Enzymes from the haloacid dehalogenase (HAD) superfamily catalyse the elusive dephosphorylation step of riboflavin biosynthesis.
| Autor: | Haase I; Hamburg School of Food Science, Institute of Food Chemistry, University of Hamburg, Grindelallee 117, 20146 Hamburg (Germany), Homepage: www.hsfs.org., Sarge S, Illarionov B, Laudert D, Hohmann HP, Bacher A, Fischer M |
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| Jazyk: | angličtina |
| Zdroj: | Chembiochem : a European journal of chemical biology [Chembiochem] 2013 Nov 25; Vol. 14 (17), pp. 2272-5. Date of Electronic Publication: 2013 Oct 07. |
| DOI: | 10.1002/cbic.201300544 |
| Abstrakt: | 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. (Copyright © 2013 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.) |
| Databáze: | MEDLINE |
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