Tetrahydroxynaphthalene reductase: catalytic properties of an enzyme involved in reductive asymmetric naphthol dearomatization

Abstract

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. This effect allows the identification of a homologous enzyme.