Structural Studies on Flavin Reductase PheA2 Reveal Binding of NAD in an Unusual Folded Conformation and Support Novel Mechanism of Action

The catabolism of toxic phenols in the thermophilic organism Bacillus thermoglucosidasius A7 is initiated by a two-component enzyme system. The smaller flavin reductase PheA2 component catalyzes the NADH-dependent reduction of free FAD according to a ping-pong bisubstrate-biproduct mechanism. The reduced FAD is then used by the larger oxygenase component PheA1 to hydroxylate phenols to the corresponding catechols. We have determined the x-ray structure of PheA2 containing a bound FAD cofactor (2.2 Angstrom), which is the first structure of a member of this flavin reductase family. We have also... Mehr ...

Verfasser: Albert J. R. Heck
Adrie H. Westphal
Robert H. H. van den Heuvel
Andrea Mattevi
Martin A. Walsh
Willem J. H. van Berkel
Stefano Rovida
Dokumenttyp: Artikel
Erscheinungsdatum: 2004
Schlagwörter: Netherlands / Cell Biology / Molecular Biology / Biochemistry
Sprache: Englisch
Permalink: https://search.fid-benelux.de/Record/base-26811808
Datenquelle: BASE; Originalkatalog
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Link(s) : https://www.openaccessrepository.it/record/95179