The Enzyme Database

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Accepted name: candidapepsin
Reaction: Preferential cleavage at the carboxyl of hydrophobic amino acids, but fails to cleave Leu15-Tyr, Tyr16-Leu and Phe24-Phe of insulin B chain. Activates trypsinogen, and degrades keratin
Other name(s): Candida albicans aspartic proteinase; Candida albicans carboxyl proteinase; Candida albicans secretory acid proteinase; Candida olea acid proteinase; Candida aspartic proteinase; Candida olea aspartic proteinase
Comments: This endopeptidase from the imperfect yeast Candida albicans is inhibited by pepstatin, but not by methyl 2-diazoacetamidohexanoate or 1,2-epoxy-3-(p-nitrophenoxy)propane. In peptidase family A1 (pepsin A family). Formerly included in EC
Links to other databases: BRENDA, EXPASY, Gene, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 69458-91-9
1.  Remold, H., Fasold, H. and Staib, F. Purification and characterization of a proteolytic enzyme from Candida albicans. Biochim. Biophys. Acta 167 (1968) 399–406. [DOI] [PMID: 5729955]
2.  Rüchel, R. Properties of a purified proteinase from the yeast Candida albicans. Biochim. Biophys. Acta 659 (1981) 99–113. [DOI] [PMID: 7018586]
3.  Negi, M., Tsuboi, R., Matsui, T. and Ogawa, H. Isolation and characterization of proteinase from Candida albicans: substrate specificity. J. Invest. Dermatol. 83 (1984) 32–36. [DOI] [PMID: 6203988]
4.  Lott, T.J., Page, L.S., Boiron, P., Benson, J. and Reiss, E. Nucleotide sequence of the Candida albicans aspartyl proteinase gene. Nucleic Acids Res. 17 (1989) 1779. [DOI] [PMID: 2646602]
[EC created 1992 (EC created 1992 (EC created 1961 as EC, transferred 1972 to EC, modified 1981 [EC, EC, EC, EC, EC, EC and EC all created 1972 and incorporated 1978], part incorporated 1992)]

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