Neurolysin
| Neurolysin | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.4.24.16 | ||||||||
| CAS no. | 149371-24-4 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Neurolysin (EC 3.4.24.16, neurotensin endopeptidase, endopeptidase 24.16, endo-oligopeptidase B (proline-endopeptidase)) is an enzyme.[1][2][3] This enzyme catalyses the following chemical reaction
- Preferential cleavage in neurotensin: Pro10-Tyr
This enzyme belongs to the peptidase family M3.
References
- ^ Checler F, Vincent JP, Kitabgi P (August 1986). "Purification and characterization of a novel neurotensin-degrading peptidase from rat brain synaptic membranes". The Journal of Biological Chemistry. 261 (24): 11274–81. PMID 3525564.
- ^ Barelli H, Vincent JP, Checler F (August 1988). "Peripheral inactivation of neurotensin. Isolation and characterization of a metallopeptidase from rat ileum". European Journal of Biochemistry. 175 (3): 481–9. doi:10.1111/j.1432-1033.1988.tb14220.x. PMID 3409880.
- ^ Checler F, Barelli H, Vincent JP (January 1989). "Tissue distribution of a novel neurotensin-degrading metallopeptidase. An immunological approach using monospecific polyclonal antibodies". The Biochemical Journal. 257 (2): 549–54. PMC 1135613. PMID 2649078.
External links
- Neurolysin at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
