Dehydrogenase Rss feed

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.

Preparatory methods for dna hydrolysis cytochemistry immunocytochemistry and ploidy analysis their application to automated and routine diagnostic cytopathology

Watts K.C., 1987: Preparatory methods for dna hydrolysis cytochemistry immunocytochemistry and ploidy analysis their application to automated and routine diagnostic cytopathology. Analytical & Quantitative Cytology & Histology: 218-224 A review is presented of some methods used to prepare cytologic specimens for analytical and/or automated studies, with the steps of the procedures detailed in appendices. The [...]


Preparative scale regiospecific and stereospecific oxidoreduction of cholic acid and dehydrocholic acid catalyzed by hydroxysteroid dehydrogenases

Carrea G., 1986: Preparative scale regiospecific and stereospecific oxidoreduction of cholic acid and dehydrocholic acid catalyzed by hydroxysteroid dehydrogenases. Journal Of Organic Chemistry: 2902-2906 Nad(P)-dependent hydroxysteroid dehydrogenases were used as catalysts for the oxidoreduction of the hydroxyl-keto groups of cholic acid (3.alpha.,7.alpha.,12.alpha.-trihydroxy-5.beta.-cholan-24-oic acid) and dehydrocholic acid (3,7,12-trioxo-5.beta.-cholan-24-oic acid). Cholic acid was regiospecifically oxidized, on a [...]


Preparations of holo dehydrogenases by covalent fixation of nad analogs to alcohol dehydrogenase and lactate dehydrogenase

Schaefer H G., 1983: Preparations of holo dehydrogenases by covalent fixation of nad analogs to alcohol dehydrogenase and lactate dehydrogenase. Bioorganic Chemistry: 45-57 Diazoniumaryl residues which are connected to the adenosine part of the coenzyme Nad react with amino acid residues of dehydrogenases These coenzyme analogs bind to the active site of the enzymes. The [...]


Preparation of optically active 1 2 diols and alpha hydroxy ketones using glycerol dehydrogenase as catalyst limits to enzyme catalyzed synthesis due to noncompetitive and mixed inhibition by product

Whitesides G.M., 1986: Preparation of optically active 1 2 diols and alpha hydroxy ketones using glycerol dehydrogenase as catalyst limits to enzyme catalyzed synthesis due to noncompetitive and mixed inhibition by product. Journal Of Organic Chemistry: 25-36 Glycerol dehydrogenase (Gdh, Ec 1.1.1.6, from Enterobacter aerogenes or Cellulomonas sp.) catalyzes the interconversion of analogues of glycerol [...]


Preparation of nitrogen 15 labeled l alanine by immobilized l alanine dehydrogenase differential incorporation of nitrogen 15 in bacterial proteins

“Barzu O., 1987: Preparation of nitrogen 15 labeled l alanine by immobilized l alanine dehydrogenase differential incorporation of nitrogen 15 in bacterial proteins. Enzyme & Microbial Technology: 663-667 This paper describes a system for continuous synthesis of 15n-labeled L-alanine from lactic acid, 15NH4Cl and Nadh, which uses immobilized alanine dehydrogenase and soluble lactate dehydrogenase as [...]


Preparation of highly purified 3 alpha hydroxy steroid dehydrogenase ec 1.1.1.50 and 3 beta hydroxy steroid dehydrogenase ec 1.1.1.145 from pseudomonas sp

Shikita, M.; Talalay, P., 1979: Preparation of highly purified 3 alpha hydroxy steroid dehydrogenase ec 1.1.1.50 and 3 beta hydroxy steroid dehydrogenase ec 1.1.1.145 from pseudomonas sp. Analytical Biochemistry 95(1): 286-292 A method is described for preparing highly purified 3.alpha.- and 3.beta.-hydroxysteroid dehydrogenases (Ec 1.1.1.50 and Ec 1.1.1.145, respectively), essentially uncontaminated with one another, from [...]


Preparation of a mono clonal antibody to rat liver glucose 6 phosphate dehydrogenase ec 1.1.1.49 and the study of its immuno reactivity with native and inactivated enzyme

Dao, M. L.; Johnson, B. C.; Hartman, P. E., 1982: Preparation of a mono clonal antibody to rat liver glucose 6 phosphate dehydrogenase ec 1.1.1.49 and the study of its immuno reactivity with native and inactivated enzyme. Proceedings of the National Academy of Sciences of the United States of America 79(9): 2860-2864 A monoclonal antibody [...]


Preparation and properties of immobilized arthrobacter simplex by 2 13 cells possessing 3 keto steroid delta 1 dehydrogenase activity

Zhong L., 1983: Preparation and properties of immobilized arthrobacter simplex by 2 13 cells possessing 3 keto steroid delta 1 dehydrogenase activity. Weishengwu Xuebao: 128-132 Cells of A. simplex By-2-13 having 3-ketosteroid-.Delta.1-dehydrogenase activity were immobilized in 10% polyacrylamide gel; they retained.apprx. 80% of the original activity. Enzyme activity of immobilized cells could be increased.apprx. 40% [...]


Preoperative ultrasound scanning of the liver in cases of colo rectal cancer a comparative investigation

Kronborg O., 1987: Preoperative ultrasound scanning of the liver in cases of colo rectal cancer a comparative investigation. Ugeskrift For Laeger: 155-156 A prospective comparative study of the diagnostic efficiency of preoperative liver ultrasonography, measurements of liver enzymes and inspection and palpation of the liver for detection of hepatic metastases, was performed in 99 patients [...]


Prenatal diagnosis of medium chain acyl coenzyme a dehydrogenase deficiency

Pollitt R.J., 1987: Prenatal diagnosis of medium chain acyl coenzyme a dehydrogenase deficiency. Prenatal Diagnosis: 135-142 A fatal case of medium-chain acyl-coenzyme A dehydrogenase deficiency is described in a patient who presented with hypoglycaemia and a gross non-ketotic dicarboxylic aciduria. Cultured skin fibroblasts released 14co2 from octanoic acid at half the normal rate. Prenatal diagnosis [...]