Candidapepsin
Definition:
EC Tree > 3 Hydrolases > 3.4 Acting on peptide bonds (peptidases) > 3.4.23 Aspartic endopeptidases > 3.4.23.24 Candidapepsin
Candidapepsin is an aspartic endopeptidase from the imperfect yeast Candida albicans, inhibited by pepstatin but not by methyl 2-diazoacetamidohexanoate or 1,2-epoxy-3-(p-nitrophenoxy)propane. It belongs to peptidase family A1 and was formerly in EC 3.4.23.6. It preferentially cleaves after hydrophobic amino acids but fails to cleave Leu15-Tyr, Tyr16-Leu and Phe24-Phe of the insulin B chain; it activates trypsinogen and degrades keratin. In the pathogen it contributes to mucosal invasion and tissue damage. It features a pepsin-like aspartic-protease fold.
Candidapepsin is an aspartic endopeptidase from the imperfect yeast Candida albicans, inhibited by pepstatin but not by methyl 2-diazoacetamidohexanoate or 1,2-epoxy-3-(p-nitrophenoxy)propane. It belongs to peptidase family A1 and was formerly in EC 3.4.23.6. It preferentially cleaves after hydrophobic amino acids but fails to cleave Leu15-Tyr, Tyr16-Leu and Phe24-Phe of the insulin B chain; it activates trypsinogen and degrades keratin. In the pathogen it contributes to mucosal invasion and tissue damage. It features a pepsin-like aspartic-protease fold.
References:
Biomedical Dictionary
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