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Jenner, Matthew; Afonso, José P.; Kohlhaas, Christoph; Karbaum, Petra; Frank, Sarah; Piel, Jörn; Oldham, Neil J. (2016)
Publisher: Royal Society of Chemistry
Languages: English
Types: Article
Subjects:

Classified by OpenAIRE into

mesheuropmc: lipids (amino acids, peptides, and proteins), stomatognathic system, animal structures, humanities, bacteria
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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