The structures of the O-glycosyltransferase LanGT2 and the engineered, C—C bond-forming variant LanGT2S8Ac show how the replacement of a single loop can change the functionality of the enzyme. Crystal structures of the enzymes in complex with a nonhydrolyzable nucleotide-sugar analogue revealed that there is a conformational transition to create the binding sites for the aglycon substrate. This induced-fit transition was explored by molecular docking experiments with various aglycon substrates.

New Thailandepsin B pseudo‐natural products have been prepared. Our synthetic strategy offers the possibility to introduce varying warheads via late stage modification. Additionally, it gives access to the asymmetric branched allylic ester moiety of the natural product in a highly diastereoselective manner applying rhodium‐catalyzed hydrooxycarbonylation. The newly developed pseudo‐natural products are extremely potent and selective HDAC inhibitors. The non‐proteinogenic amino acid d ‐norleucine was obtained enantioselectively by a recently developed method of rhodium‐catalyzed hydroamination.

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The cis‐ and trans‐dicyano‐tris[2.2.2]‐σ‐homobenzenes 9/10 have been synthesized and characterized by spectroscopic methods and X‐ray structural analyses. From the relative ease of their transformations and from the products of their vapour phase pyrolyses, it is concluded that a pericyclic mechanism is no longer operative.

Strukturen der O-Glycosyltransferase LanGT2 und der generierten C-Glycosyltransferase LanGT2S8Ac zeigen, dass der Austausch eines kurzen Peptidfragments die Funktionalität eines Enzyms deutlich verändern kann. Eine synthetische TDP-Carbaolivose wurde mit den Enzymen kokristallisiert. Es zeigte sich, dass die Bindung des Carbazuckers zu einer Konformationsänderung des Enzyms führt, die dann eine Bindestelle für ein Aglykonsubstrat erzeugt. Obwohl eine Bindung des Aglykons nicht experimentell nachgewiesen wurde, deuten Docking-Studien auf unterschiedliche Bindungsmodi im Fall von O-bzw. C-Glycosylierung hin.