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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

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 Isomerases
         5.3 Intramolecular oxidoreductases
             5.3.4 Transposing S-S bonds
                5.3.4.1 protein disulfide-isomerase

Crystallization

Crystallization on EC 5.3.4.1 - protein disulfide-isomerase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure of reduced and oxidized enzyme
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purified native and selenomethionine-labeled DsbG in oxidized and in redox-mixed state, DsbG is oxidized by 1.7 mM (1,10-phenanthroline)Cu(II), crystallization in 20% PEG 4000, 0.1 M sodium citrate, pH 3.8-4.2, and 0.2 M ammonium sulfate, X-ray diffraction structure determination and analysis at 1.7-2.0 A resolution
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purified recombinant His6-tagged DsbC and DsbG dimerization domains, sitting drop vapour-diffusion method, 4-6 mg/ml protein in 25 mM HEPES, pH 7.5, 150 mM NaCl, 0.001 ml of protein and of reservoir solution, containing 2.0 M Li2SO4, 0.1 M MgSO4 and 5% 2-propanol, pH 4.5, are mixed, for crystallization of DsbG also addition of 0.2 M CdCl2 and 33% MPD, X-ray diffraction structure determination and analysis at 2.0 and 1.9 A, respectively
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purified recombinant reduced DsbC, hanging drop vapour diffusion method, the reservoir solution contains 0.2 M Li2SO4, o.1 M Tris, pH8.4, and 20% PEG 4000, 0.0015 ml of protein and of reservoir solution are mixed, X-ray diffraction reduced structure determination and analysis at 2.5 A resolution
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ERp57 and its isolated bb' and b' domains in complex with the lectin chaperone calnexin, hanging drop vapour diffusion method, equilibration of 14 mg/ml protein in 50 mM Tris-HCl, 0.15 M NaCl, 1 mM DTT, pH 7.5, against 30% w/v PEG 3350, 0.1 M (NH4)2SO4, 0.1 M HEPES buffer, pH 7.5, for 1-3 days at 20°C, X-ray diffraction structure determination and analysis at 2.0 A resoution
hanging drop vapor diffusion method, using 0.01 M zinc chloride, 20% (w/v) polyethylene glycol 6000, and 0.1 M Tris-HCl (pH 8.0)
hanging drop vapor diffusion method, using 0.2 M ammonium sulfate, 0.1 M bis-Tris pH 5.5, 25% (w/v) PEG 3350
hanging-drop vapour-diffusion, mixing of 0.003 ml protein solution i.e. 15 mg/ml protein, 25 mM HEPES, pH 7.5 with 0.003 mL reservoir solution containing 20-23% polyethylene glycol 5000, 200 mM ammonium acetate, 100 mM HEPES, pH 7.5 and 5% glycerol
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molecular modeling offers a role for the conserved residue R103 in coordinating the oxidative transition-state complex
small angle X-ray scattering analysis of purified recombinant wild-type and deletion mutant PDIs, structure modeling, the enzyme forms an approximately flat elliptical cylinder
in complex with alpha-synuclein, using 0.1 M HEPES buffer (pH 7.5) containing 25% (w/v) PEG3350
sitting drop vapor diffusion method, using 30% (w/v) PEG 8000, 0.1 M MES buffer, pH 6.0, 80 mM calcium acetate
purified recombinant b and b' domains and the bb' fragments of ERp57 and ERp72, hanging drop vapor diffusion method, 0.002 ml protein solution containing 10 mg/ml protein in 50 mM Tris-HCl, pH 7.5, 0.15 M NaCl, and 1 mM DTT, are mixed with 0.002 ml reservoir solution containing 18% w/v PEG MME 2000, 25% glycerol, and 0.1 M Tris, pH 8.0, suspended over 1 ml reservoir solution, 1-3 days, 20°C, X-ray diffraction structure determination and analysis at 1.9 A resolution, overview
hanging drop vapor diffusion method, using 24% (w/v) PEG 4000, 100 mM sodium acetate, pH 6.4, 25 mM sodium citrate, pH 6.4, and 17% (v/v) glycerol
purified recombinant residues 23-522 of PDI1, X-ray diffraction structure determination and analysis at 2.4 A resolution, modeling
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to 3.7 A resolution. PDI is a highly flexible molecule with its catalytic domains, a and a', representing two mobile arms connected to a more rigid core composed of the b and b' domains. The linker between the a domain and the core is more susceptible to degradation than that connecting the a' domain to the core. Molecular flexibility is essential for the enzymatic activity in vitro and in vivo
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