Dissecting how modular polyketide synthase ketoreductases interact with acyl carrier protein-attached substrates
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Peer-reviewed
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Authors
Moretto, L
Vance, S
Heames, B
Broadhurst, RW
Abstract
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.
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Journal Title
Chemical Communications
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53
Publisher
Royal Society of Chemistry
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Sponsorship
Wellcome Trust (094252/Z/10/Z)
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.