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Literature summary for 3.2.1.17 extracted from

  • Caldarini, M.; Vasile, F.; Provasi, D.; Longhi, R.; Tiana, G.; Broglia, R.A.
    Identification and characterization of folding inhibitors of hen egg lysozyme: an example of a new paradigm of drug design (2009), Proteins, 74, 390-399.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
additional information study on the inhibitory effect on the enzymatic activity of lysozyme of a number of peptides each containing about 10 amino acids and overlapping exhaustively the protein sequence. A small fraction of them are able to inhibit the biological activity of the protein with micromolar efficiency. The peptide displaying the same sequence of segment 91-100 of the protein, and essentially corresponding to the last three turns of helix C, is the most efficient. The inhibitory mechanism is nonconventional. Local elementary structures formed in the denatured state, drive the folding process and selected peptides compete with these structures in binding complementary regions of the protein, preventing the formation of the native state Gallus gallus

Organism

Organism UniProt Comment Textmining
Gallus gallus P00698
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