Acyl hydrolases from trans-AT polyketide synthases target acetyl units on acyl carrier proteins
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...
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| Format: | Article |
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Royal Society of Chemistry
2016
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| Online Access: | https://eprints.nottingham.ac.uk/34373/ |
| _version_ | 1848794837694808064 |
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| author | Jenner, Matthew Afonso, José P. Kohlhaas, Christoph Karbaum, Petra Frank, Sarah Piel, Jörn Oldham, Neil J. |
| author_facet | Jenner, Matthew Afonso, José P. Kohlhaas, Christoph Karbaum, Petra Frank, Sarah Piel, Jörn Oldham, Neil J. |
| author_sort | Jenner, Matthew |
| building | Nottingham Research Data Repository |
| collection | Online Access |
| description | 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. |
| first_indexed | 2025-11-14T19:22:32Z |
| format | Article |
| id | nottingham-34373 |
| institution | University of Nottingham Malaysia Campus |
| institution_category | Local University |
| last_indexed | 2025-11-14T19:22:32Z |
| publishDate | 2016 |
| publisher | Royal Society of Chemistry |
| recordtype | eprints |
| repository_type | Digital Repository |
| spelling | nottingham-343732020-05-04T17:41:50Z https://eprints.nottingham.ac.uk/34373/ Acyl hydrolases from trans-AT polyketide synthases target acetyl units on acyl carrier proteins Jenner, Matthew Afonso, José P. Kohlhaas, Christoph Karbaum, Petra Frank, Sarah Piel, Jörn Oldham, Neil J. 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. Royal Society of Chemistry 2016-03-15 Article PeerReviewed Jenner, Matthew, Afonso, José P., Kohlhaas, Christoph, Karbaum, Petra, Frank, Sarah, Piel, Jörn and Oldham, Neil J. (2016) Acyl hydrolases from trans-AT polyketide synthases target acetyl units on acyl carrier proteins. Chemical Communications, 52 (30). pp. 5262-5265. ISSN 1364-548X http://pubs.rsc.org/en/Content/ArticleLanding/2016/CC/C6CC01453D#!divAbstract doi:10.1039/C6CC01453D doi:10.1039/C6CC01453D |
| spellingShingle | Jenner, Matthew Afonso, José P. Kohlhaas, Christoph Karbaum, Petra Frank, Sarah Piel, Jörn Oldham, Neil J. Acyl hydrolases from trans-AT polyketide synthases target acetyl units on acyl carrier proteins |
| title | Acyl hydrolases from trans-AT polyketide synthases target acetyl units on acyl carrier proteins |
| title_full | Acyl hydrolases from trans-AT polyketide synthases target acetyl units on acyl carrier proteins |
| title_fullStr | Acyl hydrolases from trans-AT polyketide synthases target acetyl units on acyl carrier proteins |
| title_full_unstemmed | Acyl hydrolases from trans-AT polyketide synthases target acetyl units on acyl carrier proteins |
| title_short | Acyl hydrolases from trans-AT polyketide synthases target acetyl units on acyl carrier proteins |
| title_sort | acyl hydrolases from trans-at polyketide synthases target acetyl units on acyl carrier proteins |
| url | https://eprints.nottingham.ac.uk/34373/ https://eprints.nottingham.ac.uk/34373/ https://eprints.nottingham.ac.uk/34373/ |