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Literature summary for 3.2.1.17 extracted from

  • Alcantara, E.H.; Kim, D.H.; Do, S.I.; Lee, S.S.
    Bi-functional activities of chimeric lysozymes constructed by domain swapping between bacteriophage T7 and K11 lysozymes (2007), J. Biochem. Mol. Biol., 40, 539-546.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
additional information constructions of chimeric lysozymes are carried out by swapping the N-terminal and C-terminal domains between phage T7 and K11 lysozymes. This technique generates two chimeras, T7K11-lysozyme (N-terminal T7 domain and C-terminal K11 domain) and K11T7-lysozyme (N-terminal K11 domain and C-terminal T7 domain), which are both enzymatically active. The amidase activity of T7K11-lysozyme is comparable with the parental enzymes while K11T7-lysozyme exhibits an activity that is approximately 45% greater than the wild-type lysozymes. The chimeric constructs have optimum pH of 7.2-7.4 similar to the parental lysozymes but exhibit greater thermal stabilities. The chimeras inhibit transcription comparable with the parental lysozymes depending on the source of their N-terminals. Domain swapping technique localizes the N-terminal region as the domain responsible for the transcription inhibition specificity of the wild type T7 and K11 lysozymes Escherichia phage T7
additional information constructions of chimeric lysozymes are carried out by swapping the N-terminal and C-terminal domains between phage T7 and K11 lysozymes. This technique generates two chimeras, T7K11-lysozyme (N-terminal T7 domain and C-terminal K11 domain) and K11T7-lysozyme (N-terminal K11 domain and C-terminal T7 domain), which are both enzymatically active. The amidase activity of T7K11-lysozyme is comparable with the parental enzymes while K11T7-lysozyme exhibits an activity that is approximately 45% greater than the wild-type lysozymes. The chimeric constructs have optimum pH of 7.2-7.4 similar to the parental lysozymes but exhibit greater thermal stabilities. The chimeras inhibit transcription comparable with the parental lysozymes depending on the source of their N-terminals. Domain swapping technique localizes the N-terminal region as the domain responsible for the transcription inhibition specificity of the wild type T7 and K11 lysozymes Enterobacteria phage K11

Organism

Organism UniProt Comment Textmining
Enterobacteria phage K11
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Escherichia phage T7
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Purification (Commentary)

Purification (Comment) Organism
rapid purification scheme in purifying both the wild-type and chimeric lysozymes Escherichia phage T7
rapid purification scheme in purifying both the wild-type and chimeric lysozymes Enterobacteria phage K11