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 P0CS83
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)

P0CS83
CARP2_CANAX
Candida albicans
Candidapepsin-2

PDB Structure

PDB 1EAG
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
The crystal structure of a major secreted aspartic proteinase from Candida albicans in complexes with two inhibitors.
Cutfield, S.M., Dodson, E.J., Anderson, B.F., Moody, P.C.E., Marshall, C.J., Sullivan, P.A., Cutfield, J.F.
Structure