• 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