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

Snapalysin
Identifiers
EC no.3.4.24.77
CAS no.945859-47-2
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
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PMCarticles
PubMedarticles
NCBIproteins
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

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  1. ^ 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.
  2. ^ Butler MJ, Rawlings ND, Woessner JF (1998). "Snapalysin". In Barrett AJ (ed.). Handbook of Proteolytic Enzymes. London: Handbook of Proteolytic Enzymes. pp. 1134–1135.
  3. ^ 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.
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