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

Ilka Haase; Sonja Sarge; Boris Illarionov; Dietmar Laudert; Hans-Peter Hohmann; Adelbert Bacher; Markus Fischer

doi:10.1002/cbic.201300544

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.

Authors

Ilka Haase¹, Sonja Sarge, Boris Illarionov, Dietmar Laudert, Hans-Peter Hohmann, Adelbert Bacher, Markus Fischer

Affiliation

¹ Hamburg School of Food Science, Institute of Food Chemistry, University of Hamburg, Grindelallee 117, 20146 Hamburg (Germany), Homepage: www.hsfs.org.

PMID: 24123841
DOI: 10.1002/cbic.201300544

Abstract

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

Substances

Hydrolases
2-haloacid dehalogenase
Riboflavin