yapsin 1;
yeast aspartic protease 3;
Yap3 gene product (Saccharomyces cerevisiae)

Hydrolases;
Acting on peptide bonds (peptidases);
Aspartic endopeptidases

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

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]

1  [PMID:8626758]

Cawley NX, Chen HC, Beinfeld MC, Loh YP.

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) 4168-76.

Saccharomyces cerevisiae [GN:sce]

2

Fuller, R.S.

Yapsin 2.

In: Barrett, A.J., Rawlings, N.D. and Woessner, J.F. (Eds.), Handbook of Proteolytic Enzymes, Academic Press, London, 1998, p. 908-909.

3  [PMID:9485427]

Olsen V, Guruprasad K, Cawley NX, Chen HC, Blundell TL, Loh YP.

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) 2768-77.

Saccharomyces cerevisiae [GN:sce]