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Issue 13, 2017
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The polyketide backbone of thiolactomycin is assembled by an unusual iterative polyketide synthase

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Abstract

Following the in vivo investigation of thiotetronate assembly in Lentzea sp. and in S. thiolactonus NRRL 15439 (Havemann et al., Chem. Commun., 2017, DOI: 10.1039/c6cc09933e), the minimal set of genes required for thiolactomycin production was determined through heterologous expression and the mechanism for polyketide assembly was established in vitro through incubation of recombinant TlmB with its substrates in the presence of either nonhydrolysable or hydrolysable chemical probes. The results presented here constitute unequivocal evidence of enzymatic processing by an unusual iterative polyketide synthase.

Graphical abstract: The polyketide backbone of thiolactomycin is assembled by an unusual iterative polyketide synthase

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Supplementary files

Article information


Submitted
14 Dec 2016
Accepted
17 Jan 2017
First published
26 Jan 2017

This article is Open Access

Chem. Commun., 2017,53, 2182-2185
Article type
Communication

The polyketide backbone of thiolactomycin is assembled by an unusual iterative polyketide synthase

M. E. Yurkovich, R. Jenkins, Y. Sun, M. Tosin and P. F. Leadlay, Chem. Commun., 2017, 53, 2182
DOI: 10.1039/C6CC09934C

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