title: Enzymes from the haloacid dehalogenase (HAD) superfamily catalyse the elusive dephosphorylation step of riboflavin biosynthesis.
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.
authors.affiliation: Hamburg School of Food Science, Institute of Food Chemistry, University of Hamburg, Grindelallee 117, 20146 Hamburg (Germany), Homepage: www.hsfs.org.
authors.forename: Ilka
authors.initials: I
authors.lastname: Haase
authors.forename: Sonja
authors.initials: S
authors.lastname: Sarge
authors.forename: Boris
authors.initials: B
authors.lastname: Illarionov
authors.forename: Dietmar
authors.initials: D
authors.lastname: Laudert
authors.forename: Hans-Peter
authors.initials: HP
authors.lastname: Hohmann
authors.forename: Adelbert
authors.initials: A
authors.lastname: Bacher
authors.forename: Markus
authors.initials: M
authors.lastname: Fischer
mesh_terms: D055162:Biocatalysis; D004926:Escherichia coli / Q000201:enzymology; D006867:Hydrolases / Q000378:metabolism*; D008968:Molecular Conformation; D010766:Phosphorylation; D012256:Riboflavin / Q000096:biosynthesis* / Q000737:chemistry
chemical_list: D006867:Hydrolases; C034507:2-haloacid dehalogenase; D012256:Riboflavin
keywords: biosynthesis; haloacid dehalogenase; hydrolases; isoenzymes; vitamin B2