The Enzyme Database

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EC 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, 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. [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]
 
 


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