Jump to main content
Jump to site search

Issue 10, 2017
Previous Article Next Article

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

Author affiliations

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).

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

Back to tab navigation

Supplementary files

Publication details

The article was received on 22 Dec 2016, accepted on 13 Jan 2017 and first published on 13 Jan 2017


Article type: Communication
DOI: 10.1039/C6CC10172K
Citation: Chem. Commun., 2017,53, 1727-1730
  •   Request permissions

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

    E. Liddle, A. Scott, L. Han, D. Ivison, T. J. Simpson, C. L. Willis and R. J. Cox, Chem. Commun., 2017, 53, 1727
    DOI: 10.1039/C6CC10172K

Search articles by author

Spotlight

Advertisements