Matthew Jenner
Acyl hydrolases from trans-AT polyketide synthases target acetyl units on acyl carrier proteins
Authors
Afonso
Christoph Kohlhaas
Petra Karbaum
Sarah Frank
Piel
NEIL OLDHAM NEIL.OLDHAM@NOTTINGHAM.AC.UK
Professor of Biomolecular Spectrometry
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.
Citation
Jenner, M., Afonso, J. P., Kohlhaas, C., Karbaum, P., Frank, S., Piel, J., & Oldham, N. J. (in press). Acyl hydrolases from trans-AT polyketide synthases target acetyl units on acyl carrier proteins. Chemical Communications, 52(30), https://doi.org/10.1039/C6CC01453D
Journal Article Type | Article |
---|---|
Acceptance Date | Mar 15, 2016 |
Online Publication Date | Mar 15, 2016 |
Deposit Date | Jun 24, 2016 |
Publicly Available Date | Jun 24, 2016 |
Journal | Chemical Communications |
Print ISSN | 1359-7345 |
Electronic ISSN | 1364-548X |
Publisher | Royal Society of Chemistry |
Peer Reviewed | Peer Reviewed |
Volume | 52 |
Issue | 30 |
DOI | https://doi.org/10.1039/C6CC01453D |
Public URL | https://nottingham-repository.worktribe.com/output/780353 |
Publisher URL | http://pubs.rsc.org/en/Content/ArticleLanding/2016/CC/C6CC01453D#!divAbstract |
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