Biology:Snapalysin
From HandWiki
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
- ↑ "Characterization of a small metalloprotease from Streptomyces caespitosus with high specificity to aromatic residues". J. Ferment. Bioeng. 83: 590–592. 1997. doi:10.1016/s0922-338x(97)81142-7.
- ↑ "Snapalysin". Handbook of Proteolytic Enzymes. London: Handbook of Proteolytic Enzymes. 1998. pp. 1134–1135.
- ↑ "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. November 2000. doi:10.1016/s0162-0134(00)00136-7. PMID 11132632.
External links
- Snapalysin at the US National Library of Medicine Medical Subject Headings (MeSH)
Original source: https://en.wikipedia.org/wiki/Snapalysin.
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