title: [Homology of lysozymes of bacterial and vertebrate origin].
abstract: Theoretical analysis of structural and functional organization of vertebrate lysozymes, T4-phage lysozyme, lambda-phage endolysin and extracellular lysozyme of Chalaropsis species suggests a genetic relationship between the enzymes in question. It has been shown that the lysozyme sequences exhibit both inter- and intramolecular homology. The obtained data lend support to the concept postulating a common ancestor for the lysozyme family and subsequent divergent evolution of these proteins. The two-component primary structure of lysozymes can result from structural gene duplication and allows to explain similar catalytic activity and different substrate specificity of these enzymes by the differentiation and specialization of functions of the N- and C-components of the protein chains.
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D010582:Bacteriophage lambda / Q000201:enzymology*; D004926:Escherichia coli / Q000201:enzymology*; D005796:Genes; D003904:Mitosporic Fungi / Q000201:enzymology*; D009113:Muramidase / Q000235:genetics* / Q000378:metabolism; D011487:Protein Conformation; D013045:Species Specificity; D013305:Streptomyces griseus / Q000201:enzymology*; D013604:T-Phages / Q000201:enzymology*
chemical_list: D009113:Muramidase
vernacular_title: Gomologiia lizotsimov bakterial'nogo i zhivotnogo proiskhozhdeniia.