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Literature summary extracted from

  • Wilkinson, B.; Xiao, R.; Gilbert, H.F.
    A structural disulfide of yeast protein-disulfide isomerase destabilizes the active site disulfide of the N-terminal thioredoxin domain (2005), J. Biol. Chem., 280, 11483-11487.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
5.3.4.1 GSH required for activity Saccharomyces cerevisiae
5.3.4.1 GSSG required for activity Saccharomyces cerevisiae

Cloned(Commentary)

EC Number Cloned (Comment) Organism
5.3.4.1 expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) Saccharomyces cerevisiae

Protein Variants

EC Number Protein Variants Comment Organism
5.3.4.1 C90A site-directed mutagenesis, mutation of a non-active site cysteine residue, reduced oxidase and isomerase activities compared to the wild-type enzyme Saccharomyces cerevisiae
5.3.4.1 C90A/C97A site-directed mutagenesis, mutation of both non-active site cysteine residues, 60% and 80% reduced oxidase and isomerase activities, respectively, compared to the wild-type enzyme Saccharomyces cerevisiae
5.3.4.1 C97A site-directed mutagenesis, mutation of a non-active site cysteine residue, reduced oxidase and isomerase activities compared to the wild-type enzyme Saccharomyces cerevisiae

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
5.3.4.1 additional information
-
 additional information redox equilibrium measurements of wild-type and mutant C90A/C97A enzymes, determination of oxidase and isomerase activities Saccharomyces cerevisiae

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
5.3.4.1 endoplasmic reticulum
-
 Saccharomyces cerevisiae 5783
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
5.3.4.1 additional information Saccharomyces cerevisiae the enzyme is an essential catalyst of disulfide formation with two cysteines in the active site facilitating thiol-disulfide exchange ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
5.3.4.1 Saccharomyces cerevisiae
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
5.3.4.1 recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography Saccharomyces cerevisiae

Reaction

EC Number Reaction Comment Organism Reaction ID
5.3.4.1 catalyses the rearrangement of -S-S- bonds in proteins active site structure Saccharomyces cerevisiae
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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 ?
-
 ?
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 ?
-
 ?
5.3.4.1 ribonuclease refolding of ribonuclease, isomerase activity, renaturation of reduced ribonuclease, in presence of GSH and GSSG Saccharomyces cerevisiae ?
-
 ?

Subunits

EC Number Subunits Comment Organism
5.3.4.1 More non-active site cysteines form a disulfide bridge that is stable even under very reducing environment destabilizing the N-terminal active site disulfide which becomes a 18fold better oxidant by this way Saccharomyces cerevisiae

Synonyms

EC Number Synonyms Comment Organism
5.3.4.1 PDI
-
 Saccharomyces cerevisiae

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
5.3.4.1 25
-
 assay at Saccharomyces cerevisiae

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
5.3.4.1 8
-
 assay at Saccharomyces cerevisiae