ExplorEnz: EC 3.4.24.36

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3.4.24.36

Accepted name:

leishmanolysin

Reaction:

Preference for hydrophobic residues at P1 and P1′ and basic residues at P2′ and P3′. A model nonapeptide is cleaved at -Ala-Tyr┼Leu-Lys-Lys-

Other name(s):

promastigote surface endopeptidase; glycoprotein gp63; Leishmania metalloproteinase; surface acid proteinase; promastigote surface protease

Comments:

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:

BRENDA, EXPASY, Gene, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 161052-06-8

References:

1.	Button, L.L. and McMaster, W.R. Molecular cloning of the major surface antigen of Leishmania. J. Exp. Med. 167 (1988) 724–729. [PMID: 3346625]
2.	Bouvier, J., Cordier, C., Vogel, H., Reichelt, R. and Etges, R. Characterization of the promastigote surface protease of Leishmania as a membrane-bound zinc endopeptidase. Mol. Biochem. Parasitol. 37 (1989) 235–246. [DOI] [PMID: 2608099]
3.	Chaudhuri, G., Chaudhuri, M., Pan, A. and Chang, K.-P. Surface acid proteinase (gp63) of Leishmania mexicana. A metalloenzyme capable of protecting liposome-encapsulated proteins from phagolysosomal degradation by macrophages. J. Biol. Chem. 264 (1989) 7483–7489. [PMID: 2708373]
4.	Bouvier, J., Schneider, P., Etges, R. and Bordier, C. Peptide substrate specificity of the membrane-bound metalloprotease of Leishmania. Biochemistry 29 (1990) 10113–10119. [PMID: 2271643]

[EC 3.4.24.36 created 1992]