The Enzyme Database

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Accepted name: snapalysin
Reaction: Hydrolyses proteins with a preference for Tyr or Phe in the P1′ position. Has no action on amino-acid p-nitroanilides
Other name(s): small neutral protease; SnpA gene product (Streptomyces lividans)
Comments: Type example of peptidase family M7.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 945859-47-2
1.  Kurisu, G., Sugimoto, A., Harada, S., Takagi, M., Imanaka, T. and Kai, Y. Characterization of a small metalloprotease from Streptomyces caespitosus with high specificity to aromatic residues. J. Ferment. Bioeng. 83 (1997) 590–592.
2.  Butler, M.J. Snapalysin. In: Barrett, A.J., Rawlings, N.D. and Woessner, J.F. (Ed.), Handbook of Proteolytic Enzymes, Handbook of Proteolytic Enzymes, London, 1998, pp. 1134–1135.
3.  Kurisu, G., Kai, Y. and Harada, S. 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 (2000) 225–228. [DOI] [PMID: 11132632]
[EC created 2001]

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