Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 5.3.4.1 extracted from

  • Tsai, B.; Rodighiero, C.; Lencer, W.I.; Rapoport, T.A.
    Protein disulfide isomerase acts as a redox-dependent chaperone to unfold cholera toxin (2001), Cell, 104, 937-948.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression of GST-PDI fusion protein in Escherichia coli Saccharomyces cerevisiae

Localization

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

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Purification (Commentary)

Purification (Comment) Organism
GST-PDI fusion protein Saccharomyces cerevisiae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
folded cholera toxin PDI binds in the reduced state to the A chain of cholera toxin, in the oxidized state it releases it, PDI may be involved in the retrograde protein transport into the cytosol Saccharomyces cerevisiae unfolded cholera toxin
-
?

Synonyms

Synonyms Comment Organism
PDI
-
Saccharomyces cerevisiae