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Direct acylation of carrier proteins with functionalized beta-lactones.

ABSTRACT: As the key component of many biosynthetic assemblies, acyl-carrier proteins offer a robust entry point for introduction of small molecule probes and pathway intermediates. Current labeling strategies primarily rely on modifications to the phosphopantetheine cofactor or its biosynthetic precursors followed by attachment to the apo form of a given carrier protein. As a greatly simplified alternative, direct and selective acylation of holo-acyl-carrier proteins using readily accessible beta-lactones as electrophilic partners for the phosphopantetheine-thiol has been demonstrated.

SUBMITTER: Amoroso JW

PROVIDER: S-EPMC4237225 | biostudies-literature | 2010 May

REPOSITORIES: biostudies-literature

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Direct acylation of carrier proteins with functionalized beta-lactones.

Amoroso Jon W JW Borketey Lawrence S LS Prasad Gitanjeli G Schnarr Nathan A NA

Organic letters 20100501 10

As the key component of many biosynthetic assemblies, acyl-carrier proteins offer a robust entry point for introduction of small molecule probes and pathway intermediates. Current labeling strategies primarily rely on modifications to the phosphopantetheine cofactor or its biosynthetic precursors followed by attachment to the apo form of a given carrier protein. As a greatly simplified alternative, direct and selective acylation of holo-acyl-carrier proteins using readily accessible beta-lactone ...[more]

PMID: 20433156

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