The growing VAO flavoprotein family

N.G.H. Leferink, D.P.H.M. Heuts, M.W. Fraaije, W.J.H. van Berkel

Research output: Contribution to journalArticleAcademicpeer-review

85 Citations (Scopus)

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-8alpha-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.
Original languageEnglish
Pages (from-to)292-301
JournalArchives of Biochemistry and Biophysics
Volume474
Issue number2
DOIs
Publication statusPublished - 2008

Keywords

  • gamma-lactone dehydrogenase
  • vanillyl-alcohol oxidase
  • berberine bridge enzyme
  • para-cresol methylhydroxylase
  • covalently-bound flavin
  • vitamin-c biosynthesis
  • hydroxylase genes ehya/ehyb
  • site-directed mutagenesis
  • 6-hydroxy-d-nicotine oxidase
  • ascorbic-

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