| 词条 | Leishmanolysin |
| 释义 |
| Name = Leishmanolysin | EC_number = 3.4.24.36 | CAS_number = 161052-06-8 | IUBMB_EC_number = 3/4/24/36 | GO_code = | image = | width = | caption = }}Leishmanolysin ({{EC number|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. References1. ^{{cite journal | vauthors = Button LL, McMaster WR | title = Molecular cloning of the major surface antigen of leishmania | journal = The Journal of Experimental Medicine | volume = 167 | issue = 2 | pages = 724–9 | date = February 1988 | pmid = 3346625 | pmc = 2188825 | doi = 10.1084/jem.167.2.724 }} 2. ^{{cite journal | vauthors = Bouvier J, Bordier C, Vogel H, Reichelt R, Etges R | title = Characterization of the promastigote surface protease of Leishmania as a membrane-bound zinc endopeptidase | journal = Molecular and Biochemical Parasitology | volume = 37 | issue = 2 | pages = 235–45 | date = December 1989 | pmid = 2608099 | doi = 10.1016/0166-6851(89)90155-2 }} 3. ^{{cite journal | vauthors = Chaudhuri G, Chaudhuri M, Pan A, Chang KP | title = Surface acid proteinase (gp63) of Leishmania mexicana. A metalloenzyme capable of protecting liposome-encapsulated proteins from phagolysosomal degradation by macrophages | journal = The Journal of Biological Chemistry | volume = 264 | issue = 13 | pages = 7483–9 | date = May 1989 | pmid = 2708373 }} 4. ^{{cite journal | vauthors = Bouvier J, Schneider P, Etges R, Bordier C | title = Peptide substrate specificity of the membrane-bound metalloprotease of Leishmania | journal = Biochemistry | volume = 29 | issue = 43 | pages = 10113–9 | date = October 1990 | pmid = 2271643 | doi = 10.1021/bi00495a015 }} External links
1 : EC 3.4.24 |
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