title: N-acetylmuramyl-L-alanine amidase of Vi phage III.
abstract: 1. A lytic enzyme was isolated from Vi phage III-induced lysate of Salmonella typhi, and purified about 200-fold by chromatography on IRC-50, CM-cellulose, and Sephadex G-75 columns. 2. Both E. coli B murein and muropeptide C6 were digested on incubation with the lytic enzyme. The main product of murein and muropeptide C6 digestion is identical with tetrapeptide Ala-Glu-DAP-Ala. The release of amino groups during digestion was not accompanied by the appearance of either reducing groups or hexosamines. 3. It is concluded that Vi phage III-induced lytic enzyme is N-acetylmuramyl-L-alanine amidase, which cleaves the amide bond between N-acetylmuramic acid and L-alanine.
mesh_terms: D000581:Amidohydrolases / Q000302:isolation & purification / Q000378:metabolism*; D007700:Kinetics; D009112:Muramic Acids / Q000378:metabolism; D012483:Salmonella Phages / Q000201:enzymology*; D012485:Salmonella typhi / Q000201:enzymology
chemical_list: D009112:Muramic Acids; D000581:Amidohydrolases