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.
Shinde L.S., 1983: Photosynthetic products and enzymes in a mangrove aegiceras corniculatum and a halophyte sesuvium portulacastrum. Photosynthetica (prague): 59-63 A. corniculatum (L.) Blanco and S. portulacastrum L. synthesize aspartate and alanine as major products of short-time photosynthesis. In these plants the activity of phosphoenol pyruvate carboxylase Ec 220.127.116.11 was much higher than that of [...]
Feuillade, J.; Feuillade, M.; Jolivet, E., 1982: Photosynthetic metabolism in the cyanophyte oscillatoria rubescens carbon metabolism under nitrogen starvation. Archives of Microbiology 131(2): 107-111 Short term 14c labeling experiments and enzymatic activities related to primary pathways of photosynthesis were studied in the cyanophyte O. rubescens D.C. from axenic cyclostat cultures. Responses of samples from cultures [...]
Bauwe H., 1984: Photosynthetic enzyme activities and immuno fluorescence studies on the localization of ribulose 1 5 bis phosphate carboxylase oxygenase in leaves of 3 carbon pathway 4 carbon pathway and 3 carbon 4 carbon pathway intermediate species of flaveria asteraceae. Biochemie Und Physiologie Der Pflanzen (bpp): 253-268 Activities of ribulose-1,5-bisphosphate carboxylase (rubisco), phosphoenolpyruvate carboxylase [...]
Ku, M. S. B.; Monson, R. K.; Littlejohn, R. O. Jr ; Nakamoto, H.; Fisher, D. B.; Edwards, G. E., 1983: Photosynthetic characteristics of 3 carbon 4 carbon pathway intermediates flaveria spp leaf anatomy photosynthetic responses to oxygen and carbon di oxide and activities of key enzymes in the 3 carbon and 4 carbon pathways. [...]
Bhosale L.J., 1985: Photosynthesis in avicennia and thespesia. Indian Botanical Reporter: 46-49 Photosynthetic studies in the mangroves Avicennia officinalis Linn. and A. marina var. acutissima Stapf and Moldenke, as well as in saline and nonsaline Thespesia populnea Soland. an associated mangrove, were carried out. It is observed that aspartate and alanine aquire heavy label during [...]
Robenek H., 1984: Photosynthesis and carbon metabolism in photoautotrophic cell suspensions of chenopodium rubrum from different phases of batch growth. Physiologia Plantarum: 349-355 Rapidly dividing photoautotrophic cell suspensions from C. rubrum L. assimilated.apprx. 85.mu.mol Co2 (mg chlorophyll)-1 h- During the late stationary phase of culture growth, Co2 fixation rate was reduced to.apprx. 60.mu.mol Co2 (mg [...]
Luening K., 1981: Photoperiod affects enzyme activities in the kelp laminaria hyperborea. Zeitschrift Fuer Pflanzenphysiologie: 81-84 Activities of ribulose-1,5-bisphosphate carboxylase, phosphoenolpyruvate carboxykinase, malate dehydrogenase and mannitol-1-phosphate dehydrogenase were compared in plants from short day conditions, inductive of new blade formation, and from short-day-plus-light-break regime, which prevents new blade formation. All 4 enzymes were more active [...]
Inano, H.; Ohba, H.; Tamaoki, B. I., 1983: Photochemical inactivation of human placental estradiol 17 beta dehydrogenase ec 18.104.22.168 in the presence of 2 3 butanedione. Journal of Steroid Biochemistry 19(5): 1617-1622 Estradiol 17.beta.-dehydrogenase of human placenta was rapidly inactivated by 2,3-butanedione under Uv light, and no protection against the inactivation was observed in the [...]
Earley, F. G. P.; Ragan, C. I., 1984: Photoaffinity labeling of mitochondrial nadh dehydrogenase ec 22.214.171.124 with arylazidoamorphigenin an analog of rotenone. Biochemical Journal 224(2): 525-534 A photoaffinity-labeling analog of the respiratory inhibitor rotenone was synthesized from the naturally occurring rotenoid amorphigenin. The analog inhibits Nadh-ubiquinone oxidoreductase activity at concentrations comparable with those of rotenone. [...]
Hatefi Y., 1985: Photoaffinity labeling of d levo beta hydroxybutyrate dehydrogenase by arylazido beta alanyl substituted nad. Biochemistry: 4912-4916 (Arylazido)-.beta.-alanyl-substituted nicotinamide adenine dinucleotide (N3-Nad) is a photosensitive analogue of Nad capable of photoinduced nitrene generation and insertion into a nearby molecule. In the dark, N3-Nad can replace Nad as a cosubstrate for the mitochondrial D-(.sbd.)-.beta.-hydroxybutyrate [...]