Covalent flavinylation of vanillyl-alcohol oxidase is an autocatalytic process
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منابع مشابه
Covalent flavinylation of vanillyl-alcohol oxidase is an autocatalytic process.
Vanillyl-alcohol oxidase (VAO; EC 1.1.3.38) contains a covalently 8alpha-histidyl bound FAD, which represents the most frequently encountered covalent flavin-protein linkage. To elucidate the mechanism by which VAO covalently incorporates the FAD cofactor, apo VAO was produced by using a riboflavin auxotrophic Escherichia coli strain. Incubation of apo VAO with FAD resulted in full restoration ...
متن کاملCovalent flavinylation is essential for efficient redox catalysis in vanillyl-alcohol oxidase.
By mutating the target residue of covalent flavinylation in vanillyl-alcohol oxidase, the functional role of the histidyl-FAD bond was studied. Three His(422) mutants (H422A, H422T, and H422C) were purified, which all contained tightly but noncovalently bound FAD. Steady state kinetics revealed that the mutants have retained enzyme activity, although the turnover rates have decreased by 1 order...
متن کاملStructural analysis of flavinylation in vanillyl-alcohol oxidase.
Vanillyl-alcohol oxidase (VAO) is member of a newly recognized flavoprotein family of structurally related oxidoreductases. The enzyme contains a covalently linked FAD cofactor. To study the mechanism of flavinylation we have created a design point mutation (His-61 --> Thr). In the mutant enzyme the covalent His-C8alpha-flavin linkage is not formed, while the enzyme is still able to bind FAD an...
متن کاملCovalent flavinylation is essential for efficient redox catalysis in vanillyl-alcohol
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متن کاملInversion of stereospecificity of vanillyl-alcohol oxidase.
Vanillyl-alcohol oxidase (VAO) is the prototype of a newly recognized family of structurally related oxidoreductases sharing a conserved FAD-binding domain. The active site of VAO is formed by a cavity where the enzyme is able to catalyze many reactions with phenolic substrates. Among these reactions is the stereospecific hydroxylation of 4-ethylphenol-forming (R)-1-(4'-hydroxyphenyl)ethanol. D...
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ژورنال
عنوان ژورنال: FEBS Journal
سال: 2008
ISSN: 1742-464X
DOI: 10.1111/j.1742-4658.2008.06649.x