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 ; Oldham, Neil J. (2016)
  • Publisher: Royal Society of Chemistry
  • Related identifiers: doi: 10.1039/C6CC01453D
  • Subject:
    mesheuropmc: humanities | bacteria | lipids (amino acids, peptides, and proteins) | animal structures | stomatognathic system

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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