Title of article
The growing VAO flavoprotein family
Author/Authors
F. Leferink، نويسنده , , Nicole G.H. and Heuts، نويسنده , , Dominic P.H.M. and Fraaije، نويسنده , , Marco W. and van Berkel، نويسنده , , Willem J.H.، نويسنده ,
Issue Information
روزنامه با شماره پیاپی سال 2008
Pages
10
From page
292
To page
301
Abstract
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-cysteinyl-8α-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.
Keywords
Chitooligosaccharide oxidase , Covalent flavinylation , Eugenol oxidase , flavoenzyme , l-Galactono-1 , 4-lactone dehydrogenase , Vanillyl-alcohol oxidase , VAO family , Vitamin C , Alditol oxidase
Journal title
Archives of Biochemistry and Biophysics
Serial Year
2008
Journal title
Archives of Biochemistry and Biophysics
Record number
1629490
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