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首页> 外文期刊>Journal of bacteriology >Membrane-bound thioesterase activity in mycoplasmas.
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Membrane-bound thioesterase activity in mycoplasmas.

机译：支原体中的膜结合硫酯酶活性。

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摘要

Thioesterase activity was found in all mycoplasmas tested. Activity was highest in Acholeplasma species, whereas most of the sterol-requiring Mycoplasma species showed little activity. The thioesterase activity of Acholoplasma laidlawii is confined to the cell membrane. The enzyme could not be released from the membrane by either low- or high-ionic-strength solutions, with or without ethylenediaminetetraacetic acid, nor solubilized by detergents. The enzyme has a general specificity for long-chain saturated and unsaturated fatty acid thioesters. The preferred substrates among the saturated fatty acyl derivatives are the myristyl and palmityl derivatives. Arrhenius plots of thioesterase activities in A. laidlawii membranes enriched with elaidic or palmitic acids showed discontinuities at 12 and 18 degrees C, respectively. The possible regulatory significance of the thioesterase activity for the fatty acid synthetase and the possibllity that the activity of the enzyme is controlled by the physical state of membrane lipids are discussed.
机译：在所有测试的支原体中均发现了硫酯酶活性。活性在无花果属物种中最高，而大多数需要固醇的支原体物种几乎没有活性。放线菌（Acholoplasma laidlawii）的硫酯酶活性仅限于细胞膜。在有或没有乙二胺四乙酸的情况下，低或高离子强度溶液都无法从膜上释放酶，也不能被去污剂溶解。该酶对长链饱和和不饱和脂肪酸硫酯具有一般特异性。在饱和脂肪酰基衍生物中优选的底物是肉豆蔻基和棕榈基衍生物。在富含蛋黄酸或棕榈酸的A. Ladlawii膜中，硫酯酶活性的阿累尼乌斯曲线分别在12和18摄氏度下显示出不连续性。讨论了硫酯酶活性对脂肪酸合成酶的可能的调控意义以及该酶的活性受膜脂的物理状态控制的可能性。

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