23255-41-6Relevant academic research and scientific papers
Enediyne polyketide synthases stereoselectively reduce the β-ketoacyl intermediates to β- D -hydroxyacyl intermediates in enediyne core biosynthesis
Ge, Hui-Ming,Huang, Tingting,Rudolf, Jeffrey D.,Lohman, Jeremy R.,Huang, Sheng-Xiong,Guo, Xun,Shen, Ben
supporting information, p. 3958 - 3961 (2014/08/18)
PKSE biosynthesizes an enediyne core precursor from decarboxylative condensation of eight malonyl-CoAs. The KR domain of PKSE is responsible for iterative β-ketoreduction in each round of polyketide chain elongation. KRs from selected PKSEs were investiga
Employing modular polyketide synthase ketoreductases as biocatalysts in the preparative chemoenzymatic syntheses of diketide chiral building blocks
Piasecki, Shawn K.,Taylor, Clint A.,Detelich, Joshua F.,Liu, June,Zheng, Jianting,Komsoukaniants, Arkady,Siegel, Dionicio R.,Keatinge-Clay, Adrian T.
experimental part, p. 1331 - 1340 (2012/02/01)
Chiral building blocks are valuable intermediates in the syntheses of natural products and pharmaceuticals. A scalable chemoenzymatic route to chiral diketides has been developed that includes the general synthesis of α-substituted, β-ketoacyl N-acetylcysteamine thioesters followed by a biocatalytic cycle in which a glucose-fueled NADPH-regeneration system drives reductions catalyzed by isolated modular polyketide synthase (PKS) ketoreductases (KRs). To identify KRs that operate as active, stereospecific biocatalysts, 11 isolated KRs were incubated with 5 diketides and their products were analyzed by chiral chromatography. KRs that naturally reduce small polyketide intermediates were the most active and stereospecific toward the panel of diketides. Several biocatalytic reactions were scaled up to yield more than 100 mg of product. These syntheses demonstrate the ability of PKS enzymes to economically and greenly generate diverse chiral building blocks on a preparative scale.
