Snider M D, Kennedy E P
J Bacteriol. 1977 Jun;130(3):1072-83. doi: 10.1128/jb.130.3.1072-1083.1977.
Glycerophosphate acyltransferase, a membrane-bound enzyme catalyzing the initial step of phospholipid biosynthesis in Escherichia coli, has been extracted with Triton X-100, a nonionic detergent, and purified 20- to 40-fold. This preparation is free from lysophosphatidate acyltransferase. Glycerophosphate acyltransferase is inactive in detergent extracts, but can be reconstituted by the addition of phospholipid. Under such conditions, the enzyme is associated with phospholipid. The sole product of the reaction with acyl coenzyme A as substrate is 1-acyl-sn-glycero-3-phosphate. Furthermore, the enzyme shows a marked preference for saturated fatty acyl conenzyme A, implying that this enzyme is responsible for the predominance of saturated moieties in position 1 of E. coli phospholipids. Acyltransferase from two mutants, plsA and plsB, was partially purified and characterized. Results support the view that plsB is a structural gene for the acyltransferase, but suggest that the plsA gene product is not directly involved in phospholipid biosynthesis.
甘油磷酸酰基转移酶是一种膜结合酶，催化大肠杆菌中磷脂生物合成的起始步骤，已用非离子去污剂 Triton X-100 提取，并纯化了 20 至 40 倍。该制剂不含溶血磷脂酸酰基转移酶。甘油磷酸酰基转移酶在去污剂提取物中无活性，但可通过添加磷脂进行重构。在这种条件下，该酶与磷脂结合。以酰基辅酶 A 为底物的反应的唯一产物是 1-酰基-sn-甘油-3-磷酸。此外，该酶对饱和脂肪酰辅酶 A 表现出明显的偏好，这意味着该酶负责大肠杆菌磷脂 1 位上饱和部分的优势。来自两个突变体 plsA 和 plsB 的酰基转移酶被部分纯化并进行了表征。结果支持 plsB 是酰基转移酶的结构基因的观点，但表明 plsA 基因产物不直接参与磷脂生物合成。
