Characterization of the Baeyer-Villiger monooxygenase in the pathway of the bacterial pyrrolizidine alkaloids, legonmycins.

The Baeyer-Villiger monooxygenase (BVMO), LgnC, plays a crucial role in the biosynthesis of bacterial pyrrolizidine alkaloids, legonmycins. It processes bicyclic indolizidine substrates generated from the coordinative action of two non-ribosomal peptide synthetases (LgnB and LgnD) and the standalone type II thioesterase-like enzyme (LgnA). It has been demonstrated that the enzyme selectively inserts molecular oxygen into the carbon-carbon bond adjacent to the carbonyl group in legonindolizidines to form bicyclic 1,3-oxazepine carbamate intermediates.

Exploring a wax synthase using acyl-SNACs as donor substrates.

The demand of fragrance and food industries for short/branched wax esters is increasing due to their rich scent and low toxicity. Wax synthase and acyl-CoA:diacylglycerol -acyltransferase (WS/DGAT) are a family of bacterial enzymes capable of catalysing the production of wax esters. Here, we report that a WS/DGAT from is able to mediate the reactions between alcohol acceptors and synthetic acyl-donor mimics, acyl-SNACs.