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Catalytic Site Atlas

CSA LITERATURE entry for 1eed

E.C. nameendothiapepsin
SpeciesCryphonectria parasitica (CpMYRV-1)
E.C. Number (IntEnz) 3.4.23.22
CSA Homologues of 1eedThere are 272 Homologs
CSA Entries With UniProtID P11838
CSA Entries With EC Number 3.4.23.22
PDBe Entry 1eed
PDBSum Entry 1eed
MACiE Entry 1eed

Literature Report

IntroductionEndothiapepsin is a member of the aspartic protease family which catalyse the hydrolysis of peptide substrates. Investigation into the inhibition of endothiapepsin has been aimed at forming an inhibitor for renin, another aspartic protease responsible for the formation of the potentially vasoactive peptide angiotensin II.
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.
Trp 39 has been implicated in the proton relay mechanism involving Ser 35 and a water molcule, but mutagenesis W39A does not prevent catalytic activity.
Reaction

Catalytic Sites for 1eed

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
Cooper J
X-ray crystallographic analysis of inhibition of endothiapepsin by cyclohexyl renin inhibitors.
Biochemistry 1992 31 8142-8150
PubMed: 1525155
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