5.3.4.1: protein disulfide-isomerase
This is an abbreviated version!
For detailed information about protein disulfide-isomerase, go to the full flat file.
Reaction
catalyses the rearrangement of -S-S- bonds in proteins
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Synonyms
5'-MD, 58 kDa glucose regulated protein, 58 kDa microsomal protein, AGR2, anterior gradient homolog 2, BPA-binding protein, CaBP1, CaBP2, Cellular thyroid hormone binding protein, cotyledon-specific chloroplast biogenesis factor CYO1, CYO1, DbsG, disulfide bond isomerase, disulfide bond-forming enzyme, Disulfide interchange enzyme, disulfide isomerase, Disulfide isomerase ER-60, disulfide-bond isomerase, dithiol-disulfide isomerase, Dsb, DsbA, DsbB, DsbC, DsbD, DsbG, ECaSt/PDI, endoplasmic reticulum protein EUG1, Eps1p, ER protein 57, ER58, ER60, ERcalcistorin/protein-disulfide isomerase, ERdj5, Ero1, Erp, ERP-57, ERp-72 homolog, ERp18, ERp27, ERp28, ERp44, Erp46, ERp5, ERp57, ERP59, ERP60, ERp72, Eug1p, fibronectin, gPDI-1, gPDI-2, gPDI-3, HIP-70, HlPDI-1, HlPDI-2, HlPDI-3, Iodothyronine 5'-monodeiodinase, More, Mpd1p, Mpd2p, multifunctional protein disulfide isomerase, ncgl2478, P5, P55, P58, pancreas-specific protein disulfide isomerase, PDI, PDI A4, PDI I, PDI II, pdi-15, PDI-1a, pdi-40, pdi-47, pdi-52, PDI-A, PDI-M, PDI-P5, PDI-related protein, PDI1, PDI11, PDI2, PDI7, PDI8, PDIA1, PDIA2, PDIA3, PDIA4, PDIA6, PDIL-1, PDIL-2, PDIL1-1, PDIL1;1, PDIL1Aalpha, PDIL1B, PDIL2, PDIL2-3, PDIL3A, PDIL4D, PDIL5A, PDILT, PDIp, PDIr, protein disulfide isomerase, protein disulfide isomerase 1, protein disulfide isomerase 2, protein disulfide isomerase 3, protein disulfide isomerase A1, protein disulfide isomerase A3, protein disulfide isomerase A5, protein disulfide isomerase A6, protein disulfide isomerase associated 3, Protein disulfide isomerase P5, protein disulfide isomerase-1, protein disulfide isomerase-11, protein disulfide isomerase-2, protein disulfide isomerase-3, protein disulfide isomerase-8, protein disulfide isomerase-like protein of the testis, protein disulfide isomerase-P5, protein disulfide isomerase-related chaperone Wind, Protein disulfide isomerase-related protein, protein disulfide oxidoreductase, protein disulfide reductase/isomerase, protein disulfide-isomerase A4, Protein disulphide isomerase, Protein ERp-72, protein-disulfide isomerase, R-cognin, RB60, Rearrangease, Reduced ribonuclease reactivating enzyme, Retina cognin, S-S rearrangase, SSO0192, SsPDO, thiol-disulfide oxidoreductase, thiol-protein oxidoreductase, thioredoxin domain-containing protein 5, Thyroid hormone-binding protein, Thyroxine deiodinase, TXNDC5, yPDI
ECTree
Reaction
Reaction on EC 5.3.4.1 - protein disulfide-isomerase
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catalyses the rearrangement of -S-S- bonds in proteins
catalyses the rearrangement of -S-S- bonds in proteins
mechanism
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catalyses the rearrangement of -S-S- bonds in proteins
mechanism
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catalyses the rearrangement of -S-S- bonds in proteins
mechanism
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catalyses the rearrangement of -S-S- bonds in proteins
mechanism
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catalyses the rearrangement of -S-S- bonds in proteins
reaction mechanism
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catalyses the rearrangement of -S-S- bonds in proteins
active site structure
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catalyses the rearrangement of -S-S- bonds in proteins
substrate binding and catalytic mechanism
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catalyses the rearrangement of -S-S- bonds in proteins
substrate binding and catalytic mechanism
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catalyses the rearrangement of -S-S- bonds in proteins
substrate binding and catalytic mechanism
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catalyses the rearrangement of -S-S- bonds in proteins
substrate binding and catalytic mechanism
catalyses the rearrangement of -S-S- bonds in proteins
substrate binding and catalytic mechanism
catalyses the rearrangement of -S-S- bonds in proteins
active site location, structure, and redox state
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catalyses the rearrangement of -S-S- bonds in proteins
disulfide formation and isomerization mechanism by domains a and a', during transfer of oxidizing or reducing equivalents to substrates, the CXXC active site cycles between its oxidized, disulfide and reduced, thiol states
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catalyses the rearrangement of -S-S- bonds in proteins
disulfide formation and isomerization mechanism by domains a and a', during transfer of oxidizing or reducing equivalents to substrates, the CXXC active site cycles between its oxidized, disulfide and reduced, thiol states
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catalyses the rearrangement of -S-S- bonds in proteins
