Snapalysin
Snapalysin | |||||||||
---|---|---|---|---|---|---|---|---|---|
Identifiers | |||||||||
EC number | 3.4.24.77 | ||||||||
CAS number | 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 | ||||||||
|
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
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, M.J.; Rawlings, N.D.; Woessner, J.F. (1998). "Snapalysin". In Barrett, A.J. Handbook of Proteolytic Enzymes. London: Handbook of Proteolytic Enzymes. pp. 1134–1135.
- ↑ Kurisu, G.; Kai, Y.; Harada, S. (2000). "Structure of the zinc-binding site in the crystal structure of a zinc endoprotease from Streptomyces caespitosus at 1 Å resolution". J. Inorg. Biochem. 82: 225–228. doi:10.1016/s0162-0134(00)00136-7. PMID 11132632.
External links
- Snapalysin at the US National Library of Medicine Medical Subject Headings (MeSH)
This article is issued from Wikipedia - version of the 5/23/2016. The text is available under the Creative Commons Attribution/Share Alike but additional terms may apply for the media files.