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In vitro kinetic study of the squalestatin tetraketide synthase dehydratase reveals the stereochemical course of a fungal highly reducing polyketide synthase

Liddle, Emma, Scott, Alan, Han, Li-Chen, Ivison, David, Simpson, Thomas J., Willis, Christine L. and Cox, Russell J. 2017. In vitro kinetic study of the squalestatin tetraketide synthase dehydratase reveals the stereochemical course of a fungal highly reducing polyketide synthase. Chemical Communications 53 (10) , pp. 1727-1730. 10.1039/C6CC10172K

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Abstract

Six potential diketide substrates for the squalestatin tetraketide synthase (SQTKS) dehydratase (DH) domain were synthesised as N-acetyl cysteamine thiolesters (SNAC) and tested in kinetic assays as substrates with an isolated DH domain. 3R-3-hydroxybutyryl SNAC 3R-16 was turned over by the enzyme, but its enantiomer was not. Of the four 2-methyl substrates only 2R,3R-2-methyl-3-hydroxybutyryl SNAC 2R,3R-8 was a substrate. Combined with stereochemical information from the isolated SQTKS enoyl reductase (ER) domain, our results provide a near complete stereochemical description of the first cycle of beta-modification reactions of a fungal highly reducing polyketide synthase (HR-PKS). The results emphasise the close relationship between fungal HR-PKS and vertebrate fatty acid synthases (vFAS).

Item Type: Article
Date Type: Published Online
Status: Published
Schools: Chemistry
Publisher: Royal Society of Chemistry
ISSN: 1359-7345
Date of First Compliant Deposit: 30 May 2019
Date of Acceptance: 13 January 2017
Last Modified: 30 Jun 2019 19:30
URI: http://orca.cf.ac.uk/id/eprint/122972

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