Snapalysin
Snapalysin (EC 3.4.24.77, small neutral protease, SnpA gene product (Streptomyces lividans)) is an enzyme.[1][2][3] This enzyme catalyses the following chemical reaction
- Hydrolyses proteins with a preference for Tyr or Phe in the P1' position. Has no action on amino-acid p-nitroanilides
| Snapalysin | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.4.24.77 | ||||||||
| CAS no. | 945859-47-2 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
This enzyme belongs to the peptidase family M7.
References
- Kurisu G, Sugimoto A, Harada S, Takagi M, Imanaka T, Kai Y (1997). "Characterization of a small metalloprotease from Streptomyces caespitosus with high specificity to aromatic residues". J. Ferment. Bioeng. 83: 590–592. doi:10.1016/s0922-338x(97)81142-7.
- Butler MJ, Rawlings ND, Woessner JF (1998). "Snapalysin". In Barrett AJ (ed.). Handbook of Proteolytic Enzymes. London: Handbook of Proteolytic Enzymes. pp. 1134–1135.
- Kurisu G, Kai Y, Harada S (November 2000). "Structure of the zinc-binding site in the crystal structure of a zinc endoprotease from Streptomyces caespitosus at 1 A resolution". Journal of Inorganic Biochemistry. 82 (1–4): 225–8. doi:10.1016/s0162-0134(00)00136-7. PMID 11132632.
External links
- Snapalysin at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
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