Biology:Leishmanolysin
From HandWiki
| Leishmanolysin | |||||||||
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| Identifiers | |||||||||
| EC number | 3.4.24.36 | ||||||||
| CAS number | 161052-06-8 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
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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
- ↑ "Molecular cloning of the major surface antigen of leishmania". The Journal of Experimental Medicine 167 (2): 724–9. February 1988. doi:10.1084/jem.167.2.724. PMID 3346625.
- ↑ "Characterization of the promastigote surface protease of Leishmania as a membrane-bound zinc endopeptidase". Molecular and Biochemical Parasitology 37 (2): 235–45. December 1989. doi:10.1016/0166-6851(89)90155-2. PMID 2608099.
- ↑ "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. May 1989. PMID 2708373.
- ↑ "Peptide substrate specificity of the membrane-bound metalloprotease of Leishmania". Biochemistry 29 (43): 10113–9. October 1990. doi:10.1021/bi00495a015. PMID 2271643.
External links
- Leishmanolysin at the US National Library of Medicine Medical Subject Headings (MeSH)
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