[2,2,6,6-四甲基-4-氧代哌啶-1-氧基修饰的牛肝谷氨酸脱氢酶：酶活性和催化特性]
[Bovine liver glutamate dehydrogenase modified by 2,2,6,6-tetramethyl-4-oxopiperidine-1-oxyl: enzymatic activity and catalytic properties].
作者信息
Agadzhanian S A, Pogosian A A, Karabashian L V
出版信息
Mol Biol (Mosk). 1982 Mar-Apr;16(2):345-51.
PMID:7070387
Abstract
When modified by 2,2,6,6-tetramethyl-4-oxopiperidine-1-oxyl (TMPO) bovine liver glutamate dehydrogenase (L-glutamate NAD(P) oxidoreductase, E. C. 1.4.1.3) looses its catalytical activity and sensitivity to allosteric inhibitor GTP. The stoicheiometry of the binding of TMPO to glutamate dehydrogenase has been studied--each protomer bound one molecule of TMPO. It is supposed that TMPO reacts with lysine residue located in the enzyme's active center.
摘要
当用2,2,6,6-四甲基-4-氧代哌啶-1-氧基（TMPO）修饰时，牛肝谷氨酸脱氢酶（L-谷氨酸NAD(P)氧化还原酶，E.C.1.4.1.3）会丧失其催化活性以及对变构抑制剂GTP的敏感性。已经研究了TMPO与谷氨酸脱氢酶结合的化学计量关系——每个原体结合一个TMPO分子。据推测，TMPO与位于酶活性中心的赖氨酸残基发生反应。
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