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
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
Search
PMCarticles
PubMedarticles
NCBIproteins

This enzyme belongs to the peptidase family M7.

References

  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.
This article is issued from Wikipedia. The text is licensed under Creative Commons - Attribution - Sharealike. Additional terms may apply for the media files.