Madyarov Sh R
Institute of the Gene Pool of Plants and Animals, Uzbek Academy of Sciences, Tashkent, 101125, Uzbekistan.
Biochemistry (Mosc). 2014 Jul;79(7):687-93. doi: 10.1134/S0006297914070104.
The effects of detergents, trypsin, and bivalent metal ions on production of phosphatidic and lysophosphatidic acids by the action of phospholipase D (PLD) on lecithin and lysolecithin were studied. It was found that these reaction products and dodecyl sulfate ions activate PLD, whereas other anionic detergents are less effective. A protective effect of the functioning enzyme against its hydrolytic inactivation by trypsin was found. Bivalent metal ions can be arranged in the following sequence by their ability to activate PLD in the hydrolysis of lecithin and lysolecithin: Ca2+>Sr2+>Ba2+>Mg2+. These results are considered in relation to a proposed mechanism of activation and functioning of PLD with the participation of clusters of phosphatidates and lysophosphatidates. Such Me2+-induced formation of rafts or microdomains from the products of hydrolysis of phospholipids can rationalize not only PLD activation and self-regulation, but also the action of this mechanism on other components and properties of biomembranes. PLD and other lipolytic enzymes can be classified as lateral vector enzymes.
研究了去污剂、胰蛋白酶和二价金属离子对磷脂酶D（PLD）作用于卵磷脂和溶血卵磷脂产生磷脂酸和溶血磷脂酸的影响。发现这些反应产物和十二烷基硫酸根离子可激活PLD，而其他阴离子去污剂的效果较差。发现了发挥功能的酶对胰蛋白酶水解失活的保护作用。二价金属离子在卵磷脂和溶血卵磷脂水解中激活PLD的能力可按以下顺序排列：Ca2+>Sr2+>Ba2+>Mg2+。结合磷脂酸和溶血磷脂酸簇参与的PLD激活和功能的拟议机制来考虑这些结果。这种由磷脂水解产物形成的Me2+诱导的筏或微区不仅可以使PLD激活和自我调节合理化，而且可以使该机制对生物膜的其他成分和特性的作用合理化。PLD和其他脂解酶可归类为侧向载体酶。
