Broadening the substrate scope of strictosidine synthases by site-directed mutagenesis
September 24-28, 2017
The condensation of ß-arylethylamines with carbonyl compounds (Pictet-Spengler reaction) is employed in the synthesis of tetrahydro-β-carboline and isoquinoline scaffolds which are common motifs in many naturally occurring alkaloids. These compounds exhibit a range of biological activities and are thus interesting targets for organic synthesis and medicinal chemistry.
Nature’s equivalent to the Pictet-Spengler reaction is catalyzed by the so called Pictet-Spenglerases. Within this class of enzymes, strictosidine synthases (STRs, EC 18.104.22.168) have attracted attention [1-4]. These enzymes catalyse the formation of the 1,2,3,4-tetrahydro-β-carboline (S)-strictosidine, a key intermediate in the monoterpenoid indole alkaloid biosynthetic pathway in higher plants.
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Elisabeth Eger, Eva Fischereder, Horst Lechner, Wolfgang Kroutil, Desiree Pressnitz, Mahima Sharma, and Gideon Grogan, "Broadening the substrate scope of strictosidine synthases by site-directed mutagenesis" in "Enzyme Engineering XXIV", Pierre Monsan, Toulouse White Biotechnology, France Magali Remaud-Simeon, LISBP-INSA, University of Toulouse, France Eds, ECI Symposium Series, (2017). https://dc.engconfintl.org/enzyme_xxiv/67