Glutamate dehydrogenase (GDH) is an enzyme that is essential in the metabolism of amino acids. It catalyzes the reversible conversion of glutamate to -ketoglutarate, which is accompanied by NAD+ and NADH interconversion. GDH is found in a variety of organisms, including bacteria, plants, and animals, and it is especially prevalent in mammalian liver and kidneys.
GDH is required for cellular energy production as well as nitrogen metabolism. It contributes to the Krebs cycle, commonly known as the tricarboxylic acid (TCA) cycle or the citric acid cycle, by aiding glutamate oxidative deamination. This process produces energy in the form of ATP and serves as an intermediary in biosynthetic pathways.
Furthermore, GDH regulates glutamate, a significant excitatory neurotransmitter in the central nervous system. GDH acts as a “biosensor” in some brain areas, responding to variations in glutamate concentration by regulating its enzymatic activity accordingly. This regulating system contributes to neurotransmission and overall brain function by maintaining appropriate glutamate levels.
Because of its consequences in a variety of physiological and pathological circumstances, GDH is the focus of current research. Its dysregulation has been associated with neurodegenerative diseases like as Alzheimer’s and Parkinson’s, as well as metabolic problems such as hyperinsulinism. Understanding how GDH works and how it is regulated may provide insights into these disorders and possibly lead to the development of therapeutic approaches.
Glutamate dehydrogenase (GDH) is an enzyme that is essential in the metabolism of amino acids. It catalyzes the reversible conversion of glutamate to alpha-ketoglutarate while also utilizing NAD+ or NADP+ as a cofactor. GDH is found in a wide range of organisms, including bacteria, fungi, and animals. It is primarily found in the liver, pancreas, and kidneys of animals. GDH exists in two distinct forms: NAD+-linked GDH and NADP+-linked GDH. GDH is essential in the regulation of ammonia metabolism in the liver. It is in charge of converting ammonia to glutamate, which is then used in the synthesis of other amino acids like alanine and aspartate. The enzyme is also involved in the gluconeogenesis process, which converts excess amino acids to glucose. GDH has been extensively studied in the context of neurodegenerative disorders such as Alzheimer’s. In these conditions, glutamate homeostasis is disrupted, resulting in the accumulation of excess glutamate, which can be toxic to neurons. GDH has been identified as a potential therapeutic target because inhibiting it could reduce glutamate production and protect neurons from damage.
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