为您找到"
GDHH-1
"相关结果约100,000,000个
Glutamate dehydrogenase (GLDH, GDH) is an enzyme observed in both prokaryotes and eukaryotic mitochondria. The aforementioned reaction also yields ammonia, which in eukaryotes is canonically processed as a substrate in the urea cycle. Typically, the α-ketoglutarate to glutamate reaction does not occur in mammals, as glutamate dehydrogenase equilibrium favours the production of ammonia and α ...
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 (Figure 1) [1]. In addition to contributing to Krebs cycle anaplerosis and energy production, GDH function is linked to redox homeostasis and cell signaling processes [2, 3].
Glutamate dehydrogenase (GDH) is a key enzyme in mammalian glutamate metabolism. It is located at the intersection of multiple metabolic pathways and participates in a variety of cellular activities. GDH activity is strictly regulated by a variety of allosteric compounds. Here, we review the unique …
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. In mammalian tissues, oxidative deamination of glutamate via GDH generates α-ketoglutarate, which is metabolized by the Krebs cycle ...
Glutamate dehydrogenase is an enzyme that localizes predominantly to the mitochondrial matrix (and to a lesser extent to the rough endoplasmic reticulum) and catalyzes the reversible oxidative deamination of glutamate to produce α-ketoglutarate and a free ammonium ion [13]. The oxidative deamination of glutamate uses NAD + as cofactor and releases H + and the reduced compound NADH, whereas ...
Glutamate dehydrogenase (GDH) is found in all organisms and catalyzes the reversible oxidative deamination of l -glutamate to 2-oxoglutarate using NAD + and/or NADP + as coenzyme [1]. In nearly all organisms, GDH is a homohexameric enzyme composed of subunits comprised of ~500 residues in animals and ~450 residues in the other kingdoms. While the chemical details of the enzymatic reaction have ...
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, ...
GLUD1 (glutamate dehydrogenase 1) is a mitochondrial matrix enzyme, one of the family of glutamate dehydrogenases that are ubiquitous in life, with a key role in nitrogen and glutamate (Glu) metabolism and energy homeostasis. This dehydrogenase is expressed at high levels in liver, brain, pancreas and kidney, but not in muscle. In the pancreatic cells, GLUD1 is thought to be involved in ...
1 School of Mathematics, Statistics and Computational Sciences, Central University of Rajasthan, Bandarsindri, Ajmer, India. 2 Institute of Theoretical and Experimental Biophysics, Pushchino, Russia.
Glutamate dehydrogenase (GDH) is found in all organisms and catalyzes the reversible oxidative deamination of l -glutamate to 2-oxoglutarate using NAD + and/or NADP + as coenzyme [1]. In nearly all organisms, GDH is a homohexameric enzyme composed of subunits comprised of ~500 residues in animals and ~450 residues in the other kingdoms. While the chemical details of the enzymatic reaction have ...