Mechanistic insight on the activity and substrate selectivity of nonheme iron dioxygenases

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    Nonheme iron dioxygenases catalyze vital reactions for human health particularly related to aging processes. They are involved in the biosynthesis of amino acids, but also the biodegradation of toxic compounds. Typically they react with substrate through oxygen atom transfer, although often with the
    assistance of a co-substrate like α-ketoglutarate that is converted to succinate and CO2. Many reaction processes catalyzed by the nonheme iron dioxygenases are stereoselective or regiospecific and hence understanding the mechanism and protein involvement in the selectivity is important for the design of biotechnological applications of these enzymes. In this Account I will review recent work of our group on nonheme iron dioxygenases and include background information on their general structure and catalytic cycle. Examples of stereoselective and regiospecific reaction mechanisms we elucidated are for the AlkB repair enzyme, prolyl-4-hydroxylase and the ergothioneine biosynthesis enzyme. Finally, I cover an example where we bioengineered S-phydroxymandelate synthase into the R-p-hydroxymandelate synthase.
    Original languageEnglish
    Pages (from-to)1501-1516
    JournalChemical Records
    Issue number10
    Early online date7 Jun 2018
    Publication statusPublished - Oct 2018


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