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

BRENDA support

Literature summary for 5.3.4.1 extracted from

  • Winter, J.; Klappa, P.; Freedman, R.B.; Lilie, H.; Rudolph, R.
    Catalytic activity and chaperone function of human protein-disulfide isomerase are required for the efficient refolding of proinsulin (2002), J. Biol. Chem., 277, 310-317.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
genistein suppresses binding of proinsulin to PDI, inhibits 66% of PDIs chaperone activity Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant PDI Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
unfolded proinsulin PDI acts both as a chaperone and as an isomerase during folding and disulfid bond formation of proinsulin, chaperone and isomerization activity is required at the beginning of proinsulin folding, the late refolding process only depends on the isomerase activity Homo sapiens refolded proinsulin
-
?

Synonyms

Synonyms Comment Organism
PDI
-
Homo sapiens