Reactivation of D-beta-hydroxybutyrate dehydrogenase with short-chain lecithins: stoichiometry and kinetic mechanism.
Reactivation of D-beta-hydroxybutyrate dehydrogenase with short-chain lecithins: stoichiometry and kinetic mechanism.
复制标题
用短链卵磷脂重新激活 D-β-羟基丁酸脱氢酶：化学计量和动力学机制。
DOI：
10.1021/bi00259a027
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发表时间：
1982
期刊：
影响因子：
2.9
通讯作者：
Fleischer,S
中科院分区：
文献类型：
--
作者：
Cortese,JD;Vidal,JC;Churchill,P;McIntyre,JO;Fleischer,S
Jorge D. Córtese，* Juan C. Vidal，s佩里丘吉尔，11 J奥利弗麦金太尔和西德尼弗莱舍 * 摘要：o-/3-羟基丁酸脱氢酶（BDH），作为可溶性、无脂脱辅基酶（无活性）从牛心脏或大鼠肝脏线粒体中纯化，可被单体状态的短链卵磷脂重新激活。用二己酰基-[PC（6：0）]、二庚酰基-[PC-（7：0）]和二辛酰基卵磷脂[PC（8：0）]再活化酶。作为磷脂浓度函数的酶活性的滴定曲线与酶含有两个相同的、不相互作用的卵磷脂结合位点的模型一致。同时占领这些网站（通过平衡随机机制）是激活脱辅基酶所必需的。用bothrat肝和牛心脱辅基酶得到了类似的结果。用不同卵磷脂得到的最大速度相似[110-140 gmol NAD+还原
Jorge D. Córtese,* Juan C. Vidal, s Perry Churchill, 11 J. Oliver McIntyre, and Sidney Fleischer* abstract: o-/3-Hydroxybutyrate dehydrogenase (BDH), purified as soluble, lipid-free apoenzyme (inactive) from either beef heart or rat liver mitochondria, can be reactivated by short-chain lecithins in the monomeric state. The enzyme was reactivated with dihexanoyl-[PC (6: 0)], diheptanoyl-[PC-(7: 0)], and dioctanoyllecithins [PC (8: 0)]. The titration curves of enzyme activity as a function of the phospholipid concen-tration are consistent with a model in which the enzyme contains two identical, noninteracting lecithin binding sites. The simultaneous occupation of these sites (via an equilibrium random mechanism) is required to activate the apoenzyme. Similar results were obtained with bothrat liver and beef heart apoenzymes. Themaximal velocities obtained with the dif-ferent lecithins were similar [110-140 gmol of NAD+ reduced