%ACha, L.%AMilikisiyants, S.%ADavidson, M.%AXue, S.%ASmirnova, T.%ASmirnov, A.%AGuo, Y.%AChang, W.-c.%ABooker, S Ed.%BJournal Name: Biochemistry; Journal Volume: 59 %D2020%I %JJournal Name: Biochemistry; Journal Volume: 59 %K %MOSTI ID: 10217433 %PMedium: X %TAlternative Reactivity of Leucine 5-Hydroxylase Using an Olefin-Containing Substrate to Construct a Substituted Piperidine Ring. %XApplying enzymatic reactions to produce useful molecules is a central focus of chemical biology. Iron and 2-oxoglutarate (Fe/2OG) enzymes are found in all kingdoms of life and catalyze a broad array of oxidative transformations. Herein, we demonstrate that the activity of an Fe/2OG enzyme can be redirected when changing the targeted carbon hybridization from sp3 to sp2. During leucine 5-hydroxylase catalysis, installation of an olefin group onto the substrate redirects the Fe(IV)−oxo species reactivity from hydroxylation to asymmetric epoxidation. The resulting epoxide subsequently undergoes intramolecular cyclization to form the substituted piperidine, 2S,5S-hydroxypipecolic acid. %0Journal Article