Dissecting how modular polyketide synthase ketoreductases interact with acyl carrier protein-attached substrates
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Authors
Journal Title
Chemical Communications
Publisher
Royal Society of Chemistry
Volume
53
Pages
11457-11460
Type
Article
Metadata
Show full item recordAbstract
Interaction studies using fragments excised from the modular mycolactone polyketide synthase show that ketoreductase domains possess a generic binding site for acyl carrier protein domains and provide evidence that the pendant 5′-phosphopantetheine prosthetic group plays a key role in delivering acyl substrates to the active site in the correct orientation.
Sponsorship
The authors would like to thank the Wellcome Trust (grant number 094252/Z/10/Z) for funding this research. LM was supported by an EPSRC PhD studentship.
Funder references
Wellcome Trust (094252/Z/10/Z)
Identifiers
External DOI: https://doi.org/10.1039/c7cc04625a
This record's URL: https://www.repository.cam.ac.uk/handle/1810/279838
Rights
Attribution 4.0 International (CC BY 4.0)
Licence URL: https://creativecommons.org/licenses/by/4.0/
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Except where otherwise noted, this item's licence is described as Attribution 4.0 International (CC BY 4.0)