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.
Thompson S.N., 1980: Preliminary characterization of phenyl oxidase activity in the salivary secretion of the parasite exeristes roborator. Journal Of Insect Physiology: 505-510 Melanization of artificial media which was due to phenyloxidase activity secreted by the developing larvae into the diet accompanied feeding by the parasite E. roborator. The enzyme was localized in the salivary [...]
Hanly E.W., 1980: Preliminary characterization and physical properties of pyridoxal oxidase activity from drosophila melanogaster. Molecular & General Genetics: 455-462 A method of extracting pyridoxal oxidase (Po) activity from D. melanogaster adults is described. In crude extracts, this method allows the activity to remain stable for an extended period of time so that subsequent work [...]
Rivett A.J., 1985: Preferential degradation of the oxidatively modified form of glutamine synthetase by intracellular mammalian proteases. Journal Of Biological Chemistry: 300-305 Four intracellular proteases partially purified from liver preferentially degraded the oxidatively modified (catalytically inactive) form of glutamine synthetase. One of the proteases was cathepsin D which is of lysosomal origin; the other 3 [...]
Fowler, C. J., 1980: Potentiation of the inhibition of rat liver mono amine oxidase a ec 18.104.22.168 by clorgyline after pre treatment with skf 525 a proadifen hydro chloride. Medical Biology (Helsinki) 58(5): 285-287 Pretreatment of rat liver homogenates with 1.5.times. 10-4 M Skf 545a is without effect on the activity of monoamine oxidase-A (Ec [...]
Heineman W.R., 1982: Potential dependent enzymatic activity in an enzyme thin layer cell. Analytical Chemistry: 1377-1383 An enzyme thin-layer electrochemical cell is described and characterized by using galactose oxidase. This cell incorporates 2 working electrodes: a Pt electrode for the amperometric determination of H2o2 and a Au working electrode for the simultaneous control of solution [...]
Harik S.I., 1988: Potent neurotoxic fluorinated 1 methyl 4 phenyl 1 2 3 6 tetrahydropyridine analogs as potential probes in models of parkinson disease. Journal Of Neurochemistry: 1319-1321 We synthesized a number of fluorinated analogs of 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (Mptp), and tested their suitability as substrates for monoamine oxidase B in vitro and their dopaminergic neurotoxicity in [...]
Kappas A., 1981: Potent heme degrading action of antimony and antimony containing parasiticidal agents. Journal Of Experimental Medicine: 245-256 The ability of Sb and Sb containing parasiticidal agents to enhance the heme degradation rate in liver and kidney was investigated. Trivalent Sb was an extremely potent heme oxygenase inducer, the initial and rate-limiting enzyme in [...]
Yamakado M., 1985: Postnatal development of barreloid neuropils in the ventrobasal complex of mouse thalamus a histochemical study for cytochrome oxidase. Brain & Nerve (tokyo): 497-506 Postnatal development of barreloid neuropils were studied in the ventrobasal complex of mouse thalamus. A single-barreloid neuropil which topographically represented a corresponding facial vibrissa on the contralateral side was [...]
Mazzacca G., 1987: Postheparin plasma diamine oxidase in subjects with small bowel mucosal atrophy. Digestive Diseases & Sciences: 313-317 Diamine oxidase (Dao) is an enzyme whose low plasma values are enhanced by an intravenous injection of heparin, which releases the enzyme from the enterocytes of the villous tips. In 20 normal controls and 15 untreated [...]