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Catalytic Site Atlas

CSA LITERATURE entry for 1am5

E.C. namepepsin A
SpeciesGadus morhua (Atlantic cod)
E.C. Number (IntEnz) 3.4.23.1
CSA Homologues of 1am5There are 272 Homologs
CSA Entries With UniProtID
CSA Entries With EC Number 3.4.23.1
PDBe Entry 1am5
PDBSum Entry 1am5
MACiE Entry 1am5

Literature Report

IntroductionPepsins belong to the aspartic endopeptidase family and are digestive proteases present in the gastric juice of vertebrates. 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 1am5

Literature References

Notes:
Karlsen S
Structure and proposed amino-acid sequence of a pepsin from atlantic cod (Gadus morhua).
Acta Crystallogr D Biol Crystallogr 1998 54 32-46
PubMed: 9761815
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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