Projects per year
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).
|Number of pages||4|
|Early online date||13 Jan 2017|
|Publication status||Published - 4 Feb 2017|
- Bristol BioDesign Institute
FingerprintDive into the research topics of 'In vitro kinetic study of the squalestatin tetraketide synthase dehydratase reveals the stereochemical course of a fungal highly reducing polyketide synthase'. Together they form a unique fingerprint.
- 4 Finished
3-month Core Capability for Chemistry Research
1/01/13 → 1/04/13
Understanding Programming in Highly Reducing Iterative Fungal Polyketide Synthases - a Structural and Mechanistic Approach
Simpson, T. J.
1/07/11 → 1/01/15
CHEMICAL ANALYSIS OF HYBRID FUNGAL MEGASYNTHASES
Cox, R. J.
1/10/08 → 1/10/12