Boekelheide K, Patt S L, Weisz G, Baldo J H, Sykes B D
Can J Biochem. 1979 Jun;57(6):785-88. doi: 10.1139/o79-097.
The cleavage of cell wall tetrasaccharide, the beta(1 leads to 4)-linked dimer of the basic repeating disaccharide N-acetyl-D-glucosamine-beta(1 leads to 4)-N-acetyl-D-muramic acid, by lysozyme has been studied at various concentrations of lysozyme and over long time ranges. A theoretical analysis of the kinetic results indicates that direct hydrolysis of the tetrasaccharide by binding in subsities CDEF of the active site of lysozyme is significant at long times relative to the transglycosylation pathway. The binding constant for tetrasaccharide in CDEF is shown to be 10(3) times larger than that determined on the basis of an analysis of kinetic data over a more restricted range of times and concentrations.
在不同溶菌酶浓度和较长时间范围内，研究了溶菌酶对细胞壁四糖（即基本重复二糖N-乙酰-D-葡糖胺-β(1→4)-N-乙酰-D-胞壁酸的β(1→4)连接二聚体）的裂解作用。动力学结果的理论分析表明，相对于转糖基化途径，在长时间条件下，溶菌酶活性位点的CDEF亚位点结合导致四糖直接水解的作用显著。结果显示，四糖在CDEF中的结合常数比基于在更有限的时间和浓度范围内对动力学数据进行分析所确定的值大10³倍。
