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Literature summary for 5.3.4.1 extracted from

  • Sun, X.X.; Dai, Y.; Liu, H.P.; Chen, S.M.; Wang, C.C.
    Contributions of protein disulfide isomerase domains to its chaperone activity (2000), Biochim. Biophys. Acta, 1481, 45-54.
    View publication on PubMed

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
denatured D-glyceraldehyde-3-phosphate dehydrogenase chaperone activity of PDI Homo sapiens refolded D-glyceraldehyde-3-phosphate dehydrogenase
-
?
unfolded RNase A all five consecutive PDI domains, a-b-b'-a'-c are necessary for PDI's disulfide isomerase and chaperone activity Homo sapiens refolded RNase A
-
?

Synonyms

Synonyms Comment Organism
PDI
-
Homo sapiens