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单细胞绿藻集胞藻谷氨酸脱氢酶:底物诱导的构象转变。

Glutamate dehydrogenase of the unicellular green alga Scenedesmus acutus : Substrate-induced conformational transition.

机构信息

Fakultät für Biologie der Universität, Postfach 5560, D-7750, Konstanz, Germany.

出版信息

Planta. 1983 Jul;157(4):367-70. doi: 10.1007/BF00397409.

Abstract

The coenzyme-non-specific glutamate dehydrogenase (EC 1.4.1.3) from Scenedesmus acutus in inhibited by p-hydroxymercuribenzoate only in the deamination reaction. From this result and from its stability in the presence of urea it is concluded that this enzyme exhibits and equilibrium between three conformations: aminating and deaminating conformations induced by NADH-2-oxoglutarate and NAD(+)-glutamate, respectively, and the "native" conformation in the absence of substrates.

摘要

小球藻中的辅酶非特异性谷氨酸脱氢酶(EC 1.4.1.3)仅在脱氨反应中被对羟汞苯甲酸抑制。根据这一结果以及脲存在时的稳定性,可以得出结论,该酶表现出三种构象之间的平衡:由 NADH-2-酮戊二酸和 NAD(+)-谷氨酸分别诱导的氨化和脱氨构象,以及在没有底物的情况下的“天然”构象。

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