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Catalytic Site Atlas

CSA LITERATURE entry for 1apt

E.C. namepenicillopepsin
SpeciesPenicillium janthinellum (Penicillium vitale)
E.C. Number (IntEnz) 3.4.23.20
CSA Homologues of 1aptThere are 261 Homologs
CSA Entries With UniProtID P00798
CSA Entries With EC Number 3.4.23.20
PDBe Entry 1apt
PDBSum Entry 1apt
MACiE Entry 1apt

Literature Report

IntroductionPepsins belong to the aspartic endopeptidase family. The catalytic site of pepsin-like enzymes is formed at the junction of the two domains of the protein and contains two catalytic aspartic acid residues, one in each domain.
MechansimThe mechanism proceeds via a general acid/base mechanism, and involves nucleophilic attack by an activated water molecule on the substrate.
Reaction

Catalytic Sites for 1apt

Literature References

Notes:
James MN
Crystallographic analysis of transition state mimics bound to penicillopepsin: difluorostatine- and difluorostatone-containing peptides.
Biochemistry 1992 31 3872-3886
PubMed: 1567842
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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