Leishmanolysin
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
- ↑ Button, L.L. and McMaster, W.R. (1988). "Molecular cloning of the major surface antigen of Leishmania". J. Exp. Med. 167: 724–729. doi:10.1084/jem.167.2.724. PMID 3346625.
- ↑ Bouvier, J., Cordier, C., Vogel, H., Reichelt, R. and Etges, R. (1989). "Characterization of the promastigote surface protease of Leishmania as a membrane-bound zinc endopeptidase". Mol. Biochem. Parasitol. 37: 235–246. doi:10.1016/0166-6851(89)90155-2. PMID 2608099.
- ↑ Chaudhuri, G., Chaudhuri, M., Pan, A. and Chang, K.-P. (1989). "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. PMID 2708373.
- ↑ Bouvier, J., Schneider, P., Etges, R. and Bordier, C. (1990). "Peptide substrate specificity of the membrane-bound metalloprotease of Leishmania". Biochemistry 29: 10113–10119. doi:10.1021/bi00495a015. PMID 2271643.
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