Acitivity of glutamine synthetase toward the optical isomers of alpha-aminoadipic acid.
Acitivity of glutamine synthetase toward the optical isomers of alpha-aminoadipic acid.
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谷氨酰胺合成酶对 α-氨基己二酸光学异构体的活性。
DOI：
10.1021/bi00875a017
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发表时间：
1966
期刊：
影响因子：
2.9
通讯作者：
A. Meister
中科院分区：
文献类型：
--
作者：
V. P. Wellner;M. Zoukis;A. Meister
Vaira P. Wellner、玛丽Zoukis和Alton Meister摘要：纯化的羊脑谷氨酰胺合成酶作用于α-氨基己二酸的光学异构体，从而催化l-和D-高谷氨酰胺、类似的w-异羟肟酸的合成，以及（在不存在氨和羟胺的情况下）6-哌啶酮-2-羧酸的形成。确定了几种反应的表观Km值和相对最大速度。虽然由α-氨基己二酸形成异羟肟酸的速率是相当大的（与谷氨酸的异构体相比），但高谷氨酰胺合成的速率小于异羟肟酸形成的速率的3%。
Vaira P. Wellner, Mary Zoukis, and Alton Meister abstract: Purified sheep brain glutamine synthetase acts on the optical isomers of a-aminoadipic acid thus catalyzing the synthesis of l- and D-homoglu-tamine, the analogous w-hydroxamic acids, and (in the absence of ammonia and hydroxylamine) the formation of 6-piperidone-2-carboxylic acid. Values for apparent Km and relative maximal velocity were determined for the several reactions. Although the rates of hydroxamate formation from the a-aminoadipic acids are substantial (as compared to the isomers of glutamic acid), therates of homoglutamine synthesis are less than 3% of those of hydroxamate formation.