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 P32951
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)

P32951
CARP1_CANPA
Candida parapsilosis
Candidapepsin-1

PDB Structure

PDB 3FV3
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
The crystal structure of the secreted aspartic protease 1 from Candida parapsilosis in complex with pepstatin A
Dostal, J., Brynda, J., Hruskova-Heidingsfeldova, O., Sieglova, I., Pichova, I., Rezacova, P.
J.Struct.Biol.