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Malonyl carba(dethia)- and Malonyl oxa(dethia)-coenzyme A as Tools for Trapping Polyketide Intermediates

Malonyl carba(dethia)- and Malonyl oxa(dethia)-coenzyme A as Tools for Trapping Polyketide Intermediates

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TOSIN, Manuela, Dieter SPITELLER, Jonathan B. SPENCER, 2009. Malonyl carba(dethia)- and Malonyl oxa(dethia)-coenzyme A as Tools for Trapping Polyketide Intermediates. In: ChemBioChem. 10(10), pp. 1714-1723. ISSN 1439-4227. eISSN 1439-7633. Available under: doi: 10.1002/cbic.200900093

@article{Tosin2009-07-06Malon-15298, title={Malonyl carba(dethia)- and Malonyl oxa(dethia)-coenzyme A as Tools for Trapping Polyketide Intermediates}, year={2009}, doi={10.1002/cbic.200900093}, number={10}, volume={10}, issn={1439-4227}, journal={ChemBioChem}, pages={1714--1723}, author={Tosin, Manuela and Spiteller, Dieter and Spencer, Jonathan B.} }

Spencer, Jonathan B. eng 2011-10-19T07:33:45Z Tosin, Manuela Publ. in: ChemBioChem [A European Journal of Chemical Biology] ; 10 (2009), 10. - pp. 1714-1723 Spencer, Jonathan B. Tosin, Manuela deposit-license Spiteller, Dieter 2009-07-06 2011-10-19T07:33:45Z Caught in a trap. In this study trapped polyketide species (see figure) were off-loaded from a type III PKS by novel nonhydrolyzable malonyl coenzyme A analogues in which a methylene group or an oxygen atom replaces the sulfur atom of malonyl-CoA. This strategy allows the straightforward characterisation of intermediates of polyketide biosynthesis by LC-HR-ESI-MS/MS and provides valuable insights on the mechanism and timing of polyketide formation.<br /><br />In order to study intermediates in polyketide biosynthesis two nonhydrolyzable malonyl coenzyme A analogues were synthesised by a chemoenzymatic route. In these analogues the sulfur atom of CoA was replaced either by a methylene group (carbadethia analogue) or by an oxygen atom (oxadethia analogue). These malonyl-CoA analogues were found to compete with the natural extender unit malonyl-CoA and to trap intermediates from stilbene synthase, a type III polyketide synthase (PKS). From the reaction of stilbene synthase with its natural phenylpropanoid substrates, diketide, triketide and tetraketide species were successfully off-loaded and characterised by LC-MS. Moreover, the reactivity of the nonhydrolyzable analogues offers insights into the flexibility of substrate alignment in the PKS active site for efficient malonyl decarboxylation and condensation. Malonyl carba(dethia)- and Malonyl oxa(dethia)-coenzyme A as Tools for Trapping Polyketide Intermediates Spiteller, Dieter

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