Characterization of recombinant murine GDE4 and GDE7, enzymes producing lysophosphatidic acid and/or cyclic phosphatidic acid.
Characterization of recombinant murine GDE4 and GDE7, enzymes producing lysophosphatidic acid and/or cyclic phosphatidic acid.
复制标题
重组鼠 GDE4 和 GDE7（产生溶血磷脂酸和/或环磷脂酸的酶）的表征。
DOI：
10.1093/jb/mvab091
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发表时间：
2022
期刊：
影响因子：
--
通讯作者：
Izumi T.
中科院分区：
文献类型：
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作者：
Tserendavga B;Ohshima N;Fujita C;Yuzawa K;Ohshima M;Yanaka N;Minamishima YA;Izumi T.
GDE 4和GDE 7是表现出溶血磷脂酶D活性的膜结合酶。我们发现GDE 7不仅产生溶血磷脂酸（LPA），而且还通过转磷脂酰化反应从溶血磷脂中产生环状磷脂酸（cPA）。相比之下，GDE 4只产生LPA。底物特异性的分析表明，1-烷基溶血磷脂是两种酶的首选底物，而不是1-烷基溶血磷脂和1-烯基溶血磷脂。在测试的具有不同极性头部基团的各种溶血磷脂中，溶血磷脂酰甘油和溶血磷脂酰丝氨酸分别是GDE 4和GDE 7的优选底物。GDE 4和GDE 7的酶活性对二价阳离子的依赖性的详细分析表明，多个二价阳离子结合在两种酶的活性位点。综上所述，这些结果表明GDE 7可能在体内作为一种产生cPA的酶发挥作用。
GDE4 and GDE7 are membrane-bound enzymes that exhibit lysophospholipase D activities. We found that GDE7 produced not only lysophosphatidic acid (LPA) but also cyclic phosphatidic acid (cPA) from lysophospholipids by a transphosphatidylation reaction. In contrast, GDE4 produced only LPA. The analysis of substrate specificity showed that 1-alkyl-lysophosphospholipids were preferred substrates for both enzymes rather than 1-alkyl-lysophospholipids and 1-alkenyl-lysophospholipids. Among the various lysophospholipids with different polar head groups that were tested, lysophosphatidylglycerol and lysophosphatidylserine were preferred substrates for GDE4 and GDE7, respectively. The detailed analysis of the dependency of the enzyme activities of GDE4 and GDE7 on divalent cations suggested multiple divalent cations were bound in the active sites of both enzymes. Taken together, these results suggest the possibility that GDE7 functions as a cPA-producing enzyme in the body.