Enzymes from the Haloacid Dehalogenase (HAD) Superfamily Catalyse the Elusive Dephosphorylation Step of Riboflavin Biosynthesis. Issue 17 (7th October 2013)

• Record Type: Journal Article
• Authors: Haase, Ilka; Sarge, Sonja; Illarionov, Boris; Laudert, Dietmar; Hohmann, Hans‐Peter; Bacher, Adelbert; Fischer, Markus
• Is Part Of: Chembiochem. Volume 14:Issue 17(2013)
• Page Start: 2272
• Page End: 2275
• Publication Date: 2013-10-07
• Subjects: Biochemistry -- Periodicals; Molecular biology -- Periodicals; Pharmaceutical chemistry -- Periodicals; 572
• DOI: 10.1002/cbic.201300544
• Languages: English
• ISSNs: 1439-4227

Abstract

<abstract abstract-type="graphical" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p> <bold>The missing link:</bold> Studies on the biosynthesis of riboflavin have failed to characterise dephosphorylation of the intermediate 5‐amino‐6‐ribitylamino‐2, 4(1<italic>H</italic>, 3<italic>H</italic>)‐pyrimidinedione 5′‐phosphate. We show that this reaction can be catalysed in <italic>Escherichia coli</italic> by YigB and YbjI and in plant chloroplasts by AtcpFHy1, which are members of the haloacid dehalogenase superfamily.<boxed-text content-type="graphic" position="anchor" orientation="portrait"><graphic position="anchor" mimetype="image" xlink:href="ark:/27927/pgg4t78w348" orientation="portrait" xlink:type="simple" xmlns:xlink="http://www.w3.org/1999/xlink" /></boxed-text></p> </abstract>