CATH Classification

Domain Context

CATH Clusters

Superfamily Acid Proteases
Functional Family Aspartic protease

Enzyme Information

3.4.23.24
Candidapepsin.
based on mapping to UniProt P0CY27
Preferential cleavage at the carboxyl of hydrophobic amino acids, but fails to cleave 15-Leu-|-Tyr-16, 16-Tyr-|-Leu-17 and 24-Phe-|-Phe-25 of insulin B chain. Activates trypsinogen, and degrades keratin.
-!- 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. -!- Belongs to peptidase family A1. -!- Formerly EC 3.4.4.17 and EC 3.4.23.6.

UniProtKB Entries (1)

P0CY27
CARP1_CANAL
Candida albicans SC5314
Candidapepsin-1

PDB Structure

PDB 2QZW
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
X-ray structures of Sap1 and Sap5: Structural comparison of the secreted aspartic proteinases from Candida albicans.
Borelli, C., Ruge, E., Lee, J.H., Schaller, M., Vogelsang, A., Monod, M., Korting, H.C., Huber, R., Maskos, K.
Proteins