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Acyl hydrolases from trans-AT polyketide synthases target acetyl units on acyl carrier proteins
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Jenner, Matthew, Afonso, Jose 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. doi:10.1039/c6cc01453d ISSN 1359-7345.
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Official URL: http://dx.doi.org/10.1039/C6CC01453D
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.
Item Type: | Journal Article | ||||||||||
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Divisions: | Faculty of Science, Engineering and Medicine > Science > Chemistry | ||||||||||
Journal or Publication Title: | Chemical Communications | ||||||||||
Publisher: | Royal Society of Chemistry | ||||||||||
ISSN: | 1359-7345 | ||||||||||
Official Date: | 18 April 2016 | ||||||||||
Dates: |
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Volume: | 52 | ||||||||||
Number: | 30 | ||||||||||
Page Range: | pp. 5262-5265 | ||||||||||
DOI: | 10.1039/c6cc01453d | ||||||||||
Status: | Peer Reviewed | ||||||||||
Publication Status: | Published | ||||||||||
Access rights to Published version: | Restricted or Subscription Access |
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