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.
Word Map on EC 5.3.4.1
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5.3.4.1
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collagen
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laminin
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integrins
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endothelial
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actin
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fibrosis
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adhesive
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basement
-
mesenchymal
-
vessel
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fiber
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metastasis
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proteoglycans
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vitronectin
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fibrinogen
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matrices
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nephropathy
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albumin
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gelatin
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interstitial
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mesangial
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platelet
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monolayer
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cytoskeleton
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glomerular
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rgd
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vimentin
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e-cadherin
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cell-cell
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adhesions
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zeta
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myofibroblasts
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willebrand
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epithelial-mesenchymal
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factor-beta
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fak
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fibrin
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metalloproteinases
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preterm
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dish
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biomaterials
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procollagens
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heparan
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alpha-smooth
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dermal
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tgf-beta
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plasminogen
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fibrillar
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drug development
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heparin-binding
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synthesis
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thrombospondin
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medicine
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industry
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diagnostics
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pharmacology
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biotechnology
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analysis
- 5.3.4.1
- collagen
- laminin
- integrins
- endothelial
- actin
- fibrosis
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adhesive
-
basement
- mesenchymal
- vessel
- fiber
- metastasis
- proteoglycans
- vitronectin
- fibrinogen
- matrices
- nephropathy
- albumin
- gelatin
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interstitial
-
mesangial
- platelet
- monolayer
- cytoskeleton
- glomerular
- rgd
- vimentin
- e-cadherin
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cell-cell
- adhesions
- zeta
- myofibroblasts
- willebrand
-
epithelial-mesenchymal
- factor-beta
- fak
- fibrin
- metalloproteinases
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preterm
-
dish
-
biomaterials
- procollagens
- heparan
-
alpha-smooth
- dermal
- tgf-beta
- plasminogen
-
fibrillar
- drug development
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heparin-binding
- synthesis
- thrombospondin
- medicine
- industry
- diagnostics
- pharmacology
- biotechnology
- analysis
Reaction
catalyses the rearrangement of -S-S- bonds in proteins =
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
5.3.4.1 protein disulfide-isomeraseAdvanced search results
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results (Natural Substrates Products
Natural Substrates Products on EC 5.3.4.1 - protein disulfide-isomerase
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NATURAL SUBSTRATE 
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
apolipoprotein B100
?
-
the enzyme assists in the oxidative folding of apolipoprotein B100
-
-
?
E2A homodimer
E2A-basic helix-loop-helix protein heterodimer
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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
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?
estrogen receptor alpha
?
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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
-
-
?
integrin subunit alpha11
?
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the enzyme activates integrin subunit alpha11
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-
?
neuronal nitric oxide synthase
?
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the enzyme catalyzes neuronal nitric oxide synthase dimerization
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-
?
reduced denatured RNase A + GSH
reduced renatured RNase A + GSSG
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-
-
-
?
reduced ribonuclease A
denatured ribonuclease A
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-
-
?
alkaline protease inhibitor
?
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folding and rearrangement of alkaline protease inhibitor
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-
?
alkaline protease inhibitor
?
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folding and rearrangement of alkaline protease inhibitor
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-
?
Insulin-(SS) + GSH
Insulin-(SH)2 + GSSG
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protein disulfide isomerase supports proinsulin folding as chaperone and isomerase
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-
?
Proteins
?
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facilitates the formation of the correct disulfide bonds within newly synthesized polypeptides
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-
?
Proteins
?
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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
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-
?
Proteins
?
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enzyme may play a physiological role in the catalysis of S-S-bond formation in prolactin
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-
?
Proteins
?
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may play a role in the formation of disulfide bonds in extracellular and periplasmic proteins
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-
?
Proteins
?
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facilitates the formation of disulfides during the folding and processing of membrane and secretory proteins
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-
?
Proteins
?
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enzyme may be involved in the formation of intra-chain and inter-chain disulfide bonds in procollagen
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-
?
Proteins
?
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may play a role in retaining prolyl 4-hydroxylase in its native conformation
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?
Proteins
?
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enzyme may be involved in the formation of intra-chain and inter-chain disulfide bonds in procollagen
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-
?
Proteins
?
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platelet enzyme may play a role in the various haemostatic and tissue remodelling processes in which platelets are involved
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?
