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

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Jenner, Matthew, Afonso, José P., Kohlhaas, Christoph, Karbaum, Petra, Frank, Sarah, 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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Official URL: http://pubs.rsc.org/en/Content/ArticleLanding/2016/CC/C6CC01453D#!divAbstract

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
RIS ID:	https://nottingham-repository.worktribe.com/output/780353
Schools/Departments:	University of Nottingham, UK > Faculty of Science > School of Chemistry
Identification Number:	10.1039/C6CC01453D
Related URLs:	URL URL Type UNSPECIFIED Publisher
Depositing User:	Oldham, Dr Neil J
Date Deposited:	24 Jun 2016 13:50
Last Modified:	04 May 2020 17:41
URI:	https://eprints.nottingham.ac.uk/id/eprint/34373

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