Tetrahydroxynaphthalene Reductase: Catalytic Properties of an Enzyme Involved in Reductive Asymmetric Naphthol Dearomatization

In reduced circumstances: Tetrahydroxynaphthalene reductase shows a broad substrate range including alternate phenolic compounds and cyclic ketones. Structural modeling reveals major enzyme–substrate interactions; C‐terminal truncation of the enzyme causes an altered substrate preference, in accorda...

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Veröffentlicht in:Angewandte Chemie International Edition 2012-03, Vol.51 (11), p.2643-2646
Hauptverfasser: Schätzle, Michael A., Flemming, Stephan, Husain, Syed Masood, Richter, Michael, Günther, Stefan, Müller, Michael
Format: Artikel
Sprache:eng
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Zusammenfassung:In reduced circumstances: Tetrahydroxynaphthalene reductase shows a broad substrate range including alternate phenolic compounds and cyclic ketones. Structural modeling reveals major enzyme–substrate interactions; C‐terminal truncation of the enzyme causes an altered substrate preference, in accordance with stabilization of the substrate by the C‐terminal carboxylate (see picture). This effect allows the identification of a homologous enzyme.
ISSN:1433-7851
1521-3773
DOI:10.1002/anie.201107695