ENTRY       EC 3.4.23.24
NAME        Candidapepsin
            Candida albicans aspartic proteinase
CLASS       Hydrolases
            Acting on peptide bonds (peptidases)
            Aspartic endopeptidases
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
SUBSTRATE   Protein
            Peptide
            Trypsinogen
            Keratin
            H2O
PRODUCT     Protein
            Peptide
            Trypsin
INHIBITOR   Pepstatin
COMMENT     This endopeptidase from the imperfect yeast Candida albicans is
            inhibited by pepstatin, but not by methyl 2-diazoacetamido-
            hexanoate or 1,2-epoxy-3-(p-nitrophenoxy)propane.  Formerly
            included in EC 3.4.23.6.
MOTIF       PS: PS00141  [LIVMFGAC]-[LIVMTADN]-[LIVFSA]-D-[ST]-G-[STAV]-
                         [STAPDENQ]-x-[LIVMFSTNC]-x-[LIVMFGTA]
STRUCTURES  PDB: 1EAG  1ZAP  
DBLINKS     University of Geneva ENZYME DATA BANK: 3.4.23.24
            WIT (What Is There) Metabolic Reconstruction: 3.4.23.24
///