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由于二氢硫辛酸和NADH导致的α-酮戊二酸脱氢酶协同性质的变化。

Change in alpha-ketoglutarate dehydrogenase cooperative properties due to dihydrolipoate and NADH.

作者信息

Bunik V I, Buneeva O A, Gomazkova V S

机构信息

Department of Biochemistry, Moscow State University, USSR.

出版信息

FEBS Lett. 1990 Aug 20;269(1):252-4. doi: 10.1016/0014-5793(90)81166-l.

DOI:10.1016/0014-5793(90)81166-l
PMID:2117555
Abstract

Reducing 2 SH-groups of KGD by dihydrolipoate leads to cooperativity in substrate binding. Cooperative properties of KGD in the KGD complex are modulated by NADH. Physiological significance of these observations is discussed.

摘要

二氢硫辛酸使2-酮戊二酸脱氢酶（KGD）的两个巯基还原，导致底物结合产生协同性。KGD复合物中KGD的协同性质受NADH调节。讨论了这些观察结果的生理学意义。

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Change in alpha-ketoglutarate dehydrogenase cooperative properties due to dihydrolipoate and NADH.由于二氢硫辛酸和NADH导致的α-酮戊二酸脱氢酶协同性质的变化。
FEBS Lett. 1990 Aug 20;269(1):252-4. doi: 10.1016/0014-5793(90)81166-l.
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