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Literature summary extracted from

  • Chen, S.L.; Li, Z.S.; Fang, W.H.
    Theoretical investigation of astacin proteolysis (2012), J. Inorg. Biochem., 111, 70-79.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.4.24.21 crystal structure analysis, PDB ID 3LQ0 Astacus astacus

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.24.21 L-prolyl-L-leucyl-N-hydroxyglycinamide enzyme binding structure modeling Astacus astacus

Organism

EC Number Organism UniProt Comment Textmining
3.4.24.21 Astacus astacus P07584
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
3.4.24.21 Hydrolysis of peptide bonds in substrates containing five or more amino acids, preferentially with Ala in P1', and Pro in P2' proposed reaction mechanism for astacin Astacus astacus
a

General Information

EC Number General Information Comment Organism
3.4.24.21 evolution the enzyme belongs to the family of extracellular zinc peptidases, termed stacin family, and of the metzincin superfamily Astacus astacus
3.4.24.21 additional information analysis of the astacin reaction mechanism from the crystal structure by computational methods, Optimized structure of the astacin active site with the model substrate bound, overview. All calculations were performed using density functional theory with the hybrid functional B3LYP, which is composed of Becke's three-parameter hybrid exchange functional (B3) and the correlation functional of Lee, Yang, and Parr. A model of the active site of astacin is built on the basis of the crystal structure of astacin in complex with the Pro-Leu-Gly-hydroxamate inhibitor, PDB entry 1QJJ Astacus astacus