EC 126.96.36.199 - Leishmanolysin
IntEnz Enzyme Nomenclature
promastigote surface endopeptidase
promastigote surface protease
surface acid proteinase
- Preference for hydrophobic residues at P1 and P1' and basic residues at P2' and P3'. A model nonapeptide is cleaved at -Ala-TyrLeu-Lys-Lys-.
A membrane-bound glycoprotein found on the promastigote of various species of Leishmania protozoans. Contains consensus sequence for a zinc-binding site; Z-Tyr-Leu-NHOH is a strong inhibitor. The enzyme can activate its proenzyme by cleavage of the Val100┼Val bond. An acid pH optimum is found with certain protein substrates. Type example of peptidase family M8.
Links to other databases
Molecular cloning of the major surface antigen of Leishmania.J. Exp. Med. 167 : 724-729 (1988). [PMID: 3346625]
Characterization of the promastigote surface protease of Leishmania as a membrane-bound zinc endopeptidase.Mol. Biochem. Parasitol. 37 : 235-246 (1989). [PMID: 2608099]
Surface acid proteinase (gp63) of Leishmania mexicana. A metalloenzyme capable of protecting liposome-encapsulated proteins from phagolysosomal degradation by macrophages.J. Biol. Chem. 264 : 7483-7489 (1989).
Peptide substrate specificity of the membrane-bound metalloprotease of Leishmania.Biochemistry 29 : 10113-10119 (1990). [PMID: 2271643]
[EC 188.8.131.52 created 1992]