Leishmanolysin

Leishmanolysin
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

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, 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.
  2. 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.
  3. 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.
  4. 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.

External links

This article is issued from Wikipedia - version of the Thursday, March 31, 2016. The text is available under the Creative Commons Attribution/Share Alike but additional terms may apply for the media files.