Leucolysin (EC 3.4.24.6, Leucostoma neutral proteinase, Leucostoma peptidase A) is an enzyme.[1][2] This enzyme catalyses the following chemical reaction
| Leucolysin | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.4.24.6 | ||||||||
| CAS no. | 72561-03-6 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
- Cleavage of Phe1-Val, His5-Leu, Ala14-Leu, Gly20-Glu, Gly23-Phe and Phe24-Phe bonds in insulin B chain as well as N-blocked dipeptides
This enzyme is isolated from the venom of the western cottonmouth moccasin snake (Agkistrodon piscivorus leucostoma).
References edit
- ^ Wagner FW, Spiekerman AM, Prescott JM (September 1968). "Leucostoma peptidase A. Isolation and physical properties". The Journal of Biological Chemistry. 243 (17): 4486–93. PMID 5684005.
- ^ Spiekerman AM, Fredericks KK, Wagner FW, Prescott JM (February 1973). "Leucostoma peptidase A: a metalloprotease from snake venom". Biochimica et Biophysica Acta (BBA) - Enzymology. 293 (2): 464–75. doi:10.1016/0005-2744(73)90353-7. PMID 4711816.
External links edit
- Leucolysin at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
