1 Proteins - Bacteria ? - ? 369260 5.3.4.1 Proteins - Homo sapiens ? - ? 369260 5.3.4.1 Proteins - Rattus norvegicus ? - ? 369260 5.3.4.1 Proteins - Bos taurus ? - ? 369260 5.3.4.1 Proteins - Canis lupus familiaris ? - ? 369260 5.3.4.1 Proteins native, reduced or with wrong disulfide bonds eukaryota ? - ? 369260 5.3.4.1 Proteins native, reduced or with wrong disulfide bonds Escherichia coli ? - ? 369260 5.3.4.1 Proteins native, reduced or with wrong disulfide bonds Homo sapiens ? - ? 369260 5.3.4.1 Proteins native, reduced or with wrong disulfide bonds Rattus norvegicus ? - ? 369260 5.3.4.1 Proteins native, reduced or with wrong disulfide bonds Bos taurus ? - ? 369260 5.3.4.1 Proteins native, reduced or with wrong disulfide bonds Triticum aestivum ? - ? 369260 5.3.4.1 Proteins native, reduced or with wrong disulfide bonds Klebsiella aerogenes ? - ? 369260 5.3.4.1 Proteins native, reduced or with wrong disulfide bonds Pseudomonas aeruginosa ? - ? 369260 5.3.4.1 Proteins native, reduced or with wrong disulfide bonds Pseudomonas stutzeri ? - ? 369260 5.3.4.1 Proteins native, reduced or with wrong disulfide bonds Proteus mirabilis ? - ? 369260 5.3.4.1 Proteins native, reduced or with wrong disulfide bonds Methylophilus methylotrophus ? - ? 369260 5.3.4.1 Proteins native, reduced or with wrong disulfide bonds Providencia sp. ? - ? 369260 5.3.4.1 Proteins involved in the assembly of wheat storage proteins within the endoplasmic reticulum Triticum aestivum ? - ? 369260 5.3.4.1 Proteins proposed physiological role as catalyst of formation of native disulfide bonds in nascent and newly synthesized secretory proteins Rattus norvegicus ? - ? 369260 5.3.4.1 Proteins facilitates the formation of the correct disulfide bonds within newly synthesized polypeptides Bos taurus ? - ? 369260 5.3.4.1 Proteins 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 Bos taurus ? - ? 369260 5.3.4.1 Proteins enzyme may play a physiological role in the catalysis of S-S-bond formation in prolactin Canis lupus familiaris ? - ? 369260 5.3.4.1 Proteins enzyme may be involved in the formation of intra-chain and inter-chain disulfide bonds in procollagen Gallus gallus ? - ? 369260 5.3.4.1 Proteins enzyme may be involved in the formation of intra-chain and inter-chain disulfide bonds in procollagen Mus musculus ? - ? 369260 5.3.4.1 Proteins enzyme may be involved in the formation of intra-chain and inter-chain disulfide bonds in procollagen Homo sapiens ? - ? 369260 5.3.4.1 Proteins involved in cotranslational disulfide bond formation Rattus norvegicus ? - ? 369260 5.3.4.1 Proteins involved in cotranslational disulfide bond formation Bos taurus ? - ? 369260 5.3.4.1 Proteins may play a role in the formation of disulfide bonds in extracellular and periplasmic proteins Escherichia coli ? - ? 369260 5.3.4.1 Proteins may play a role in the formation of disulfide bonds in extracellular and periplasmic proteins Klebsiella aerogenes ? - ? 369260 5.3.4.1 Proteins may play a role in the formation of disulfide bonds in extracellular and periplasmic proteins Pseudomonas aeruginosa ? - ? 369260 5.3.4.1 Proteins may play a role in the formation of disulfide bonds in extracellular and periplasmic proteins Pseudomonas stutzeri ? - ? 369260 5.3.4.1 Proteins may play a role in the formation of disulfide bonds in extracellular and periplasmic proteins Proteus mirabilis ? - ? 369260 5.3.4.1 Proteins may play a role in the formation of disulfide bonds in extracellular and periplasmic proteins Methylophilus methylotrophus ? - ? 369260 5.3.4.1 Proteins may play a role in the formation of disulfide bonds in extracellular and periplasmic proteins Providencia sp. ? - ? 