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

Jenner, Matthew; Afonso, Jos� P.; Kohlhaas, Christoph; Karbaum, Petra; Frank, Sarah; Piel, J�rn; Oldham, Neil J.

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
• Contract Date: Jun 24, 2016