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Catalytic Site Atlas

CSA LITERATURE entry for 1eag

E.C. namecandidapepsin
SpeciesCandida albicans (Yeast)
E.C. Number (IntEnz) 3.4.23.24
CSA Homologues of 1eagThere are 267 Homologs
CSA Entries With UniProtID P28871
CSA Entries With EC Number 3.4.23.24
PDBe Entry 1eag
PDBSum Entry 1eag
MACiE Entry 1eag

Literature Report

IntroductionAspartic Protease from C. albicans (SAP) acts as a virulence factor within fungal pathogen associated infections. Evidence suggests SAP can degrade proteins associated with immunological and structural defence roles, such and IgG heavy chains, keratin, acidified collagen and extracellular matrix proteins. Its inhibition plays a key role in fighting fungal deceases.
MechansimTwo Asp residues act as a general acid/base catalysis site, acting to polarise a water into a nucleophilic state to attack a protonated carbonyl on the substrate. The wide range of pH over which the catalysis occurs is determined by hydrogen bonding interactions between the catalytic resides and close proximity pKa modifying Ser and Thr residues.
Reaction

Catalytic Sites for 1eag

Literature References

Notes:
Andreeva NS
Analysis of crystal structures of aspartic proteinases: on the role of amino acid residues adjacent to the catalytic site of pepsin-like enzymes.
Protein Sci 2001 10 2439-2450
PubMed: 11714911
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