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Issue 30, 2016
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Acyl hydrolases from trans-AT polyketide synthases target acetyl units on acyl carrier proteins

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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.

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

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Article information


Submitted
17 Feb 2016
Accepted
15 Mar 2016
First published
15 Mar 2016

Chem. Commun., 2016,52, 5262-5265
Article type
Communication

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

M. Jenner, J. P. Afonso, C. Kohlhaas, P. Karbaum, S. Frank, J. Piel and N. J. Oldham, Chem. Commun., 2016, 52, 5262
DOI: 10.1039/C6CC01453D

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