Flavoenzymes: diverse catalysts with recurrent features

MW Fraaije*, A Mattevi

*Corresponding author for this work

Research output: Contribution to journalReview articlepeer-review

376 Citations (Scopus)
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Abstract

Many biochemical processes exploit the extraordinary versatility of flavoenzymes and their flavin cofactors, Flavoproteins are now known to have a variety of folding topologies but a careful examination of their structures suggests that there are recurrent features in their catalytic apparatus. The flavoenzymes that catalyse dehydrogenation reactions share a few invariant features in the hydrogen-bond interactions between their protein and flavin constituents. Similarly, the positioning of the reactive part of the substrate with respect to the cofactor is generally conserved. Modulation of substrate and cofactor reactivity and exact positioning of the substrate are key elements in the mode of action of these enzymes.

Original languageEnglish
Pages (from-to)126-132
Number of pages7
JournalTrends in Biochemical Sciences
Volume25
Issue number3
DOIs
Publication statusPublished - Mar-2000

Keywords

  • AMINO-ACID OXIDASE
  • DIHYDROOROTATE DEHYDROGENASE-A
  • ACYL-COA DEHYDROGENASES
  • OLD YELLOW ENZYME
  • CRYSTAL-STRUCTURE
  • ACTIVE-SITE
  • LACTOCOCCUS-LACTIS
  • WILD-TYPE
  • TRIMETHYLAMINE DEHYDROGENASE
  • FLAVOPROTEIN STRUCTURE

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