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
Other names: yeast aspartic protease 3; Yap3 gene product (Saccharomyces cerevisiae)
Comments: In peptidase family A1 of pepsin, and weakly inhibited by pepstatin. Can partially substitute for kexin in a deficient strain of yeast. The homologous product of the Mkc7 gene (Saccharomyces cerevisiae) has similar catalytic activity and has been termed yapsin 2 [2]
Links to other databases: BRENDA, EXPASY, KEGG, MEROPS, Metacyc, PDB, CAS registry number: 205132-58-7
References
1. Cawley, N.X., Chen, H.C., Beinfeld, M.C. and Loh, Y.P. Specificity and kinetic studies on the cleavage of various prohormone mono- and paired-basic residue sites by yeast aspartic protease 3. J. Biol. Chem. 271 (1996) 4168-4176. [PMID: 8626758]
2. Fuller, R.S. Yapsin 2. In: Handbook of Proteolytic Enzymes, (Barrett, A.J., Rawlings, N.D. and Woessner, J.F. eds), pp. 908-909 (1998) Academic Press, London
3. Olsen, V., Guruprasad, K., Cawley, N.X., Chen, H.C., Blundell, T.L. and Loh, Y.P. 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 (1998) 2768-2777. [PMID: 9485427]