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Literature summary extracted from

  • Ben Khalaf, N.; De Muylder, G.; Louzir, H.; McKerrow, J.; Chenik, M.
    Leishmania major protein disulfide isomerase as a drug target: enzymatic and functional characterization (2012), Parasitol. Res., 110, 1911-1917.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
5.3.4.1 bacitracin full inhibition of reductase activity at 0.2 mM Leishmania major
5.3.4.1 additional information ribostamycin has very slight inhibitory effect on protein disulfide isomerase chaperone activity and no effect on both reductase and isomerase activities Leishmania major

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
5.3.4.1 Insulin-(SS) + GSH Leishmania major
-
Insulin-(SH)2 + GSSG
-
?
5.3.4.1 Insulin-(SS) + GSH Leishmania major MHOM/TN/94/GLC94
-
Insulin-(SH)2 + GSSG
-
?

Organism

EC Number Organism UniProt Comment Textmining
5.3.4.1 Leishmania major
-
-
-
5.3.4.1 Leishmania major MHOM/TN/94/GLC94
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5.3.4.1 Insulin-(SS) + GSH
-
Leishmania major Insulin-(SH)2 + GSSG
-
?
5.3.4.1 Insulin-(SS) + GSH
-
Leishmania major MHOM/TN/94/GLC94 Insulin-(SH)2 + GSSG
-
?

Synonyms

EC Number Synonyms Comment Organism
5.3.4.1 PDI
-
Leishmania major
5.3.4.1 protein disulfide isomerase
-
Leishmania major

IC50 Value

EC Number IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
5.3.4.1 0.0811
-
pH and temperature not specified in the publication Leishmania major bacitracin

General Information

EC Number General Information Comment Organism
5.3.4.1 physiological function the enzyme plays a key role in assisting Leishmania protein folding via its capacity to catalyze formation, breakage, and rearrangement of disulfide bonds in nascent polypeptides. The enzyme displays a chaperone-like activity Leishmania major