4.6 Article Proceedings Paper

The growing VAO flavoprotein family

Journal

ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS
Volume 474, Issue 2, Pages 292-301

Publisher

ELSEVIER SCIENCE INC
DOI: 10.1016/j.abb.2008.01.027

Keywords

alditol oxidase; chitooligosaccharide oxidase; covalent flavinylation; eugenol oxidase; flavoenzyme; L-galactono-1,4-lactone dehydrogenase; vanillyl-alcohol oxidase; VAO family; vitamin C

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The VAO flavoprotein family is a rapidly growing family of oxidoreductases that favor the covalent binding of the FAD cofactor. In this review we report on the catalytic properties of some newly discovered VAO family members and their mode of flavin binding. Covalent binding of the flavin is a self-catalytic post-translational modification primarily taking place in oxidases. Covalent flavinylation increases the redox potential of the cofactor and thus its oxidation power. Recent findings have revealed that some members of the VAO family anchor the flavin via a dual covalent linkage (6-S-eysteinyl-8 alpha-N1-histidyl FAD). Some VAO-type aldonolactone oxidoreductases favor the non-covalent binding of the flavin cofactor. These enzymes act as dehydrogenases, using cytochrome c as electron acceptor. (c) 2008 Elsevier Inc. All rights reserved.

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