The Enzyme Database

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EC 3.4.23.25     
Accepted name: saccharopepsin
Reaction: Hydrolysis of proteins with broad specificity for peptide bonds. Cleaves -Leu-Leu┼Val-Tyr bond in a synthetic substrate. Does not act on esters of Tyr or Arg
Other name(s): yeast endopeptidase A; Saccharomyces aspartic proteinase; aspartic proteinase yscA; proteinase A; proteinase yscA; yeast proteinase A; Saccharomyces cerevisiae aspartic proteinase A; yeast proteinase A; PRA
Comments: Located in the vacuole of the baker's yeast (Saccharomyces cerevisiae) cell. In peptidase family A1 (pepsin A family).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 37228-80-1
References:
1.  Hata, T., Hayashi, R. and Dot, E. Purification of yeast proteinases. Part III. Isolation and physicochemical properties of yeast proteinase A and C. Agric. Biol. Chem. 31 (1967) 357–367.
2.  Meussdoerffer, F., Tortora, P. and Holzer, H. Purification and properties of proteinase A from yeast. J. Biol. Chem. 255 (1980) 12087–12093. [PMID: 7002931]
3.  Ammerer, G., Hunter, C.P., Rothman, J.H., Saari, G.C., Valls, L.A. and Stevens, T.H. PEP4 gene of Saccharomyces cerevisiae encodes proteinase A, a vacuolar enzyme required for processing of vacuolar precursors. Mol. Cell. Biol. 6 (1987) 2490–2499. [PMID: 3023936]
[EC 3.4.23.25 created 1992 (EC 3.4.23.6 created 1992 (EC 3.4.23.6 created 1961 as EC 3.4.4.17, transferred 1972 to EC 3.4.23.6, modified 1981 [EC 3.4.23.7, EC 3.4.23.8, EC 3.4.23.9, EC 3.4.23.10, EC 3.4.99.1, EC 3.4.99.15 and EC 3.4.99.25 all created 1972 and incorporated 1978], part incorporated 1992)]
 
 


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