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Literature summary for 3.2.1.17 extracted from

  • Pham, E.; Truong, K.
    Engineered regulation of lysozyme by the SH3-CB1 binding interaction (2012), Protein Eng. Des. Sel., 25, 307-311.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
lysozyme is amplified from bacteriophage lambda cDNA, recombinant enzyme expression in Escherichia coli strain DH5alpha Homo sapiens

Protein Variants

Protein Variants Comment Organism
additional information design and construction, based on the protein structures of lambda lysozyme and the SH3 domain of human Crk, of a synthetic protein switch that controls the activity of lysozyme by sterically hindering its active cleft through the binding of SH3 to its CB1 peptide-binding partner. Modelling of fusion protein designs with lysozyme and CB1, in the absence of SH3, the lysozyme-CB1 fusion protein functions normally. In the presence of SH3, the lysozyme activity is inhibited and with the addition of excess CB1 peptides to compete for SH3 binding, the lysozyme activity is restored Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
additional information design and construction, based on the protein structures of lambda lysozyme and the SH3 domain of human Crk, of a synthetic protein switch that controls the activity of lysozyme by sterically hindering its active cleft through the binding of SH3 to its CB1 peptide-binding partner, i.e. fusion proteins Venus-CB1-lysozyme, Venus-CB1-lysozyme-CB1, Venus-CB1 and His-nSH3C. Modelling of fusion protein designs with lysozyme and CB1, in the absence of SH3, the lysozyme-CB1 fusion protein functions normally. In the presence of SH3, the lysozyme activity is inhibited and with the addition of excess CB1 peptides to compete for SH3 binding, the lysozyme activity is restored Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
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-
-

Synonyms

Synonyms Comment Organism
lambda lysozyme
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Homo sapiens