谷氨酸合酶：来自酿酒酵母的依赖还原型烟酰胺腺嘌呤二核苷酸的酶的特性
Glutamate synthase: properties of the reduced nicotinamide adenine dinucleotide-dependent enzyme from Saccharomyces cerevisiae.
作者信息
Roon R J, Even H L, Larimore F
出版信息
J Bacteriol. 1974 Apr;118(1):89-95. doi: 10.1128/jb.118.1.89-95.1974.
Abstract
A reduced nicotinamide adenine dinucleotide (NADH)-dependent glutamate synthase has been detected and partially purified from crude extracts of Saccharomyces cerevisiae. The enzyme is specific for NADH, glutamine, and alpha-ketoglutarate (K(m) values of 2.6 muM, 1.0 mM, and 140 muM, respectively) and has a pH optimum between 7.1 and 7.7. The stoichiometry of the reaction has been determined as 2 mol of glutamate synthesized per mol of glutamine consumed. Glutamate synthase can be distinguished from either of the glutamate dehydrogenases of yeast on the basis of its substrate requirements and behavior during agarose gel and ion exchange chromatography. Variations in the specific activity of glutamate synthase, which occur in response to changes in the growth medium, are similar in character to those observed with the nicotinamide adenine dinucleotide phosphate-dependent (anabolic) glutamate dehydrogenase.
摘要
已从酿酒酵母的粗提物中检测到并部分纯化了一种依赖于还原型烟酰胺腺嘌呤二核苷酸（NADH）的谷氨酸合酶。该酶对NADH、谷氨酰胺和α-酮戊二酸具有特异性（K(m)值分别为2.6 μM、1.0 mM和140 μM），最适pH在7.1至7.7之间。已确定该反应的化学计量比为每消耗1摩尔谷氨酰胺合成2摩尔谷氨酸。根据其底物需求以及在琼脂糖凝胶和离子交换色谱中的行为，谷氨酸合酶可与酵母的两种谷氨酸脱氢酶区分开来。谷氨酸合酶的比活性会随着生长培养基的变化而变化，其变化特征与观察到的依赖于烟酰胺腺嘌呤二核苷酸磷酸（合成代谢）的谷氨酸脱氢酶相似。
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