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.
Nalecz, K. A.; Bolli, R.; Azzi, A., 1983: Preparation of monomeric cytochrome c oxidase ec 184.108.40.206 its kinetics differ from those of the dimeric enzyme. Biochemical and Biophysical Research Communications 114(2): 822-828 Bovine cytochrome c oxidase in 0.1% dodecylmaltoside, 50 mM KCl and 10 mM Tris-HCl, pH 7.4 is monodisperse with an apparent Mw 360,000 [...]
Zenk M.H., 1987: Preparation of dehydrobenzylisoquinolines by immobilized s tetrahydroprotoberberine oxidase from plant cell cultures. Phytochemistry (oxford): 3235-3240 (S)-Tetrahydroprotoberberine oxidase (Stox) has been isolated in enriched (7.4-fold) form from a high yielding cell suspension of Berberis wilsoniae var. subcaulialata in a three step procedure and was immobilized by several different methods. The properties of immobilized [...]
Henderson R., 1982: Preparation of 2 dimensional arrays from purified beef heart cytochrome c oxidase. Biochemistry: 2525-2529 A method for preparing 2-dimensional crystals from highly purified beef heart cytochrome c oxidase is described. This involves mixing the enzyme with phosphatidylcholine and then extracting excess lipid with deoxycholate. The reconstituted crystals show P1 symmetry. Alternating rows [...]
Doeppner T., 1983: Preparation and properties of mycelium bound glucose oxidase co immobilized with excess catalase. Biotechnology Letters: 743-748 The mycelium of Aspergillus niger containing glucose oxidase and catalase was permeabilized with an organic solvent and entrapped by a thin layer of excess catalase. The stability of the 2 enzyme system was increased. Some characteristics [...]
Mohr P., 1980: Preparation and properties of immobilized glucose oxidase. Acta Biologica Et Medica Germanica-12: 1121-1128 Glucose oxidase from Penicillium notatum was immobilized by covalent, adsorptive or ion exchange attachment to insoluble carriers. The yields of immobilization using Spherons, Deae-Sephadex, Deae-cellulose and porous glass as carriers are compared. Methods used for the estimation of kinetic [...]
Saleemuddin M., 1983: Preparation and properties of concanavalin a cellulose immobilized glucose oxidase. Indian Journal Of Biochemistry & Biophysics: 33-38 Glucose oxidase was immobilized by covalent attachment to Ae-cellulose and by binding to Con A cellulose. About 9 times more enzyme could be immobilized by binding glucose oxidase to Con A cellulose than by the [...]
Delacour J., 1984: Prenatal ontogenesis of p octopamine m octopamine and phenylethanolamine in relation to catecholamines and their metabolizing enzymes in the developing rat brain and heart. Neuroscience: 1271-1276 Noncatecholamines such as phenylethanolamine and – are present in many invertebrate nervous systems, sometimes in large amounts. These amines are normally present in the rat brain [...]
Tromp A., 1987: Prenatal diagnosis of zellweger syndrome by measurement of very long chain fatty acid 26 carbon atoms o beta oxidation in cultured chorionic villous fibroblasts implications for early diagnosis of other peroxisomal disorders. Clinica Chimica Acta-3: 303-310 In this paper we show that cultured chorionic villous fibroblasts efficiently catalyse the peroxisomal.beta.-oxidation of hexacosanoic [...]
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 [...]