disulfide formation and isomerization mechanism by domains a and a', during transfer of oxidizing or reducing equivalents to substrates, the CXXC active site cycles between its oxidized, disulfide and reduced, thiol states
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catalyses the rearrangement of -S-S- bonds in proteins
disulfide formation and isomerization mechanism by domains a and a', during transfer of oxidizing or reducing equivalents to substrates, the CXXC active site cycles between its oxidized, disulfide and reduced, thiol states
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catalyses the rearrangement of -S-S- bonds in proteins
PDI introduces disulfides into proteins, oxidase activity, and provides quality control by catalyzing the rearrangement of incorrect disulfides, isomerase activity
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catalyses the rearrangement of -S-S- bonds in proteins
protein with nonconsecutive disulfie bonds require activity of DsbC for their full activity, the disulfide bonds are formed during the translocation across the cytoplasmic membrane
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catalyses the rearrangement of -S-S- bonds in proteins
structure of oxidized and reduced active site, the active site motif is -C-X-X-C-
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catalyses the rearrangement of -S-S- bonds in proteins
the catalytic domain, residues 88-231, shows a thioredoxin fold with a helical insert, and an active site motif -C-X-X-C-, active site structure
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catalyses the rearrangement of -S-S- bonds in proteins
mechanism of enzyme-assisted folding of plant cyclotides
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catalyses the rearrangement of -S-S- bonds in proteins
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
catalyses the rearrangement of -S-S- bonds in proteins
NCgl2478 reduces S-mycothiolated mixed disulfides and intramolecular disulfides via a monothiol-disulfide and a dithiol-disulfide exchange mechanism, respectively. NCgl2478 reduces mycothiolated mixed disulfides preferably via a monothiol mechanism. NCgl2478 reduces intramolecular disulfide bonds via a dithiol mechanism. NCgl2478 lacks oxidase activity
catalyses the rearrangement of -S-S- bonds in proteins
NCgl2478 reduces S-mycothiolated mixed disulfides and intramolecular disulfides via a monothiol-disulfide and a dithiol-disulfide exchange mechanism, respectively. NCgl2478 reduces mycothiolated mixed disulfides preferably via a monothiol mechanism. NCgl2478 reduces intramolecular disulfide bonds via a dithiol mechanism. NCgl2478 lacks oxidase activity
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catalyses the rearrangement of -S-S- bonds in proteins
NCgl2478 reduces S-mycothiolated mixed disulfides and intramolecular disulfides via a monothiol-disulfide and a dithiol-disulfide exchange mechanism, respectively. NCgl2478 reduces mycothiolated mixed disulfides preferably via a monothiol mechanism. NCgl2478 reduces intramolecular disulfide bonds via a dithiol mechanism. NCgl2478 lacks oxidase activity
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catalyses the rearrangement of -S-S- bonds in proteins
NCgl2478 reduces S-mycothiolated mixed disulfides and intramolecular disulfides via a monothiol-disulfide and a dithiol-disulfide exchange mechanism, respectively. NCgl2478 reduces mycothiolated mixed disulfides preferably via a monothiol mechanism. NCgl2478 reduces intramolecular disulfide bonds via a dithiol mechanism. NCgl2478 lacks oxidase activity
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catalyses the rearrangement of -S-S- bonds in proteins
NCgl2478 reduces S-mycothiolated mixed disulfides and intramolecular disulfides via a monothiol-disulfide and a dithiol-disulfide exchange mechanism, respectively. NCgl2478 reduces mycothiolated mixed disulfides preferably via a monothiol mechanism. NCgl2478 reduces intramolecular disulfide bonds via a dithiol mechanism. NCgl2478 lacks oxidase activity
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catalyses the rearrangement of -S-S- bonds in proteins
NCgl2478 reduces S-mycothiolated mixed disulfides and intramolecular disulfides via a monothiol-disulfide and a dithiol-disulfide exchange mechanism, respectively. NCgl2478 reduces mycothiolated mixed disulfides preferably via a monothiol mechanism. NCgl2478 reduces intramolecular disulfide bonds via a dithiol mechanism. NCgl2478 lacks oxidase activity
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catalyses the rearrangement of -S-S- bonds in proteins
NCgl2478 reduces S-mycothiolated mixed disulfides and intramolecular disulfides via a monothiol-disulfide and a dithiol-disulfide exchange mechanism, respectively. NCgl2478 reduces mycothiolated mixed disulfides preferably via a monothiol mechanism. NCgl2478 reduces intramolecular disulfide bonds via a dithiol mechanism. NCgl2478 lacks oxidase activity
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catalyses the rearrangement of -S-S- bonds in proteins
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