Publications by authors named "Jan-Patrick Steitz"
Article Synopsis
- Thiamine diphosphate (ThDP) dependent enzymes catalyze asymmetric C-C bond formation through benzoin-type reactions, primarily producing α-hydroxy ketones.
- A wide variety of aldehydes and ketones can be used as acceptor substrates, but the usual donor substrates are mainly limited to simple, achiral molecules.
- A study identified a new subclass of ThDP-dependent enzymes that can use functionalized chiral α-keto acids as donors, greatly expanding the substrate range and allowing for high-yield production of enantioenriched compounds.
A wide range of thiamine diphosphate (ThDP)-dependent enzymes catalyze the benzoin-type carboligation of pyruvate with aldehydes. A few ThDP-dependent enzymes, such as YerE from Yersinia pseudotuberculosis (YpYerE), are known to accept ketones as acceptor substrates. Catalysis by YpYerE gives access to chiral tertiary alcohols, a group of products difficult to obtain in an enantioenriched form by other means.
View Article and Find Full Text PDFThe number of new psychoactive substances (NPS) that have emerged on the European market has been rapidly growing in recent years, with a particularly high number of new compounds from the group of synthetic cannabinoid receptor agonists. There have been various political efforts to control the trade and the use of NPS worldwide. In Germany, the Act to control the distribution of new psychoactive substances (NpSG) came into force in November 2016.
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