Candidapepsin
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 js present in yeast Candida albicans.
References
- ↑ Remold, H., Fasold, H. and Staib, F. (1968). "Purification and characterization of a proteolytic enzyme from Candida albicans". Biochim. Biophys. Acta 167: 399–406. doi:10.1016/0005-2744(68)90219-2. PMID 5729955.
- ↑ Rüchel, R. (1981). "Properties of a purified proteinase from the yeast Candida albicans". Biochim. Biophys. Acta 659: 99–113. doi:10.1016/0005-2744(81)90274-6. PMID 7018586.
- ↑ Negi, M., Tsuboi, R., Matsui, T. and Ogawa, H. (1984). "Isolation and characterization of proteinase from Candida albicans: substrate specificity". J. Invest. Dermatol. 83: 32–36. doi:10.1111/1523-1747.ep12261656. PMID 6203988.
- ↑ Lott, T.J., Page, L.S., Boiron, P., Benson, J. and Reiss, E. (1989). "Nucleotide sequence of the Candida albicans aspartyl proteinase gene". Nucleic Acids Res. 17: 1779–1779. doi:10.1093/nar/17.4.1779. PMID 2646602.
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