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Literature summary extracted from

  • Xiao, R.; Wilkinson, B.; Solovyov, A.; Winther, J.R.; Holmgren, A.; Lundstrom-Ljung, J.; Gilbert, H.F.
    The contributions of protein disulfide isomerase and its homologues to oxidative protein folding in the yeast endoplasmic reticulum (2004), J. Biol. Chem., 279, 49780-49786.
    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 PDI and mutant PDI defective in the a' domain, which bears the isomerase activity, in Escherichia coli Saccharomyces cerevisiae

Protein Variants

EC Number Protein Variants Comment Organism
5.3.4.1 additional information construction of a mutant PDI defective in the a' domain, which bears the isomerase activity, a PDI deletion yeast mutant cannot be rescued by the rat PDI 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 carboxypeptidase Y Saccharomyces cerevisiae maturation of carboxypeptidase Y ?
-
 ?
5.3.4.1 additional information Saccharomyces cerevisiae essential enzyme for yeast cell growth, both oxidase and isomerase activities are required ?
-
 ?

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 PDI and mutant PDI defective in the a' domain from Escherichia coli by nickel affnity chromatography Saccharomyces cerevisiae

Reaction

EC Number Reaction Comment Organism Reaction ID
5.3.4.1 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 Saccharomyces cerevisiae
a

Source Tissue

EC Number Source Tissue Comment Organism Textmining

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5.3.4.1 carboxypeptidase Y maturation of carboxypeptidase Y Saccharomyces cerevisiae ?
-
 ?
5.3.4.1 additional information essential enzyme for yeast cell growth, both oxidase and isomerase activities are required Saccharomyces cerevisiae ?
-
 ?
5.3.4.1 refolding of RNase renaturation of reduced RNase Saccharomyces cerevisiae ?
-
 ?

Subunits

EC Number Subunits Comment Organism
5.3.4.1 More the catalytic domains a and a' are responsible for the oxidase and the isomerase activity, respectively Saccharomyces cerevisiae

Synonyms

EC Number Synonyms Comment Organism
5.3.4.1 PDI
-
 Saccharomyces cerevisiae
5.3.4.1 protein disulfide isomerase
-
 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