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Updated: Mar 23, 2026

A Facile Protocol to Generate Site-Specifically Acetylated Proteins in Escherichia Coli
Published on: December 9, 2017
Acyl hydrolases from trans-AT polyketide synthases target acetyl units on acyl carrier proteins
Matthew Jenner1, Jose P Afonso, Christoph Kohlhaas
1School of Chemistry, University of Nottingham, University Park, Nottingham, NG7 2RD, UK. neil.oldham@nottingham.ac.uk.
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.
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