dehydrogenase


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dehydrogenase

 [de-hi´dro-jen-ās″]
an enzyme that mobilizes the hydrogen of a substrate so that it can pass to a hydrogen acceptor.
glucose-6-phosphate dehydrogenase an enzyme necessary for the oxidation of glucose-6-phosphate, an intermediate in carbohydrate metabolism. Hereditary deficiency of this enzyme in the erythrocytes is associated with a tendency toward hemolysis upon ingestion of certain antimalarial agents and sulfonamide drugs and fava beans (see favism.
lactate dehydrogenase (LDH) an enzyme that catalyzes the interconversion of lactate and pyruvate. It is widespread in tissues and is particularly abundant in kidney, skeletal muscle, liver, and myocardium. It appears in elevated concentrations when these tissues are injured.

de·hy·dro·gen·ase

(dē-hī'drō-jen-ās),
Class name for those enzymes that oxidize substrates by catalyzing removal of hydrogen from metabolites (hydrogen donors) and transferring it to other substances (hydrogen acceptors), which are thus reduced; most of the oxidative enzymes (oxidoreductases, EC class 1) perform their oxidations in this manner.

dehydrogenase

/de·hy·dro·gen·ase/ (de-hi´dro-jen-ās″) an enzyme that catalyzes the transfer of hydrogen or electrons from a donor, oxidizing it, to an acceptor, reducing it.

dehydrogenase

(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.

de·hy·dro·gen·ase

(dēhī-drojĕ-nās)
Class name for those enzymes that oxidize substrates by catalyzing removal of hydrogen from metabolites (hydrogen donors) and transferring it to other substances (hydrogen acceptors).

dehydrogenase

an enzyme, such as any of the respiratory enzymes, that catalyses a reaction in which hydrogen is removed from a molecule (often to be taken up by the ELECTRON TRANSPORT SYSTEM). For example, in the KREBS CYCLE the conversion of succinic acid (succinate) to fumaric acid (fumarate) is catalysed by succinate dehydrogenase, the hydrogen released being passed on to FAD.

de·hy·dro·gen·ase

(dēhī-drojĕ-nās)
Class name for those enzymes that oxidize substrates by catalyzing removal of hydrogen from metabolites (hydrogen donors) and transferring it to other substances (hydrogen acceptors).

dehydrogenase

(dē´hīdroj´ənās´),
n an oxidoreductase class (EC 1) enzyme that induces the transportation of electrons or hydrogen from a donor, which usually indicates the dehydrogenase, to an acceptor compound.

dehydrogenase

an enzyme that mobilizes the hydrogen of a substrate so that it can pass to a hydrogen acceptor, such as NAD+ or FAD+.

alcohol dehydrogenase
dimeric enzyme protein of the liver catalyzing the NAD+-linked dehydrogenation of ethanol to acetaldehyde.
glucose-6-phosphate dehydrogenase
see glucose-6-phosphate dehydrogenase.
glutamate dehydrogenase (GD), glutamic dehydrogenase
an enzyme that catalyzes the reversible reaction of glutamic acid into 2-oxoglutaric acid and ammonia. High concentrations occur in the liver of sheep, cattle, horses and dogs. Serum levels are useful in detecting hepatocellular damage in ruminants.
l-iditol dehydrogenase (ID)
a liver specific enzyme; serum determinations have been used in the horse to detect hepatocellular damage. Called also sorbitol dehydrogenase, SDH.
isocitrate dehydrogenase (ICD)
an enzyme found in high concentrations in many tissues. Two major forms of the enzyme, an NAD+-dependent ICD associated with the mitochondrial TCA cycle and a NADP+-dependent ICD associated with fat synthesis in adipose tissue and lactating mammary gland of ruminants or with steroidogenesis in endocrine tissues. Serum levels have been used to detect hepatocellular damage, but it is not highly specific.
lactate dehydrogenase (LDH), lactic acid dehydrogenase
an enzyme that catalyzes the interconversion of lactate and pyruvate. It is widespread in tissues and is particularly abundant in kidney, skeletal muscle, liver and myocardium. It appears in elevated concentrations when these tissues are injured. See also mouse lactic dehydrogenase elevating virus.
lactate dehydrogenase agent
polyol dehydrogenase
sorbitol dehydrogenase (SDH)
References in periodicals archive ?
Purification of human verylong-chainacyl-coenzyme A dehydrogenase and characterization of its deficiency in seven patients.
Measurement of 6-phosphogluconate dehydrogenase (6PGD) activity: The enzymatic activity of 6PGD was measured by Beutler's method.
Glucose-6-phosphate dehydrogenase deficiency and related disorders of hexose monophosphate shunt and glutathione metabolism.
Normalized lactate dehydrogenase results for HAEC female treated with antioxidants also resulted in significant differences.
Association of degree and type of edema in posterior reversible encephalopathy syndrome with serum lactate dehydrogenase level: initial experience.
Frequency of glucose-6-phosphate dehydrogenase deficiency in some ethnic groups of Pakistan.
iii) related enzymes may exhibit SI in some conditions, as is the case glutamate dehydrogenase [4].
The product of the ubiquitously expressed ADH5 gene is the glutathione-dependent formaldehyde dehydrogenase (also known as nitrosoglutathione reductase [GSNOR]).
Inactivating these two genes blocked the formation of the formate dehydrogenase enzyme, but when the bacteria were supplemented with extra selenium, they were able to synthesize the enzyme again, suggesting that the two Campylobacter genes are involved in selenium metabolism.
Aspartate aminotransferase, calcium, creatine kinase, lactate dehydrogenase, total protein, triglycerides, and uric acid in plasma were determined by a commercial laboratory (Vet Pro Labs, Tulsa, Oklahoma).
Citation: "Mechanisms of Action of Human Aldehyde Dehydrogenase Bright Cells in Therapy of Cardiovascular Diseases: Expression Analysis of Angiogenic Factors and Aldehyde Dehydrogenase Isozymes;" Hannah Storrie White et al.
Background Leakage of lactate dehydrogenase hormone from malignant tumors cells has been described.