Structural analysis and biological significance of the cell wall lytic enzymes of Streptococcus pneumoniae and its bacteriophage (original) (raw)

1992, Fems Microbiology Letters

AI-generated Abstract

This research explores the structural characteristics and biological implications of lytic enzymes in Streptococcus pneumoniae and its associated bacteriophage. It highlights the role of the principal pneumococcal autolysin in cell division, the modular organization of these enzymes, and their evolutionary adaptations. Key findings indicate that the C-terminal domains facilitate substrate binding, while the N-terminal domains confer enzymatic specificity, suggesting the evolution of these enzymes through modular exchange.