Acyl hydrolases from trans-AT polyketide synthases target acetyl units on acyl carrier proteins

Jenner, Matthew and Afonso, José P. and Kohlhaas, Christoph and Karbaum, Petra and Frank, Sarah and Piel, Jörn and Oldham, Neil J. (2016) Acyl hydrolases from trans-AT polyketide synthases target acetyl units on acyl carrier proteins. Chemical Communications, 52 (30). pp. 5262-5265. ISSN 1364-548X

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Abstract

Acyl hydrolase (AH) domains are a common feature of trans-AT PKSs. They have been hypothesised to perform a proofreading function by removing acyl chains from stalled sites. This study determines the substrate tolerance of the AH PedC for a range of acyl-ACPs. Clear preference towards short, linear acyl-ACPs is shown, with acetyl-ACP the best substrate. These results imply a more targeted housekeeping role for PedC: namely the removal of unwanted acetyl groups from ACP domains caused by erroneous transfer of acetyl-CoA, or possibly by decarboxylation of malonyl-ACP.

Item Type: Article
Schools/Departments: University of Nottingham, UK > Faculty of Science > School of Chemistry
Identification Number: 10.1039/C6CC01453D
Related URLs:
Depositing User: Oldham, Dr Neil J
Date Deposited: 24 Jun 2016 13:50
Last Modified: 15 Oct 2017 23:23
URI: http://eprints.nottingham.ac.uk/id/eprint/34373

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