Catalytic properties of Gibberella galactose oxidase.
نویسندگان
چکیده
منابع مشابه
Structure–function characterization reveals new catalytic diversity in the galactose oxidase and glyoxal oxidase family
Alcohol oxidases, including carbohydrate oxidases, have a long history of research that has generated fundamental biological understanding and biotechnological applications. Despite a long history of study, the galactose 6-oxidase/glyoxal oxidase family of mononuclear copper-radical oxidases, Auxiliary Activity Family 5 (AA5), is currently represented by only very few characterized members. Her...
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We have investigated a series of single and double mutants and a triple mutant comprising V494A, C383S and Y436H identified by directed evolution. The locations of the mutated residues are shown in Fig. 1. The most interesting effect is due to the C383S mutation that leads to a significant reduction in KM. Cys 383 lies in a pocket at the back of the active site behind the copper atom and theref...
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The estimation of galactose in plasma by the enzyme system galactose oxidaseperoxidase was investigated. The method was found to be relatively specific for galactose although xylose and ascorbic acid reacted to a slight degree with the enzyme; lactose also reacted with the enzyme, probably because partial hydrolysis of the disaccharide released galactose. The relationship between absorbance and...
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GO (galactose oxidase; E.C. 1.1.3.9) is a monomeric 68 kDa enzyme that contains a single copper ion and an amino acid-derived cofactor. The enzyme is produced by the filamentous fungus Fusarium graminearum as an extracellular enzyme. The enzyme has been extensively studied by structural, spectroscopic, kinetic and mutational approaches that have provided insight into the catalytic mechanism of ...
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The spectral and catalytic properties of the copper cofactor in highly purified bovine aortic lysyl oxidase have been examined. As isolated, various preparations of purified lysyl oxidase are associated with 5-9 loosely bound copper atoms per molecule of enzyme which are removed by dialysis against EDTA. The enzyme also contains 0.99 +/- 0.10 g atom of tightly bound copper per 32-kDa monomer wh...
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ژورنال
عنوان ژورنال: Agricultural and Biological Chemistry
سال: 1985
ISSN: 0002-1369,1881-1280
DOI: 10.1271/bbb1961.49.1201