Leishmanolysin (EC 3.4.24.36, promastigote surface endopeptidase, glycoprotein gp63, Leishmania metalloproteinase, surface acid proteinase, promastigote surface protease) is an enzyme.[1][2][3][4] This enzyme catalyses the following chemical 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-

This membrane-bound glycoprotein is present in the promastigote of various species of Leishmania protozoans.

References

  1. ^ Button LL, McMaster WR (February 1988). "Molecular cloning of the major surface antigen of leishmania". The Journal of Experimental Medicine. 167 (2): 724–9. doi:10.1084/jem.167.2.724. PMC 2188825. PMID 3346625.
  2. ^ Bouvier J, Bordier C, Vogel H, Reichelt R, Etges R (December 1989). "Characterization of the promastigote surface protease of Leishmania as a membrane-bound zinc endopeptidase". Molecular and Biochemical Parasitology. 37 (2): 235–45. doi:10.1016/0166-6851(89)90155-2. PMID 2608099.
  3. ^ Chaudhuri G, Chaudhuri M, Pan A, Chang KP (May 1989). "Surface acid proteinase (gp63) of Leishmania mexicana. A metalloenzyme capable of protecting liposome-encapsulated proteins from phagolysosomal degradation by macrophages". The Journal of Biological Chemistry. 264 (13): 7483–9. PMID 2708373.
  4. ^ Bouvier J, Schneider P, Etges R, Bordier C (October 1990). "Peptide substrate specificity of the membrane-bound metalloprotease of Leishmania". Biochemistry. 29 (43): 10113–9. doi:10.1021/bi00495a015. PMID 2271643.

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