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Literature summary for 5.3.4.1 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

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

Cloned(Commentary)

Cloned (Comment) Organism
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

Protein Variants Comment Organism
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

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

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
carboxypeptidase Y Saccharomyces cerevisiae maturation of carboxypeptidase Y ?
-
?
additional information Saccharomyces cerevisiae essential enzyme for yeast cell growth, both oxidase and isomerase activities are required ?
-
?

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged wild-type PDI and mutant PDI defective in the a' domain from Escherichia coli by nickel affnity chromatography Saccharomyces cerevisiae

Reaction

Reaction Comment Organism Reaction ID
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

Source Tissue

Source Tissue Comment Organism Textmining

Substrates and Products (Substrate)

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

Subunits

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

Synonyms

Synonyms Comment Organism
PDI
-
Saccharomyces cerevisiae
protein disulfide isomerase
-
Saccharomyces cerevisiae

Temperature Optimum [°C]

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

pH Optimum

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