Dehydrogenase, which is also known as “DHO” in scientific literature, is basically an enzyme that promotes oxidization in a substrate. This substance oxidises the substrate through a distinct reduction reaction that will transfer one or more hydrides of the substrate to an electron receptor, typically nicotinamide adenine dinucleotide (NAD+) or nicotinamide adenine dinucleotide phosphate (NADP+). The substrate oxidization can also occur in a flavin coenzyme such as flavin adenine dinucleotide (FAD) and flavin mononucleotide.
There are many different kinds of dehydrogenase, including glutamate dehydrogenase, which is an enzyme that can convert glutamate to an α-ketoglutarate and vice versa; pyruvate dehydrogenase, an enzyme that serves an important purose in the tricarboxylic acid cycle by converting pyruvate to acetyl coenzyme A; glucose-6-phosphate dehydrogenase, which is involved in the pentose phosphate pathway; and glyceraldehyde-3-phosphate dehydrogenase, which plays an important role in glycolysis.
The tricarboxylic acid cycle (or TCA cycle)—the series of chemical reactions used by aerobic organisms to generate energy from carbohydrates, fats, and proteins—also uses dehydrogenase for oxidization. The TCA cycle uses isocitrate dehydrogenase (also known as IDH, which catalyzes the third step of the process), oxoglutarate dehydrogenase complex (or α-ketoglutarate dehydrogenase complex), succinate dehydrogenase (or succinate-coenzyme Q reductase, which is found in the inner mitochondrial membrane of many bacterian cells and mammalian mitochondria), and malate dehydrogenase (also known as MDH, which is an enzyme that reverse catalyzes the oxidationof the substance malate to oxaloacetate—a reaction that is part of many metabolic pathways other than the citric acid cycle).
Other types of dehydrogenase include aldehyde dehydrogenase, acetaldehyde dehydrogenase, alcohol dehydrogenase, lactate dehydrogenase, sorbitol dehydrogenase, I-iditol dehydrogenase (ID), isocitrate dehydrogenase (ICD), and polyol dehydrogenase.
This category contains scientific information on dehydrogenase, an enzyme that catalyzes the removal and eventual transfer of hydrogen molecules from a substrate in an oxidation and reduction reaction.
Wong, K; Gill, Ta, 1987: Enzymatic determination of trimethylamine and its relationship to fish quality. Journal of food science 52(1): 1-3 A new enzymatic assay procedure based on a dehydrogenase isolated from Hyphomicrobium X gave results that correlated well with 2 other methods (the picric method and a high-performance liquid chromatographic method) for the analysis [...]
Kato, T.; Suzuki, Y., 1982: Enzymatic determination of galactosyl ceramide galactosidase ec 126.96.36.199 in tissues by nad cycling. Analytical Biochemistry 126(1): 44-51 An enzymatic determination method for galactosylceramide galactosidase was devised by using an enzymatic amplification reaction, Nad cycling. Galactose released by crude enzyme samples (tissue homogenates and cell suspensions) from galactosylceramide quantitatively reduced Nad [...]
Pons A., 1987: Enzymatic determination of carbon 14 labeled l alanine in biological samples. Analytical Chemistry: 1841-1843 A method for determination of L-alanine-specific radioactivity in biological samples is presented. This method is based on the specific enzymatic transformation of L-alanine to pyruvic acid hydrazone catalyzed by the enzyme L-alanine dehydrogenase, formation of the pyruvic acid [...]
Cabezas J.A., 1980: Enzymatic characterization of sarcolemmal membranes from the marine crab carcinus maenas. International Journal Of Biochemistry: 511-514 A plasma membrane enriched preparation was obtained from skeletal muscle of the marine crab C. maenas L. Plasma membranes were isolated by muscle homogenization, removing actomysin by inorganic salt solutions (0.2 M LiBr), differential centrifugation and [...]
Jouve De Guibert C., 1981: Enzymatic changes in rat thymus after intra peritoneal injections of acth and cortico sterone. Thymus: 299-304 I. in adult male rats with Acth (0.6 mU daily for 3 days) brought about a marked decrease in the activities of 4 thymic enzymes studied: glutamic pyruvic transaminase, glutamic oxaloacetic transaminase, isocitric dehydrogenase [...]
Jain N.C., 1982: Enzymatic changes in lamb kidney cell culture infected with bovine enterovirus and equine herpesvirus type 1. Indian Journal Of Animal Sciences: 177-181 Activities of alkaline phosphatase, glutamate oxaloacetate transaminase (Got) and lactate dehydrogenase (Ldh) were followed in lamb kidney cell culture (Lkcc) infected with equine herpesvirus type-1 (Ehv-1) and bovine enterovirus. Ehv-1 [...]
Brun W.A., 1980: Enzymatic changes during the senescence of field grown wheat triticum aestivum. Crop Science: 15-18 Senescence in the canopy of 2 field-grown hard red spring wheats (T. aestivum L. em Thell ‘Era’ and ‘Kitt’) was evaluated during the post-anthesis period. The upper 3 leaf blades and flag leaf sheath were measured for total [...]
Dahl, K. H.; Mckinley-Mckee, J. S., 1981: Enzymatic catalysis in the affinity labeling of liver alcohol dehydrogenase ec 188.8.131.52 with halo acids. European Journal of Biochemistry 118(3): 507-514 The inactivation at pH 7.0 of horse liver alcohol dehydrogenase by iodoacetamide and a series of 6 haloacids was studied, and the kinetic constants determined. Enzyme inactivation [...]
Koivula T., 1979: Enzymatic and metabolic modification of hepatic ethanol and acetaldehyde oxidation in the rat by the dietary protein level. Biochemical Pharmacology: 2313-2320 Changes in hepatic enzyme activities and the metabolic effects of acute ethanol administration were studied in rats fed for 5 wk on diets, which were otherwise nutritionally adequate, but contained respectively [...]