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Literature summary for 5.3.4.1 extracted from

  • Wang, C.; Chen, S.; Wang, X.; Wang, L.; Wallis, A.K.; Freedman, R.B.; Wang, C.C.
    Plasticity of human protein disulfide isomerase: evidence for mobility around the X-linker region and its functional significance (2010), J. Biol. Chem., 285, 26788-26797.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 5.3.4.1

Cloned(Commentary)

Cloned (Comment) Organism
-
 Homo sapiens

Protein Variants

Protein Variants Comment Organism
I272A the mutant shows similar proteinase K sensitivity like the wild type protein. The mutant shows significantly lower potency than wild type PDI in suppressing aggregation of denatured rhodanese Homo sapiens
L343A the mutant is more sensitive to proteinase K than wild type enzyme. The mutant shows the same chaperone activity as that of wild type PDI Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
endoplasmic reticulum
-
 Homo sapiens 5783
-

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
denatured rhodanese PDI exhibits chaperone activity with rhodanese Homo sapiens ?
-
 ?
insulin PDI exhibits reductase activity with insulin Homo sapiens ?
-
 ?
RNase A PDI exhibits isomerase activity with RNase A Homo sapiens ?
-
 ?

Synonyms

Synonyms Comment Organism
PDI
-
 Homo sapiens
protein disulfide isomerase
-
 Homo sapiens