Glutamate dehydrogenase (GLDH) Cat # Abt P-1009 Glutamate dehydrogenase (GLDH, EC1.4.1.2) is an enzyme present in the mitochondrial matrix of cells that can convert glutamate into α- Ketoglutaric acid can also catalyze reverse reactions. GLDH is a type of allosteric enzyme that is produced in the body through reactions such as oxidative dehydrogenation, transamination, co dehydrogenation, and non oxidative dehydrogenation, among which co dehydrogenation is the most important. GLDH is a key molecule in assimilation and differentiation pathways, with the highest content in the liver, mainly present in liver lobular cells, followed by organs such as the kidney, pancreas, brain, small intestine mucosa, and heart. Due to the liver specificity of GLDH, changes in GLDH activity in peripheral blood reflect changes in liver function to a certain extent. Biochemical research: In addition to catalyzing the dehydrogenation of L-glutamic acid, GLDH also catalyzes the deamination of other amino acids such as L-valine, L-2-aminobutyric acid, and L-leucine. Its measurement method is mainly continuous monitoring. Additionally, GLDH reversibly catalyzes the formation of α- The reaction of ketoglutaric acid, H+, NH3, and NADH generates glutamic acid. As NADH is the color source of many biochemical detection reactions, the corresponding GLDH catalyzed reaction is often widely used as the final detection step of biochemical detection reagents. Our company's glutamate dehydrogenase is a genetically recombinant product with high purity and good activity, free from animal derived viruses.