Proteins
?
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may play a role in the formation of disulfide bonds in extracellular and periplasmic proteins
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?
Proteins
?
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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
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-
?
Proteins
?
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may play a role in the formation of disulfide bonds in extracellular and periplasmic proteins
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-
?
Proteins
?
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enzyme may be involved in the formation of intra-chain and inter-chain disulfide bonds in procollagen
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-
?
Proteins
?
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may play a role in the formation of disulfide bonds in extracellular and periplasmic proteins
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?
Proteins
?
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may play a role in the formation of disulfide bonds in extracellular and periplasmic proteins
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-
?
Proteins
?
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may play a role in the formation of disulfide bonds in extracellular and periplasmic proteins
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?
Proteins
?
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may play a role in the formation of disulfide bonds in extracellular and periplasmic proteins
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?
Proteins
?
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proposed physiological role as catalyst of formation of native disulfide bonds in nascent and newly synthesized secretory proteins
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?
Proteins
?
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involved in the assembly of wheat storage proteins within the endoplasmic reticulum
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?
Proteins
?
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plays a role in the formation of disulfide bonds during biosynthesis of wheat storage proteins
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-
?
tissue factor
?
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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
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-
?
additional information
?
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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
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?
additional information
?
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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
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?
additional information
?
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structure and mechanism of PDI in disulfide formation and oxidative protein folding, overview
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?
additional information
?
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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
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?
additional information
?
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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
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?
additional information
?
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the enzyme may be significant in the action of triiodothyronine towards the target cells
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-
?
additional information
?
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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
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?
additional information
?
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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
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?
additional information
?
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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
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?
additional information
?
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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
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-
?
additional information
?
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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
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?
additional information
?
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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
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?
additional information
?
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structure and mechanism of PDI in disulfide formation and oxidative protein folding, overview
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?
additional information
?
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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
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?
additional information
?
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in vivo, disulfide bond formation is mainly catalyzed by protein disulfide isomerase
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?
additional information
?
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in vivo, disulfide bond formation is mainly catalyzed by protein disulfide isomerase
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?
additional information
?
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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
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?
additional information
?
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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
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-
?
additional information
?
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DsbC resolves incorrect disulfides whose formation has been catalyzed by redox-active copper
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-
?
additional information
?
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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
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-
?
additional information
?
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the enzyme plays a crucial role in folding periplasmatically excreted proteins
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-
?
additional information
?
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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
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?
additional information
?
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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
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-
?
additional information
?
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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
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?
additional information
?
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the enzyme acts as a thyroid-hormone binding protein
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?
additional information
?
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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
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?
additional information
?
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enzyme is involved in the proper folding or quality control of storage proteins
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?
additional information
?
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GmPDIL-1 and GmPDIL-2 function as molecular chaperones, and prevent the aggregation of unfolded rhodanese, while GmPDIL-3a and GmPDIL-3b do not
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?
additional information
?
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HlPDI-1 might be involved in tick blood feeding and Babesia parasite infection in ticks
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?
additional information
?
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HlPDI-1 might be involved in tick blood feeding and Babesia parasite infection in ticks
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?
additional information
?
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HlPDI-1 might be involved in tick blood feeding and Babesia parasite infection in ticks
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?
additional information
?
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HlPDI-1 might be involved in tick blood feeding and Babesia parasite infection in ticks
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?
additional information
?
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HlPDI-3 might be involved in tick blood feeding and Babesia parasite infection in ticks
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?
additional information
?
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HlPDI-3 might be involved in tick blood feeding and Babesia parasite infection in ticks
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?
additional information
?
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HlPDI-3 might be involved in tick blood feeding and Babesia parasite infection in ticks
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?
additional information
?
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HlPDI-3 might be involved in tick blood feeding and Babesia parasite infection in ticks
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?
additional information
?
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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
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?
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
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?
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
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-
?
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
-
-
?
additional information
?
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-
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
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?
additional information
?
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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
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?
additional information
?
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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
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?
additional information
?
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structure and mechanism of PDI in disulfide formation and oxidative protein folding, overview
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?
additional information
?
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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
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?
additional information
?
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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
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?
additional information
?
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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
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?
additional information
?
