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3.4.23.24: Candidapepsin

This is an abbreviated version!
For detailed information about Candidapepsin, go to the full flat file.

Word Map on EC 3.4.23.24

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 =

Synonyms

Aspartate protease, aspartic protease, aspartic protease 2, aspartic protease Sap2p, aspartic proteinase 3, aspartyl protease, aspartyl protease Sap2p, aspartyl protease Sap4, aspartyl protease Sap5, aspartyl protease Sap6, aspartyl proteinase, candialbicin, Candida albicans aspartic proteinase, Candida albicans carboxyl proteinase, Candida albicans secretory acid proteinase, Candida albicans-secreted aspartic proteinase, Candida olea acid proteinase, Candidapepsin-1, candidapepsin-2, EC 3.4.23.6, EC 3.4.4.17, Proteinase, Candida albicans aspartic, Proteinase, Candida aspartic, Proteinase, Candida olea aspartic, S-aspartyl proteinase, SAP, SAP1, Sap10, SAP11, Sap1p, SAP2, Sap2p, SAP2X, SAP3, Sap3p, SAP4, Sap4p, SAP5, Sap5p, SAP6, Sap6p, Sap7, Sap7p, Sap8, Sap8p, Sap9, Sap9p, SAPP1, Sapp1p, SAPP2, Sapp2p, SAPP3, SAPT1, Sapt1p, SAPT2, SAPT3, SAPT4, secreted aspartic protease, secreted aspartic protease 1, secreted aspartic protease 2, secreted aspartic proteinase, secreted aspartic proteinase 1, secreted aspartic proteinase 2, secreted aspartic proteinase-2, secreted aspartyl peptidase, secreted aspartyl protease, secreted aspartyl protease 9, secreted aspartyl proteinase, secreted aspartyl proteinase 2, secreted aspartyl proteinase 5, secreted aspartyl proteinase2, secreted aspartyl proteinases, secreted aspartyl-type peptidase, secretory aspartyl proteinase, secretory aspartyl proteinase SAP1, secretory aspartyl proteinase SAP2p, secretory aspartyl proteinase SAP3p, secretory aspartyl proteinase SAP4p, secretory aspartyl proteinase SAP5p, secretory aspartyl proteinase SAP6p, yapsin, Yps

ECTree

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.23 Aspartic endopeptidases
                3.4.23.24 Candidapepsin

Crystallization

Crystallization on EC 3.4.23.24 - Candidapepsin

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
complexed with inhibitor A-70450
of inhibited enzyme
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Sap2p-inhibitor complex solved to 2.1 A
Sap3 with PepA in the presence of 10 mM zinc acetate, Sap3 without PepA in the presence of 0.2M potassium bromide, 15% PEG4000 and 0.1 M cacodylic acid/NaOH, pH 6.5. The Sap3 protein crystallizes in the trigonal space group P3(2)21 containing one molecule per asymmetric unit.
X-ray crystal structures of Sap1 and Sap5
in complex with pepstatin A, hanging drop vapor diffusion method, using 0.1 M MES pH 6.5, 30% (w/v) PEG 400
Sapp1p in complex with pepstatin A, hanging drop vapor diffusion method, using 0.1 M Tris-HCl, pH 7.0, 2.0 M ammonium sulfate and 10% (v/v) glycerol, at 19°C
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