In biochemistry, an oxidase is any kind of enzyme that brings about an oxidation-reduction reaction involving the oxygen molecule as the electron receptor. There are many kinds of oxidases, including the cytochrome c oxidase, an essential enzyme that allows a living body to use oxygen in the generation of energy. The cytochrome c oxidase is also the final component of the electron transfer chain.
The glucose oxidase is an oxido-reductase enzyme that brings about the oxidation of glucose to hydrogen peroxide and glucono delta-lactone. In living cells, glucose oxidase helps in breaking sugar molecules down into its metabolites. This enzyme is widely used for determining the free glucose in body fluids, as well as in the food industry. Glucose oxidase is also an important substance in various fields of biotechnologies, biochemistry, and even nanotechnologies.
Monoamine oxidases, on the other hand, are a family of enzymes that bring about the oxidation of monoamines. They are typically bound to the outer memberane of mitochondria in just about any cell type in the body. This enzyme was discovered by the British biochemist Mary Bernheim in the liver and she named it tyramine oxidase.
Xanthine oxidase is basically a form of xanthine oxidoreductase, an enzyme that produces reactive oxygen species. It brings about the oxidation of hypoxanthine into xanthine, and pushes the catalyzing process further into oxidizing xanthine to uric acid. Xanthine oxidase has an essential role in the catabolism of purines in many species, including humans.
In the study of microbiogy, oxidases are used in the oxidase test, which is instrumental in the phenotypic characteristic for the identification of a variety of bacterial strains. The oxidase test also determines whether a specific bacterium sample produces cytochrome oxidases, and can therefore use oxygen with an electron transfer chain.
This category contains scientific information on oxidase, any kind of enzyme that brings about an oxidation-reduction reaction with an oxygen molecule as the electron receptor.
Rudel L.L., 1983: Ethanol related changes in liver microsomes and mitochondria from the monkey macaca fascicularis. Alcoholism Clinical & Experimental Research: 424-430 Four M. fascicularis monkeys were maintained 1 yr on a liquid diet containing 26% of calories as ethanol. Four control animals were fed a liquid diet of equivalent calories with protein, carbohydrate and [...]
Redfern B., 1988: Ethanol oxidation by cumene hydroperoxide and hydrogen peroxide supported peroxidatic activities of catalase. Biochemical Archives: 319-328 Ethanol was used as model substrate to compare the H2o2- and cumene hydroperoxide (Chp)-supported peroxidatic reactions of catalase. Our intent was to determine general experimental conditions suitable for the generation of sufficient quantities of reaction products [...]
Elens A., 1985: Ethanol metabolizing system in drosophila melanogaster subcellular distribution of some main enzymes. Experientia (basel): 1543-1546 The subcellular distribution of some enzymes which play a part in ethanol metabolism have been determined by differential centrifugation of homogenates of adult D. melanogaster flies of various genotypes. Aldehyde dehydrogenase, recently discovered in D. melanogaster, is [...]
Ulatowska M.A., 1984: Ethanol involvement in putrescine and histamine oxidation by guinea pig liver. Polish Journal Of Pharmacology & Pharmacy: 633-640 The in vitro influence of ethanol and acetaldehyde on diamine oxidase catalyzed reaction was measured with guinea pig liver and intestine. Acetaldehyde, having no influence on diamine oxidase activity, diminished the formation of Gaba [...]
Hoffman P.L., 1985: Ethanol inhibits the activity of the b form of monoamine oxidase in human platelet and brain tissue. Psychopharmacology: 152-156 Ethanol selectively inhibits the activity of the B-form of monoamine oxidase (Mao) in membranes obtained from human platelet and brain. When endogenous concentrations of phenylethylamine are used as substrate, significant inhibition is induced [...]
Mason M., 1983: Ethanol determination in wine with an immobilized enzyme electrode. American Journal Of Enology & Viticulture: 173-175 The purpose of this work was to demonstrate the accuracy and precision of a new method for ethanol determination. This method utilizes a thin microporous membrane containing immobilized alcohol oxidase (Ec 22.214.171.124) which is mounted on [...]
Ulissey M.J., 1988: Ethanol alters microvasculature enzymes in the rat forebrain. Acta Anatomica: 177-181 Forebrain arterioles were analyzed histochemically to determine the effects of an acute administration of ethanol on key enzymes of aerobic and anaerobic metabolism as well as on the hexose monophosphate shunt in rats. The enzymes were glucose 6-phosphate dehyrogenase, cytochrome oxidase, [...]
Reddy V.V.R., 1982: Estrogen effects on nadh oxidase and super oxide dis mutase in pre pubertal female rats. Steroids: 651-660 Thirty-four day old, ovariectomized rat were treated with increasing doses of estradiol, 2-hydroxyestradiol 2,3-dimethyl ether (23e2), 4-hydroxyestradiol 3,4-dimethyl ether (34e2) and 4-methoxy-estradiol (4me2) for 5 days by s.c. injection. Superoxide dismutase, phenol-activated Nadh oxidase and [...]
Yamaha T., 1981: Estimation of the prosthetic group of cyclo hexylamine oxidase of pseudomonas sp by using vitamin antagonists in the bacterial cultivation. Bulletin Of National Institute Of Hygienic Sciences (tokyo): 03-106 To indirectly estimate the prosthetic group of cyclohexylamine (Cha) oxidase, the inhibitory effects of vitamin antagonists (quinacrine and toxopyrimidine) on the growth of [...]
Patten G.S., 1980: Estimation of phospho fructo kinase activity in homogenates of rat heart using a new isotopic assay at low substrate concentration. Journal Of Molecular & Cellular Cardiology: 1053-1064 A new method is described for the determination of phosphofructokinase activity in crude extracts of heart. The assay does not require the prior removal of [...]