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Literature summary for 5.3.4.1 extracted from

  • Wang, Y.; Narayan, M.
    pH Dependence of the isomerase activity of protein disulfide isomerase: insights into its functional relevance (2008), Protein J., 27, 181-185.
    View publication on PubMed
Search for more literature for 5.3.4.1

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Rattus norvegicus

Localization

Localization Comment Organism GeneOntology No. Textmining
endoplasmic reticulum PDI possesses an anomalously low thiol pKa and is fine-tuned to catalyze oxidative folding in the lumen of the endoplasmic reticulum where the ambient pH of about 7 would otherwise retard thioldisulfide exchange reactions and hinder acquisition of the native fold Rattus norvegicus 5783
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Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Rattus norvegicus PDI possesses an anomalously low thiol pKa and is fine-tuned to catalyze oxidative folding in the lumen of the endoplasmic reticulum where the ambient pH of about 7 would otherwise retard thioldisulfide exchange reactions and hinder acquisition of the native fold ?
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 ?

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information PDI possesses an anomalously low thiol pKa and is fine-tuned to catalyze oxidative folding in the lumen of the endoplasmic reticulum where the ambient pH of about 7 would otherwise retard thioldisulfide exchange reactions and hinder acquisition of the native fold Rattus norvegicus ?
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 ?

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
additional information
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 PDI has a greater relative impact on isomerization reactions and consequently the structure-forming step in oxidative folding at pH 7, as opposed to pH’s 8 and 9 Rattus norvegicus