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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
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?
additional information
?
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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
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?
additional information
?
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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
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?
additional information
?
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protein disulfide isomerase contributes to the activation of cryptic initiator protein tissue factoron microvesicles in vitro
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?
additional information
?
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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
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?
additional information
?
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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
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?
additional information
?
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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
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?
additional information
?
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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
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?
additional information
?
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PDI catalyzes disulfide bond formation in the endoplasmic reticulum
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?
additional information
?
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PDI catalyzes disulfide bond formation in the endoplasmic reticulum
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?
additional information
?
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PDI specifically associates with signal peptide peptidase, SPP, independently of human cytomegalovirus glycoprotein US2, but not with Derlin-1
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?
additional information
?
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PDI specifically binds 3,3',5-triiodo-L-thyronine
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?
additional information
?
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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
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?
additional information
?
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the enzyme has three catalytic activities including thiol-disulfide oxireductase, disulfide isomerase, and redox-dependent chaperone
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?
additional information
?
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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
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additional information
?
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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
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additional information
?
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the enzyme has a single E2-binding site
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?
additional information
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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
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?
additional information
?
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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
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?
additional information
?
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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
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?
additional information
?
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PDILT forms intermolecular disulfide bonds in testis
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?
additional information
?
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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
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?
additional information
?
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PDI is required in vivo for both fibrin generation and platelet thrombus formation
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?
additional information
?
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protein disulfide isomerase directly promotes initiator protein tissue factor-dependent fibrin production during thrombus formation in vivo
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?
additional information
?
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AGR2 is essential for production of intestinal mucin MUC2, but is not required for establishment of intestinal secretory epithelial cell lineages
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?
additional information
?
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PDI specifically binds 3,3',5-triiodo-L-thyronine
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?
additional information
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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
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additional information
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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
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additional information
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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
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additional information
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the enzyme assists protein folding in malaria parasites
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additional information
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the enzyme assists protein folding in malaria parasites
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additional information
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the enzyme assists protein folding in malaria parasites
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additional information
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the enzyme assists protein folding in malaria parasites
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additional information
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the enzyme assists protein folding in malaria parasites
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additional information
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the enzyme assists protein folding in malaria parasites
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additional information
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the enzyme assists protein folding in malaria parasites
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additional information
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the enzyme assists protein folding in malaria parasites
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additional information
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the enzyme assists protein folding in malaria parasites
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additional information
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the enzyme assists protein folding in malaria parasites
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additional information
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the enzyme assists protein folding in malaria parasites
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additional information
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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
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additional information
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PDI has dehydroascorbate reductase activity, PDI may play a role in the intraluminal dehydroascorbate reduction
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additional information
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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
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additional information
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cell-surface PDI is required for transnitrosation of metallothionein by S-nitroso-albumin in intact pulmonary vascular endothelial cells, overview
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additional information
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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
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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
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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
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additional information
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PDI specifically binds 3,3',5-triiodo-L-thyronine
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additional information
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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
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additional information
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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
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additional information
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the enzyme has an essential role that is distinct from its function in formation of native disulphides
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essential enzyme for yeast cell growth, both oxidase and isomerase activities are required
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PDI plays a key role in catalyzing the folding of secretory proteins
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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
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additional information
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the enzyme is an essential catalyst of disulfide formation with two cysteines in the active site facilitating thiol-disulfide exchange
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additional information
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the organism is completely dependent on PDI activity for growth
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structure and mechanism of PDI in disulfide formation and oxidative protein folding, overview
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structure and mechanism of PDI in disulfide formation and oxidative protein folding, overview
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additional information
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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
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additional information
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the organism is completely dependent on PDI activity for growth
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additional information
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PDI is involved in the cellular growth and response to nutritional and oxidative stress, regulation, overview
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additional information
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PDI is involved in the cellular growth and response to nutritional and oxidative stress, regulation, overview
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additional information
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PDI is involved in the cellular growth and response to nutritional and oxidative stress, regulation, overview
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additional information
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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
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additional information
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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
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additional information
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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
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additional information
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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
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additional information
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the single domain PDI-1 and the class 1 PDI-2 are not essential for the organism
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additional information
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the single domain PDI-1 and the class 1 PDI-2 are not essential for the organism
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