1374429-01-2Relevant academic research and scientific papers
Tetrahydroxynaphthalene reductase: Catalytic properties of an enzyme involved in reductive asymmetric naphthol dearomatization
Schaetzle, Michael A.,Flemming, Stephan,Husain, Syed Masood,Richter, Michael,Guenther, Stefan,Mueller, Michael
supporting information; experimental part, p. 2643 - 2646 (2012/05/04)
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. Copyright