369260 5.3.4.1 Proteins facilitates the formation of disulfides during the folding and processing of membrane and secretory proteins eukaryota ? - ? 369260 5.3.4.1 Proteins catalysis of native disulfide bond formation Mammalia ? - ? 369260 5.3.4.1 Proteins platelet enzyme may play a role in the various haemostatic and tissue remodelling processes in which platelets are involved Homo sapiens ? - ? 369260 5.3.4.1 Proteins may play a role in retaining prolyl 4-hydroxylase in its native conformation Gallus gallus ? - ? 369260 5.3.4.1 Proteins plays a role in the formation of disulfide bonds during biosynthesis of wheat storage proteins Triticum aestivum ? - ? 369260 5.3.4.1 Proteins implicated in the biosynthesis of secretory proteins Homo sapiens ? - ? 369260 5.3.4.1 Proteins implicated in the biosynthesis of secretory proteins Rattus norvegicus ? - ? 369260 5.3.4.1 Proteins implicated in the biosynthesis of secretory proteins Bos taurus ? - ? 369260 5.3.4.1 Proteins 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 Mammalia ? - ? 369260 5.3.4.1 reduced bovine pancreatic trypsin inhibitor gPDI-2, no cativity with gPDI-1 and gPDI-3 Giardia intestinalis oxidized bovine pancreatic trypsin inhibitor - ? 368732 5.3.4.1 reduced denatured RNase A + GSH - Angiostrongylus cantonensis reduced renatured RNase A + GSSG - ? 427521 5.3.4.1 reduced Ero1alpha - Homo sapiens oxidized Ero1alpha - ? 445858 5.3.4.1 reduced glutathione peroxidase 7 - Homo sapiens oxidized glutathione peroxidase 7 - ? 445859 5.3.4.1 reduced glutathione peroxidase 8 - Homo sapiens oxidized glutathione peroxidase 8 - ? 445860 5.3.4.1 reduced ribonuclease refolding of reduced ribonuclease in presence of glutathione, isomerase activity of PDI Rattus norvegicus ? - ? 380253 5.3.4.1 reduced ribonuclease A - Triticum aestivum denatured ribonuclease A - ? 444396 5.3.4.1 reduced RNase - Schistosoma japonicum denatured RNase - ? 444397 5.3.4.1 reduced RNase A - Bombyx mori RNase A - ? 401838 5.3.4.1 refolding of RNase renaturation of reduced RNase Saccharomyces cerevisiae ? - ? 380254 5.3.4.1 rhodanese chaperone activity Homo sapiens ? - ? 380219 5.3.4.1 rhodanese prevention of rhodanese degeneration, chaperone activity Saccharomyces cerevisiae ? - ? 380219 5.3.4.1 rhodanese the protein substrate is devoid of disulfide bonds, chaperone activity Plasmodium falciparum ? - ? 380219 5.3.4.1 rhodanese prevention of rhodanese degeneration, chaperone activity Saccharomyces cerevisiae trg1/TRG1 ? - ? 380219 5.3.4.1 riboflavin binding protein 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 Homo sapiens ? - ? 401845 5.3.4.1 ribonuclease - Triticum aestivum ? - ? 380256 5.3.4.1 ribonuclease refolding of ribonuclease, isomerase activity, renaturation of reduced ribonuclease, in presence of GSH and GSSG Saccharomyces cerevisiae ? - ? 380256 5.3.4.1 ribonuclease + dithiothreitol - Bos taurus ? - ? 453619 5.3.4.1 ribonuclease A 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 Homo sapiens ? - ? 401846 5.3.4.1 ribonuclease T1 - Homo sapiens ? - ? 445865 5.3.4.1 ricin reductive activation of ricin and ricin A-chain immunotoxins, assay system involving thioredoxin reductase and NADPH, overview Bos taurus ? - ? 380258 5.3.4.1 ricin A-chain immunotoxins reductive activation of ricin and ricin A-chain immunotoxins, assay system involving thioredoxin reductase and NADPH, overview Bos taurus ? - ? 380257 5.3.4.1 RNase - Homo sapiens ? - ? 380259 5.3.4.1 RNase refolding of RNase, renaturation of reduced and of scrambled RNase with almost equal activity Saccharomyces cerevisiae ? - ? 380259 5.3.4.1 RNase refolding of RNase, renaturation of reduced bovine pancreatic RNase Escherichia coli ? - ? 