18512-30-6Relevant articles and documents
Identification and characterization of an anthrol reductase from: Talaromyces islandicus (Penicillium islandicum) WF-38-12
Singh, Shailesh Kumar,Mondal, Amit,Saha, Nirmal,Husain, Syed Masood
supporting information, p. 6594 - 6599 (2019/12/26)
An NADPH-dependent oxidoreductase from Talaromyces islandicus WF-38-12 has been identified through genome analysis. It has been shown to catalyze a regio- and stereoselective reduction of anthrols (formed in situ by the reduction of anthraquinones in the presence of Na2S2O4) to (R)-dihydroanthracenones, with high enantiomeric excess (>99%). The implications of results on the biosynthesis of deoxygenated (bis)anthraquinones and modified (bis)anthraquinones are discussed.
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
Enantioselective total synthesis of (-)-napyradiomycin A1 via asymmetricchlorination of an isolated olefin
Snyder, Scott A.,Tang, Zhen-Yu,Gupta, Ritu
supporting information; experimental part, p. 5744 - 5745 (2009/09/25)
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