Structural highlights
FunctionPublication Abstract from PubMedModular trans-acyltransferase polyketide synthases (trans-AT PKSs) are enzymatic assembly lines that biosynthesize complex polyketide natural products. Relative to their better studied cis-AT counterparts, the trans-AT PKSs introduce remarkable chemical diversity into their polyketide products. A notable example is the lobatamide A PKS, which incorporates a methylated oxime. Here we demonstrate biochemically that this functionality is installed on-line by an unusual oxygenase-containing bimodule. Furthermore, analysis of the oxygenase crystal structure coupled with site-directed mutagenesis allows us to propose a model for catalysis, as well as identifying key protein-protein interactions that support this chemistry. Overall, our work adds oxime-forming machinery to the biomolecular toolbox available for trans-AT PKS engineering, opening the way to introducing such masked aldehyde functionalities into diverse polyketides. Modular oxime formation by a trans-AT polyketide synthase.,Minas HA, Francois RMM, Hemmerling F, Fraley AE, Dieterich CL, Rudisser SH, Meoded RA, Collin S, Weissman KJ, Gruez A, Piel J Angew Chem Int Ed Engl. 2023 May 22:e202304481. doi: 10.1002/anie.202304481. PMID:37216334[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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This page was last modified 13:21, 30 August 2023.