ExplorEnz: EC 3.4.23.24

Your query returned 1 entry. Printable version

3.4.23.24

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 3.4.23.6

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 69458-91-9

References:

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 3.4.23.24 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)]