DesII is a member of the radical <i>S</i>-adenosyl-methionine (SAM) family of enzymes that catalyzes the radical-mediated deamination of TDP-4-amino-4,6-dideoxy-D-glucose during biosynthesis of the atypical carbohydrate desosamine. DesII is of particular interest, because in addition to its lyase activity, it can also act as an equally effective radical-mediated dehydrogenase when presented with the alternative substrate TDP-D-quinovose. Using a combination of EPR, kinetic isotope effect measurements and the investigation of substrate analogs, the details underlying the mechanistic switching of DesII are being established and suggest that substrate conformation plays an important role in controlling the course of the DesII-catalyzed reactions.<br/>

Mechanistic investigations of the radical SAM enzyme, DesII

2019 Spring National Meeting

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