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
中科院分区:
文献类型:
--
作者:
Latruffe,N;Brenner,SC;Fleischer,S
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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DOI:
10.1016/s0021-9258(19)41121-6
发表时间:
1975
期刊:
The Journal of biological chemistry
影响因子:
--
作者:
H. Bock;S. Fleischer
通讯作者:
S. Fleischer
DOI:
--
发表时间:
1967
期刊:
影响因子:
--
作者:
G. Rouser;S. Fleischer
通讯作者:
S. Fleischer
影响因子:
3.7
作者:
K. V. Giri
通讯作者:
K. V. Giri
影响因子:
--
作者:
J. Riordan;B. Vallée
通讯作者:
B. Vallée
影响因子:
3.9
作者:
A. W. Tan;C. Smith;T. Aogaichi;G. Plaut
通讯作者:
G. Plaut