Hara H, Suzuki H
FEBS Lett. 1984 Mar 12;168(1):155-60. doi: 10.1016/0014-5793(84)80226-4.
A simple and efficient procedure to assay peptidoglycan synthesis in vitro was established. By this procedure, a novel activity for glycan polymerization in Escherichia coli was found in the fraction containing no detectable penicillin-binding protein (PBP). This polymerase activity was relatively insensitive to moenomycin, showed requirement for Ca2+ or Mn2+ but not for Mg2+, and led to production of uncross-linked glycan chains. These properties distinguished the glycan polymerase from the activities shown by the fractions containing PBPs. The glycan polymerase catalyzing polymerization of glycan units from lipid intermediates was purified and identified as a protein of 34 kDa.
建立了一种简单有效的体外测定肽聚糖合成的方法。通过该方法，在不含可检测到的青霉素结合蛋白（PBP）的组分中发现了大肠杆菌中一种新的聚糖聚合活性。这种聚合酶活性对莫能菌素相对不敏感，需要Ca2+或Mn2+而非Mg2+，并导致产生未交联的聚糖链。这些特性将聚糖聚合酶与含PBPs的组分所显示的活性区分开来。催化脂质中间体聚糖单元聚合的聚糖聚合酶被纯化，并鉴定为一种34 kDa的蛋白质。
