Pernas P, Olivier J L, Legoy M D, Bereziat G
Laboratoire de Biochimie CHU St-Antoine, URA CNRS 217, Paris, France.
Biochem Biophys Res Commun. 1990 Apr 30;168(2):644-50. doi: 10.1016/0006-291x(90)92369-b.
The catalytic activity of extracellular phospholipase A2 was studied in low polarity solvents where hydrolytic enzymes have been demonstrated to catalyze synthesis reactions. It was demonstrated that extracellular phospholipase A2 can catalyze the esterification of lysophosphatidylcholine with oleic acid. Up to 6.5% of lysophosphatidylcholine can be esterified into phosphatidylcholine. This activity requires a preincubation of the enzyme in a pH 9 aqueous solution containing calcium, before the incubation in the non-aqueous solvent. No transfer of fatty acid between a phospholipid and a lysophospholipid or between two phospholipids was observed. These results may be useful in understanding the function of the membrane phospholipase A2 which may catalyze acylation or deacylation depending on the local physico-chemical environment.
在水解酶已被证明可催化合成反应的低极性溶剂中，研究了细胞外磷脂酶A2的催化活性。结果表明，细胞外磷脂酶A2可催化溶血磷脂酰胆碱与油酸的酯化反应。高达6.5%的溶血磷脂酰胆碱可被酯化为磷脂酰胆碱。在非水溶剂中孵育之前，该活性需要酶在含有钙的pH 9水溶液中进行预孵育。未观察到脂肪酸在磷脂与溶血磷脂之间或两种磷脂之间的转移。这些结果可能有助于理解膜磷脂酶A2的功能，其可能根据局部物理化学环境催化酰化或脱酰化反应。
