ExplorEnz: EC 3.4.23.41

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3.4.23.41

Accepted name:

yapsin 1

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 name(s):

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, MetaCyc, MEROPS, 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. [DOI] [PMID: 8626758]
2.	Fuller, R.S. Yapsin 2. In: Barrett, A.J., Rawlings, N.D. and Woessner, J.F. (Ed.), Handbook of Proteolytic Enzymes, Academic Press, London, 1998, pp. 908–909.
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. [DOI] [PMID: 9485427]

[EC 3.4.23.41 created 2000]