Demonstration of Starter Unit Interprotein Transfer from a Fatty Acid Synthase to a Multidomain, Nonreducing Polyketide Synthase

Jennifer Foulke-Abel; Craig A. Townsend

doi:10.1002/cbic.201200267

Demonstration of Starter Unit Interprotein Transfer from a Fatty Acid Synthase to a Multidomain, Nonreducing Polyketide Synthase

Jennifer Foulke-Abel, Craig A. Townsend

School of Medicine

Research output: Contribution to journal › Article › peer-review

20 Scopus citations

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).

Original language	English (US)
Pages (from-to)	1880-1884
Number of pages	5
Journal	ChemBioChem
Volume	13
Issue number	13
DOIs	https://doi.org/10.1002/cbic.201200267
State	Published - Sep 3 2012

Keywords

Fatty acids
Fungal metabolites
Phosphopantetheinylation
Polyketides
Protein-protein interactions

ASJC Scopus subject areas

Biochemistry
Molecular Medicine
Molecular Biology
Organic Chemistry

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10.1002/cbic.201200267

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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).",

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AB - 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).

KW - Fatty acids

KW - Fungal metabolites

KW - Phosphopantetheinylation

KW - Polyketides

KW - Protein-protein interactions

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Demonstration of Starter Unit Interprotein Transfer from a Fatty Acid Synthase to a Multidomain, Nonreducing Polyketide Synthase

Abstract

Keywords

ASJC Scopus subject areas

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