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

BRENDA support

Literature summary for 5.3.4.1 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
Search for more literature for 5.3.4.1

Inhibitors

Inhibitors Comment Organism Structure
bacitracin full inhibition of reductase activity at 0.2 mM Leishmania major
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)

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

Organism

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

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
PDI
-
 Leishmania major
protein disulfide isomerase
-
 Leishmania major

IC50 Value

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

General Information

General Information Comment Organism
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