Leishmanolysin Explained

Leishmanolysin
Ec Number:3.4.24.36
Cas Number:161052-06-8

Leishmanolysin (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.

Notes and References

  1. Button LL, McMaster WR . Molecular cloning of the major surface antigen of leishmania . The Journal of Experimental Medicine . 167 . 2 . 724–9 . February 1988 . 3346625 . 2188825 . 10.1084/jem.167.2.724 .
  2. Bouvier J, Bordier C, Vogel H, Reichelt R, Etges R . Characterization of the promastigote surface protease of Leishmania as a membrane-bound zinc endopeptidase . Molecular and Biochemical Parasitology . 37 . 2 . 235–45 . December 1989 . 2608099 . 10.1016/0166-6851(89)90155-2 .
  3. Chaudhuri G, Chaudhuri M, Pan A, Chang KP . 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 . 2708373 .
  4. Bouvier J, Schneider P, Etges R, Bordier C . Peptide substrate specificity of the membrane-bound metalloprotease of Leishmania . Biochemistry . 29 . 43 . 10113–9 . October 1990 . 2271643 . 10.1021/bi00495a015 .

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