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 |
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Hauptverfasser: | , , , , , |
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. |
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ISSN: | 1433-7851 1521-3773 |
DOI: | 10.1002/anie.201107695 |