Zymography of monophenolase and o-Diphenolase activities of polyphenol oxidase
| Autor: | Colja Laane, Harry Gruppen, Alfons G. J. Voragen, Riet Hilhorst, Willem J. H. van Berkel, Mamoudou H. Dicko |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2002 |
| Předmět: |
Biophysics
chemistry.chemical_element Biochemie Anisoles Oxygen Polyphenol oxidase Biochemistry Caffeic Acids Oxidoreductase Levensmiddelenchemie Life Science Zymography Benzothiazoles Molecular Biology VLAG Laccase chemistry.chemical_classification Oxidase test biology Food Chemistry Chemistry Hydrazones Quinones Cell Biology Monooxygenase Thiazoles Spectrophotometry biology.protein Edible Grain Oxidoreductases Catechol Oxidase Peroxidase |
| Zdroj: | Analytical Biochemistry, 306, 336-339 Analytical Biochemistry 306 (2002) |
| ISSN: | 0003-2697 |
| Popis: | Polyphenol oxidase (PPO) (monophenol, o-diphenol: oxygen oxidoreductase; EC 1.14.18.1) is a binuclear copper-cluster-containing monooxygenase ubiquitously present in biological systems (1, 2). PPO may be distinguished from the related oxidase laccase [p-diphenol:oxygen oxidoreductase; EC 1.10.3.2] by its substrate specificity and the type and number of catalytic coppers. PPO catalyzes the oxidation of o-diphenols (o-diphenolase or catecholase activity) to the corresponding o-quinones, by consumption of molecular oxygen. It may also catalyze the regioselective orthohydroxylation of monophenols to catechols and their subsequent oxidation to o-quinones (monophenolase or cresolase activity). The resulting quinones may undergo nonenzymatic autopolymerization or covalent heterocondensation with proteins to produce colored compounds (1). Peroxidases (POXs) (donor:hydrogen |
| Databáze: | OpenAIRE |
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