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Dissecting how modular polyketide synthase ketoreductases interact with acyl carrier protein-attached substrates.


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.

SUBMITTER: Moretto L 

PROVIDER: S-EPMC6038798 | biostudies-other | 2017 Oct

REPOSITORIES: biostudies-other

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Dissecting how modular polyketide synthase ketoreductases interact with acyl carrier protein-attached substrates.

Moretto Luisa L   Vance Steven S   Heames Brennan B   Broadhurst R William RW  

Chemical communications (Cambridge, England) 20171005 83


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. ...[more]

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