ECI Digital Archives

Title

Broadening the substrate scope of strictosidine synthases by site-directed mutagenesis

Authors

Elisabeth Eger, University of Graz, AustriaFollow
Eva Fischereder, University of Graz, Austria
Horst Lechner, University of Graz, Austria
Wolfgang Kroutil, University of Graz, Austria
Desiree Pressnitz, University of Graz, Austria
Mahima Sharma, Department of Chemistry, University of York
Gideon Grogan, Department of Chemistry, University of York

Conference Dates

September 24-28, 2017

Abstract

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 4.3.3.2) 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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Recommended Citation

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