Candidapepsin (EC 3.4.23.24, Candida albicans aspartic proteinase, Candida albicans carboxyl proteinase, Candida albicans secretory acid proteinase, Candida olea acid proteinase, Candida aspartic proteinase, Candida olea aspartic proteinase) is an enzyme.[1][2][3][4] This enzyme catalyses the following chemical 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
This endopeptidase is present in yeast Candida albicans.
^Remold H, Fasold H, Staib F (October 1968). "Purification and characterization of a proteolytic enzyme from Candida albicans". Biochimica et Biophysica Acta (BBA) - Enzymology. 167 (2): 399–406. doi:10.1016/0005-2744(68)90219-2. PMID 5729955.
^Rüchel R (May 1981). "Properties of a purified proteinase from the yeast Candida albicans". Biochimica et Biophysica Acta (BBA) - Enzymology. 659 (1): 99–113. doi:10.1016/0005-2744(81)90274-6. PMID 7018586.
^Negi M, Tsuboi R, Matsui T, Ogawa H (July 1984). "Isolation and characterization of proteinase from Candida albicans: substrate specificity". The Journal of Investigative Dermatology. 83 (1): 32–6. doi:10.1111/1523-1747.ep12261656. PMID 6203988.