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Demonstration of starter unit interprotein transfer from a fatty acid synthase to a multidomain, nonreducing polyketide synthase.

ABSTRACT: The pathway for substrate transacylation between a fungal type I fatty acid synthase (FAS) and a nonreducing polyketide synthase (NR-PKS) was determined by in vitro reconstitution of dissected domains. System kinetics were influenced by domain dissections, and the FAS phosphopantetheinyl transferase (PPT) monodomain exhibited coenzyme A selectivity for the post-translational activation of the FAS acyl carrier protein (ACP).

SUBMITTER: Foulke-Abel J

PROVIDER: S-EPMC3516909 | biostudies-literature | 2012 Sep

REPOSITORIES: biostudies-literature

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Demonstration of starter unit interprotein transfer from a fatty acid synthase to a multidomain, nonreducing polyketide synthase.

Foulke-Abel Jennifer J Townsend Craig A CA

Chembiochem : a European journal of chemical biology 20120713 13

The pathway for substrate transacylation between a fungal type I fatty acid synthase (FAS) and a nonreducing polyketide synthase (NR-PKS) was determined by in vitro reconstitution of dissected domains. System kinetics were influenced by domain dissections, and the FAS phosphopantetheinyl transferase (PPT) monodomain exhibited coenzyme A selectivity for the post-translational activation of the FAS acyl carrier protein (ACP). ...[more]

PMID: 22807303

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