Begunova E A, Stepnaya O A, Lysanskaya V Ya, Kulaev I S
Skryabin Institute of Biochemistry and Physiology of Microorganisms, Russian Academy of Sciences, Pushchino, 142292, Moscow Region, Russia.
Biochemistry (Mosc). 2003 Jul;68(7):735-9. doi: 10.1023/a:1025074714910.
Specificity of Staphylococcus aureus 209P cell wall hydrolysis by the L1 and L2-bacteriolytic enzymes from lysoamidase lytic complex was studied. L1-peptidase was shown to display both glycyl-glycine endopeptidase and N-acetylmuramyl-L-alanine amidase enzymatic activities on the S. aureus peptidoglycan molecule, whereas L2-peptidase acts as N-acetylmuramyl-L-alanine amidase.
研究了来自溶菌酰胺酶溶菌复合物的L1和L2溶菌酶对金黄色葡萄球菌209P细胞壁水解的特异性。结果表明,L1肽酶对金黄色葡萄球菌肽聚糖分子同时具有甘氨酰-甘氨酸内肽酶和N-乙酰胞壁酰-L-丙氨酸酰胺酶的酶活性,而L2肽酶则作为N-乙酰胞壁酰-L-丙氨酸酰胺酶发挥作用。