Enzymes from the haloacid dehalogenase (HAD) superfamily catalyse the elusive dephosphorylation step of riboflavin biosynthesis

Chembiochem. 2013 Nov 25;14(17):2272-5. doi: 10.1002/cbic.201300544. Epub 2013 Oct 7.


The missing link: Studies on the biosynthesis of riboflavin have failed to characterise dephosphorylation of the intermediate 5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione 5'-phosphate. We show that this reaction can be catalysed in Escherichia coli by YigB and YbjI and in plant chloroplasts by AtcpFHy1, which are members of the haloacid dehalogenase superfamily.

Keywords: biosynthesis; haloacid dehalogenase; hydrolases; isoenzymes; vitamin B2.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Biocatalysis*
  • Escherichia coli / enzymology
  • Hydrolases / metabolism*
  • Molecular Conformation
  • Phosphorylation
  • Riboflavin / biosynthesis*
  • Riboflavin / chemistry


  • Hydrolases
  • 2-haloacid dehalogenase
  • Riboflavin