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.
Anon, 1988: Preliminary evaluation of cocarboxylase in protecting the ischemic myocardium. Compendium De Investigaciones Clinicas Latinoamericanas: 74-80 Cocarboxylase (Cc), also known as thiamin pyrophosphate, is an important coenzyme for pyruvate dehydrogenase. Pyruvate dehydrogenase is the regulating enzyme for pyruvate catabolism and a possible key enzyme involving recovery of the ischemic myocardium. A stable solution of [...]
Zou C., 1988: Preliminary crystallographic studies on the coenzyme binding to glyceraldehyde 3 phosphate dehydrogenase from palinurus versicolor. Scientia Sinica Series B (chemical Biological Agricultural Medical & Earth Sciences): 313-318 The three forms of glyceraldehyde-3-phosphate dehydrogenase from Palinurus versicolor muscle, namely apo native enzyme, apo carboxymethylated enzyme and the enzyme carrying two fluorescent Nad derivatives [...]
Hsueh A.J.W., 1982: Pregnenolone biosynthesis by cultured rat granulosa cells modulation by fsh and gonadotropin releasing hormone. Endocrinology: 713-721 The mechanism by which GnRH inhibits ovarian progesterone production was investigated by studying the GnRH modulation of prenenolone biosynthesis in cultured rat granulosa cells. Granulosa cells from hypophysectomized, estrogen-treated rats were incubated for 2 days with [...]
Warburton D., 1986: Preferential x chromosome activity in human female placental tissues. Cytogenetics & Cell Genetics: 163-168 Preferential inactivation of the paternally derived X chromosome in extraembryonic membranes of female rodents has been clearly demonstrated, but the mode of X-chromosome inactivation in the human placenta has not been so clearly defined. We examined A and [...]
Patel M.S., 1986: Precocious induction of hepatic glucokinase and malic enzyme in artificially reared rat pups fed a high carbohydrate diet. Archives Of Biochemistry & Biophysics: 787-794 Glucokinase and NADP:malate dehydrogenase (malic enzyme) first appear in liver when rat pups are weaned from milk which is high fat to lab chow which is high in [...]
Torok K., 1980: Preclinical diagnosis and carrier detection in ataxia associated with abnormalities of lipo amide dehydrogenase. Neurology: 502-508 Whether kinetic assays of lipomide dehydrogenase are valuable for carrier detection or preclinical diagnosis, KmL and KmH for the enzyme were determined in platelets from families with a form of recessive Friedreich ataxia and low activities [...]
Fahien, L. A.; Kmiotek, E., 1979: Precipitation of complexes between glutamate dehydrogenase ec 220.127.116.11 and mitochondrial enzymes. Journal of Biological Chemistry 254(13): 5983-5990 When glutamate dehydrogenase Ec 1.4.13 is incubated in polyethylene glycol with mitochondrial aspartate aminotransferase (Ec 18.104.22.168.) or malate dehydrogenase, a considerable fraction of both enzymes is precipitated. If any one of these [...]
Liu, C. C.; Weaver, J. P.; Chen, A. K., 1981: Potentiometric measurement of glucose concentration using a gel immobilized glucose dehydrogenase ec 22.214.171.124 electrode. Bioelectrochemistry and Bioenergetics 8(4): 379-386 Glucose dehydrogenase, a coenzyme-dependent oxidoreductase, was immobilized by a polyacrylamide gel matrix over the surface of a plantinum screen to measure the glucose concentration in 0.1 [...]
Kamo N., 1979: Potentiometric enzyme electrode for lactate. Analytical Chemistry: 100-104 A potentiometric enzyme electrode for lactate is developed. The enzyme electrode is constructed by coating the sensor membrane of the redox electrode with a film of enzyme-gelatin gel layer. The enzyme used lactate dehydrogenase (Ec 126.96.36.199.) which catalyzes the oxidation of lactate by ferricyanide. [...]
Mcdonald J.F., 1987: Post translational control of alcohol dehydrogenase levels in drosophila melanogaster. Genetics: 693-700 A trans-acting regulatory gene that alters in vivo protein levels of alcohol dehydrogenase (Adh) has been mapped to a region of the third chromosome of Drosophila melanogaster. The gene has been found to affect the in vivo stability of Adh [...]