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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.
The domain structure of GLUD1 Each domain is colored differently - Glu-BD, NAD(P)-BD, antenna, the pivot helix.The allosteric regulators are shown as sphere models. This particular structure of GLUD1 is a combination of two X-ray structures - one with a bound GTP and the second one with a bound ADP (1NQT,8AR8).
Glycerol dehydrogenase (EC 1.1.1.6, also known as NAD +-linked glycerol dehydrogenase, glycerol: NAD + 2-oxidoreductase, GDH, GlDH, GlyDH) is an enzyme in the oxidoreductase family that utilizes the NAD + to catalyze the oxidation of glycerol to form glycerone (dihydroxyacetone). [1] [2]
Transamination is mediated by several types of aminotransferase enzymes. An aminotransferase may be specific for an individual amino acid, or it may be able to process any member of a group of similar ones, for example the branched-chain amino acids, which comprises valine, isoleucine, and leucine.
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Berthelot's reagent is an alkaline solution of phenol and hypochlorite, used in analytical chemistry.It is named after its inventor, Marcellin Berthelot.Ammonia reacts with Berthelot's reagent to form a blue product which is used in a colorimetric method for determining ammonia.
Glutaminolysis takes place in all proliferating cells, [3] such as lymphocytes, thymocytes, colonocytes, adipocytes and especially in tumor cells. [1] Glutaminolysis has been targeted for therapeutic purposes. [4]
Reaction catalyzed by lactate dehydrogenase. Lactate dehydrogenase catalyzes the interconversion of pyruvate and lactate with concomitant interconversion of NADH and NAD +.It converts pyruvate, the final product of glycolysis, to lactate when oxygen is absent or in short supply, and it performs the reverse reaction during the Cori cycle in the liver.