GDH2是GDH的无内含子形式，被认为是在不到2千3百万年前 [ 21 ]的情况下由GDH1的再定位引起的 [ 20 ]。 GDH2是X连锁的，主要存在于神经元和睾丸组织中 [ 20 ]。 GDH2与GDH1的不同之处在于，它对GTP抑制的敏感性较低，但对ADP活化的敏感性更高，热稳定性低得多，并且活性 …

Glutamate dehydrogenase (GDH) is a hexameric enzyme that catalyzes the reversible conversion of glutamate to α-ketoglutarate and ammonia while reducing NAD(P)+ to NAD(P)H. It is found in all living organisms serving both catabolic and anabolic ...

Glutamate dehydrogenase (GDH) is a homohexameric enzyme that catalyzes the reversible oxidative deamination of l -glutamate to 2-oxoglutarate. Only in the animal kingdom is this enzyme heavily allosterically regulated by a wide array of metabolites. The major activators are ADP and leucine and inhibitors include GTP, palmitoyl CoA, and ATP.

Glutamate Dehydrogenase (GLDH, GDH) is a mitochondrial enzyme that converts glutamate into α-ketoglutarate in the tricarboxylic acid (TCA) cycle, which is a series of ATP-synthesis metabolic reactions. GLUD1 and GLUD2 encode two glutamate dehydrogenase isoenzymes.

2020年10月2日 · D-glycerate dehydrogenase (GDH, also known as hydroxypyruvate reductase, HPR) catalyzes the reversible reaction of (R)-glycerate + NAD+ to hydroxypyruvate + NADH + H+.

In-vitro, glutamate dehydrogenase (GDH) catalyzes the reversible oxidative deamination of glutamate to α-ketoglutarate (α-KG). GDH is found in all organisms, but in animals is allosterically regulated by a wide array of metabolites. For many years, it was not at all clear why animals required such complex control.

谷氨酸脱氢酶 (GLDH或GDH)是线粒体酶，主要存在于肝脏、心肌及肾脏，少量存在于脑、骨骼肌及白细胞中。 GDH除催化L-谷氨酸脱氢外，还具有催化其他氨基酸如L-缬氨酸、L-2-氨基丁酸及L-亮氨酸脱氨。 其测定方法主要是连续监测法。 0-1.5U/L。 异常结果： 升高:急性病毒性肝炎、慢性肝炎、肝硬化. 检查前: (1) 抽血前一天不吃过于油腻、高蛋白食物，避免大量饮酒。 血液中的酒精成分会直接影响检验结果。 (2) 体检前一天的晚八时以后，应开始禁食12小时，以免影响检测 …

Glutamate dehydrogenase (GLDH,GDH) is a hexameric enzyme that catalyzes the conversion of glutamate to α-ketoglutarate and ammonia, while reducing NAD(P)+ to NAD(P)H. GDH pathway is linked to diverse cellular processes, including ammonia metabolism, acid-base equilibrium, redox homeostasis , lipid biosynthesis, and lactate production.

2017年2月8日 · Glutamate dehydrogenase (GDH) is a hexameric enzyme that catalyzes the reversible conversion of glutamate to α-ketoglutarate and ammonia while reducing NAD(P)⁺ to NAD(P)H. It is found in all living organisms serving both catabolic and anabolic reactions.

With an important role in carbon and nitrogen metabolism, glutamate dehydrogenase (GDH) is a widely distributed enzyme, found in eukaryotes, archaea and bacteria. Its physiological function is catalyzing the reversible oxidative deamination of glutamate into α-ketoglutarate and ammonia (Miñambres et al., 2000).