Essential sulfhydryl for reduced nicotinamide adenine dinucleotide binding in D-beta-hydroxybutyrate dehydrogenase.

Essential sulfhydryl for reduced nicotinamide adenine dinucleotide binding in D-beta-hydroxybutyrate dehydrogenase.
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D-β-羟基丁酸脱氢酶中减少烟酰胺腺嘌呤二核苷酸结合所必需的巯基。

DOI:
10.1021/bi00564a021
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发表时间:
1980
期刊:
影响因子:
2.9
通讯作者:
Fleischer,S
Fleischer,S
中科院分区:
生物学3区
文献类型:
--
作者:
Latruffe,N;Brenner,SC;Fleischer,S

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Norbert Latruffe,1 Stephen C. Brenner和Sidney Fleischer** 摘要:化学衍生化研究已针对D-|3-羟基丁酸脱氢酶,一种脂质需求酶。与N-乙基马来酰亚胺的反应导致酶活性和辅酶结合的进行性和平行损失。当每摩尔酶衍生1当量巯基时,这两种功能都丧失了。用甲基汞或空气氧化使酶失活也会导致辅酶结合丧失。我们的结论是,一个单一的“必需的”巯基是必需的辅酶结合,因此酶的活性。只有两种“可接近的”D-/3-羟基丁酸脱氢酶是一种需要脂质的酶,其功能绝对需要卵磷脂。脱辅基脱氢酶,这是缺乏脂质,已被纯化至同质。它是无活性的,但可以通过形成活性酶-磷脂复合物而发挥功能。有关综述,请参见Fleischer et al.(1974年)。o-^-羟基丁酸脱氢酶可能是研究最广泛的脂类需要酶,我们正在研究
Norbert Latruffe, 1 Stephen C. Brenner, and Sidney Fleischer** abstract: Chemical derivatization studies have been directed at the sulfhydryl group of D-| 3-hydroxybutyrate dehydrogenase, a lipid-requiring enzyme. Reaction with (V-ethylmaleimide leads to progressive and parallel loss of both enzymic activity and coenzyme binding. Both functions are lost when 1 equiv of sulfhydryl is derivatized per mol of enzyme. Inactivation of the enzyme with methylmercury or with air oxidation also leads to loss of coenzyme binding. We conclude that a single “essential” sulfhydryl is required for coenzyme binding and consequently for enzymic activity. Only two “accessible” D-/3-Hydroxybutyrate dehydrogenase is a lipid-requiring enzyme with an absolute requirement of lecithin for function. The apodehydrogenase, which is devoid of lipid, has been purified to homogeneity. It is inactive, but can be made functional by forming an active enzyme-phospholipid complex. For a review, see Fleischer et al.(1974). o-^-Hydroxybutyrate dehydrogenase is perhaps the most extensively studied lipid-requiring enzyme, and we are studying
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