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
This enzyme belongs to the peptidase family M7.
References
- ↑ Kurisu, G., Sugimoto, A., Harada, S., Takagi, M., Imanaka, T. and 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. (1998). "Snapalysin". In Barrett, A.J., Rawlings, N.D. and Woessner, J.F. Handbook of Proteolytic Enzymes. London: Handbook of Proteolytic Enzymes. pp. 1134–1135.
- ↑ Kurisu, G., Kai, Y. and 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.
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