dehydrogenase


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de·hy·dro·gen·ase

 (dē′hī-drŏj′ə-nās′, -nāz′, dē-hī′drə-jə-)
n.
An enzyme that catalyzes the removal of hydrogen from a substrate and the transfer of the hydrogen to an acceptor in an oxidation-reduction reaction.
American Heritage® Dictionary of the English Language, Fifth Edition. Copyright © 2016 by Houghton Mifflin Harcourt Publishing Company. Published by Houghton Mifflin Harcourt Publishing Company. All rights reserved.

dehydrogenase

(diːˈhaɪdrədʒəˌneɪz)
n
(Biochemistry) an enzyme, such as any of the respiratory enzymes, that activates oxidation-reduction reactions by transferring hydrogen from substrate to acceptor
Collins English Dictionary – Complete and Unabridged, 12th Edition 2014 © HarperCollins Publishers 1991, 1994, 1998, 2000, 2003, 2006, 2007, 2009, 2011, 2014

de•hy•dro•gen•ase

(diˈhaɪ drə dʒəˌneɪs, -ˌneɪz)

n.
an oxidoreductase enzyme that catalyzes the removal of hydrogen.
[1920–25]
Random House Kernerman Webster's College Dictionary, © 2010 K Dictionaries Ltd. Copyright 2005, 1997, 1991 by Random House, Inc. All rights reserved.
References in periodicals archive ?
Succinate dehydrogenase (SDH)-deficient renal cell carcinoma (RCC) is a recently recognized distinct subtype of RCC in the 2016 World Health Organization classification.
Initial laboratory tests showed white blood cell (WBC) count 22.9 x [10.sup.9]/L, red blood cell (RBC) count 2.68 mcL, hemoglobin (Hgb) 7.7 g/dL (normal: 120-160 gm /L, platelet count 545000 (normal: 150-400X10 [conjunction] 9 /L), reticulocyte percentage 18.63 (normal: 0.5-2.5%), lactate dehydrogenase (LDH) 567 U/L (normal: 125-243U/L), and total bilirubin 44.1 (normal: 3.4-20.5 umol/L.
A Newborn Screening Pilot project concluded disorders such as homocysteinemia, hyperglycemia, MSUD, phenylketonuria, hypothyroidism, and glucose-6-phosphate dehydrogenase deficiency were found to be the common errors in the neonates.
Agios Pharmaceuticals announced that the FDA has accepted the company's supplemental new drug application, or sNDA, for Tibsovo for the treatment of patients with newly diagnosed acute myeloid leukemia, or AML, with an isocitrate dehydrogenase 1, or IDH1, mutation who are not eligible for standard therapy.
Lactate Dehydrogenase (LDH) is a tetrameric molecule used to detect cell damage or cell death.
Keywords: Glucose-6-phosphate dehydrogenase, G6PD, Hepatitis E, Haemolysis.
Glucose-6-phosphate dehydrogenase (G6PDH) activity was ordered on a 3-day-old term male neonate.
Glucose-6-phosphate dehydrogenase (G6PD) deficiency is the commonest enzyme deficiency in humans, especially in those of African descent [1], with a prevalence of 400 million affected people worldwide [2].
In the article titled "Kinetic Modeling of the Mitochondrial Energy Metabolism of Neuronal Cells: The Impact of Reduced [alpha]-Ketoglutarate Dehydrogenase Activities on ATP Production and Generation of Reactive Oxygen Species" [1], there was an error in Figure 1, in which the decarboxylation of pyruvate to acetyl-CoA should be accompanied by NAD to NADH, not NADH to NAD.
Isocitrate dehydrogenase (IDH) catalyzes the oxidative decarboxylation of isocitrate to produce [alpha]-ketoglutarate and C[O.sub.2] while reducing the cofactor nicotinamide adenine dinucleotide (phosphate) (NAD(P)+) to NAD(P)H using divalent metal cation (Mg2+ or Mn2+) in the tricarboxylic acid cycle.
Firstly, it is broken down into a chemical called acetaldehyde by an enzyme called alcohol dehydrogenase (ADH).
The analyzed proteins include the complex I or NADH dehydrogenase subunits, the A and B subunits of complex II or succinate dehydrogenase, and various subunits of complex III or cytochrome bcl.