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-
Leishmanolysin
Identifiers
EC number3.4.24.36
CAS number161052-06-8
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum

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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