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Yapsin 1 (EC 3.4.23.41, yeast aspartic protease 3, Yap3 gene product (Saccharomyces cerevisiae)) is an enzyme.[1][2][3] This enzyme catalyses the following chemical reaction
- Hydrolyses various precursor proteins with Arg or Lys in P1, and commonly Arg or Lys also in P2. The P3 amino acid is usually non-polar, but otherwise additional basic amino acids are favourable in both non-prime and prime positions
This enzyme belongs to the peptidase family A1 of pepsin.
References
- ^ Cawley NX, Chen HC, Beinfeld MC, Loh YP (February 1996). "Specificity and kinetic studies on the cleavage of various prohormone mono- and paired-basic residue sites by yeast aspartic protease 3". The Journal of Biological Chemistry. 271 (8): 4168–76. doi:10.1074/jbc.271.8.4168. PMID 8626758.
- ^ Fuller RS, Rawlings ND, Woessner JF (1998). "Yapsin 2". In Barrett AJ (ed.). Handbook of Proteolytic Enzymes. London: Academic Press. pp. 908–909.
- ^ Olsen V, Guruprasad K, Cawley NX, Chen HC, Blundell TL, Loh YP (March 1998). "Cleavage efficiency of the novel aspartic protease yapsin 1 (Yap3p) enhanced for substrates with arginine residues flanking the P1 site: correlation with electronegative active-site pockets predicted by molecular modeling". Biochemistry. 37 (9): 2768–77. doi:10.1021/bi9724826. PMID 9485427.
External links
- Yapsin+1 at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
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