380259 5.3.4.1 RNase the enzyme is able to renature the denatured and reduced RNase Mus musculus ? - ? 380259 5.3.4.1 RNase A - Bos taurus ? - ? 393432 5.3.4.1 RNase A - Populus trichocarpa x Populus deltoides ? - ? 393432 5.3.4.1 RNase A reduced and denatured substrate from bovine pancreas Rattus norvegicus ? - ? 393432 5.3.4.1 RNase A reduced and denatured substrate, oxidase/isomerase activity on the refolding of the substrate Plasmodium falciparum ? - ? 393432 5.3.4.1 RNase A 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 Homo sapiens ? - ? 393432 5.3.4.1 RNase A 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 Homo sapiens ? - ? 393432 5.3.4.1 RNase A oxidase activity of PDI Entamoeba histolytica ? - ? 393432 5.3.4.1 RNase A PDI exhibits isomerase activity with RNase A Homo sapiens ? - ? 393432 5.3.4.1 RNase A + DTT the enzyme contains a WCGHCK active site Haemaphysalis longicornis ? - ? 393430 5.3.4.1 RNase A + DTT the enzyme contains a WCGHCQ active site Haemaphysalis longicornis ? - ? 393430 5.3.4.1 RNase B 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 Homo sapiens ? - ? 393434 5.3.4.1 scrambled reoxidized lysozyme isomerase activity of PDI Entamoeba histolytica ? - ? 417612 5.3.4.1 scrambled ribonuclease - Bos taurus ? - ? 453623 5.3.4.1 scrambled ribonuclease - Humicola insolens ? - ? 453623 5.3.4.1 scrambled RNAse - Leishmania amazonensis ? - ? 393484 5.3.4.1 scrambled RNAse + 2-mercaptoethanol - Saccharomyces cerevisiae ? - ? 453620 5.3.4.1 scrambled RNAse + 2-mercaptoethanol - Bos taurus ? - ? 453620 5.3.4.1 scrambled RNAse + cysteine - Saccharomyces cerevisiae ? - ? 453621 5.3.4.1 scrambled RNAse + cysteine - Bos taurus ? - ? 453621 5.3.4.1 scrambled RNAse + dithiothreitol - Bos taurus ? - ? 453622 5.3.4.1 scrambled RNase A - Bombyx mori RNase A - ? 401878 5.3.4.1 scrambled RNAse A the enzyme catalyzes intramolecular disulfide interchange in scrambled RNase A and restores both native disulfide pairing and ribonuclease activity Saccharolobus solfataricus ? - ? 428933 5.3.4.1 scrambled RNAse A the enzyme catalyzes intramolecular disulfide interchange in scrambled RNase A and restores both native disulfide pairing and ribonuclease activity Saccharolobus solfataricus P2 ? - ? 428933 5.3.4.1 sRNase - Homo sapiens ? - ? 454085 5.3.4.1 tachyplesin I - Homo sapiens ? - ? 445898 5.3.4.1 TAMRAX3CX4CX2-CONH2 - Bos taurus ? - ? 417691 5.3.4.1 thrombospondin-1 + alpha-thrombin + antithrombin III PDI catalyzes formation of disulfide linked complexes of thrombospondin Homo sapiens thrombospondin-1-S-S-alpha-thrombin-S-S-antithrombin III - ? 368725 5.3.4.1 tissue factor - Homo sapiens ? - ? 390327 5.3.4.1 tissue factor 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 Homo sapiens ? - ? 390327 5.3.4.1 tissue factor 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 Homo sapiens ? - ? 390327 5.3.4.1 transforming growth factor-beta1 - Homo sapiens ? - ? 444414 5.3.4.1 tyramine-S-S-poly(D-lysine) - Bos taurus tyramine-SH + HS-poly(D-lysine) - ? 368714 5.3.4.1 unfolded acidic phospholipase A2 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% Sus scrofa refolded acidic phospholipase A2 - ? 368719 5.3.4.1 unfolded bovine pancreatic ribonuclease A + oxidized glutathione oxidative folding of RNase A, 12fold rate acceleration in the presence of PDI Bos taurus refolded bovine pancreatic ribonuclease A + reduced glutathione - ? 368704 5.3.4.1 unfolded bovine pancreatic trypsin inhibitor - Homo sapiens refolded bovine pancreatic trypsin inhibitor - ? 368710 5.3.4.1 unfolded bovine pancreatic trypsin inhibitor - Oryctolagus cuniculus refolded bovine pancreatic trypsin inhibitor - ? 