Abstract
Rings in biologically active molecules confer rigidity that helps the molecules to bind strongly and selectively to their targets. A ring-forming mechanism has been identified that involves a biochemically unusual reaction. See Letter p.124 Polyketide synthases (PKSs) are modular enzyme complexes that produce polyketides, a large class of secondary metabolites — otherwise known as natural products. In this manuscript, the authors identify and characterize a novel PKS module from the endofungal bacterium Burkholderia rhizoxinica that catalyses a vinylogous addition of a malonyl unit to an unsaturated thioester, generating a branch in the growing polyketide chain. This enzymological activity is very unusual; all previously studied PKS modules catalyse the head-to-tail fusion of acyl and malonyl units, yielding a linear polyketide chain. This newly discovered reaction provides a simple mechanism by which structural diversity of polyketide natural products can be increased.
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