Candidapepsin

Candidapepsin
Identifiers
EC number 3.4.23.24
CAS number 69458-91-9
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum

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

  1. ↑ Remold H, Fasold H, Staib F (October 1968). "Purification and characterization of a proteolytic enzyme from Candida albicans". Biochimica et Biophysica Acta. 167 (2): 399–406. doi:10.1016/0005-2744(68)90219-2. PMID 5729955.
  2. ↑ Rüchel R (May 1981). "Properties of a purified proteinase from the yeast Candida albicans". Biochimica et Biophysica Acta. 659 (1): 99–113. doi:10.1016/0005-2744(81)90274-6. PMID 7018586.
  3. ↑ 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.
  4. ↑ Lott TJ, Page LS, Boiron P, Benson J, Reiss E (February 1989). "Nucleotide sequence of the Candida albicans aspartyl proteinase gene". Nucleic Acids Research. 17 (4): 1779. doi:10.1093/nar/17.4.1779. PMC 331855. PMID 2646602.
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