368710 5.3.4.1 unfolded bovine pancreatic trypsin inhibitor - Echinoidea refolded bovine pancreatic trypsin inhibitor - ? 368710 5.3.4.1 unfolded bovine pancreatic trypsin inhibitor oxidative refolding of denatured bovine pancreatic trypsin inhibitor Saccharomyces cerevisiae refolded bovine pancreatic trypsin inhibitor + oxidized glutathione - ? 368728 5.3.4.1 unfolded bovine pancreatic trypsin inhibitor - Giardia intestinalis folded bovine pancreatic trypsin inhibitor - ? 368730 5.3.4.1 unfolded disulfide-bonded protein - Homo sapiens refolded disulfide-bonded protein - ? 368735 5.3.4.1 unfolded insulin - Sus scrofa refolded insulin - ? 368718 5.3.4.1 unfolded insulin - Giardia intestinalis folded insulin - ? 368731 5.3.4.1 unfolded insulin + reduced glutathione - Homo sapiens refolded insulin + oxidized glutathione - ? 368708 5.3.4.1 unfolded insulin beta-chain - Rattus norvegicus refolded insulin beta-chain - ? 368702 5.3.4.1 unfolded lysozyme oxidative refolding of reduced and denatured lysozyme in glutathione redox buffer Saccharomyces cerevisiae refolded lysozyme - ? 368720 5.3.4.1 unfolded mitochondrial malate dehydrogenase maximum refolding when the PDI concentration is 20fold higher than the malate dehydrogenase concentration Sus scrofa refolded mitochondrial malate dehydrogenase - ? 368734 5.3.4.1 unfolded pro-carboxypeptidase Y - Saccharomyces cerevisiae refolded pro-carboxypeptidase Y - ? 368729 5.3.4.1 unfolded proinsulin 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 Homo sapiens refolded proinsulin - ? 368715 5.3.4.1 unfolded RNase - Homo sapiens refolded RNase - ? 368706 5.3.4.1 unfolded RNase - Bos taurus refolded RNase - ? 368706 5.3.4.1 unfolded RNase - Giardia intestinalis refolded RNase - ? 368706 5.3.4.1 unfolded RNase oxidative folding of RNase Homo sapiens refolded RNase - ? 368706 5.3.4.1 unfolded RNase 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 Homo sapiens refolded RNase - ? 368706 5.3.4.1 unfolded RNase A - Homo sapiens refolded RNase A - ? 368712 5.3.4.1 unfolded RNase A - Bos taurus refolded RNase A - ? 368712 5.3.4.1 unfolded RNase A all five consecutive PDI domains, a-b-b'-a'-c are necessary for PDI's disulfide isomerase and chaperone activity Homo sapiens refolded RNase A - ? 368712 5.3.4.1 unfolded RNase A PDI binds to DNA and may be involved in DNA-nuclear matrix anchoring Homo sapiens refolded RNase A - ? 368712 5.3.4.1 unfolded RNase A PDI catalyzes disulfide isomerization of misfolded, i.e. scrambled RNaseA into native RNase A Homo sapiens refolded RNase A - ? 368712 5.3.4.1 unfolded RNase A PDI functions in a plasma environment Homo sapiens refolded RNase A - ? 368712 5.3.4.1 unfolded RNase A 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 Homo sapiens refolded RNase A - ? 368712 5.3.4.1 unfolded RNase A tyrosine and tryptophane residues in peptides are the recognition motifs for their binding Ovis aries refolded RNase A - ? 368712 5.3.4.1 unfolded RNase A - Sus scrofa refolded RNase - ? 368723 5.3.4.1 unfolded RNase A + reduced glutathione - Bos taurus refolded RNase A + oxidized glutathione - ? 368721 5.3.4.1 unfolded rRNaSe refolding of reduced rRNaSe Homo sapiens refolded rRNase - ? 368709 5.3.4.1 unofolded bovine pancreatic ribonuclease A + oxidized dithiothreitol oxidative folding of RNase A Bos taurus refolded bovine pancreatic ribonuclease A + reduced dithiothreitol - ? 368703 5.3.4.1 vitronectin + thrombin + antithrombin PDI catalyzes the formation of disulfide-linked complexes of vitronectin with thrombin-antithrombin Homo sapiens vitronectin-thrombin-antithrombin - ? 368717