Trapping of the Enoyl-Acyl Carrier Protein Reductase-Acyl Carrier Protein Interaction

An ideal target for metabolic engineering, fatty acid biosynthesis remains poorly understood on a molecular level. These carrier protein-dependent pathways require fundamental protein Protein interactions to guide reactivity and processivity, and their control has become one of the major hurdles in...

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Vydáno v:	Journal of the American Chemical Society Ročník 138; číslo 12; s. 3962 - 3965
Hlavní autoři:	Tallorin, Lorillee, Finzel, Kara, Nguyen, Quynh G., Beld, Joris, La Clair, James J., Burkart, Michael D.
Médium:	Journal Article
Jazyk:	angličtina
Vydáno:	WASHINGTON Amer Chemical Soc 30.03.2016
Témata:	Acyl Carrier Protein - metabolism Chemistry Chemistry, Multidisciplinary Enoyl-(Acyl-Carrier-Protein) Reductase (NADH) - isolation & purification Enoyl-(Acyl-Carrier-Protein) Reductase (NADH) - metabolism Escherichia coli - enzymology Escherichia coli Proteins - isolation & purification Escherichia coli Proteins - metabolism Fatty Acid Synthase, Type II - isolation & purification Fatty Acid Synthase, Type II - metabolism Models, Molecular Molecular Structure Oxidoreductases - isolation & purification Oxidoreductases - metabolism Physical Sciences Protein Binding Protein Engineering Science & Technology Triclosan - chemistry Triclosan - metabolism TARGET TRICLOSAN FABI INHIBITION FATTY-ACID BIOSYNTHESIS MECHANISM ANALOGS PLASMODIUM-FALCIPARUM ESCHERICHIA-COLI BINDING
ISSN:	0002-7863, 1520-5126
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Shrnutí:	An ideal target for metabolic engineering, fatty acid biosynthesis remains poorly understood on a molecular level. These carrier protein-dependent pathways require fundamental protein Protein interactions to guide reactivity and processivity, and their control has become one of the major hurdles in successfully adapting these biological machines. Our laboratory has developed methods to prepare acyl carrier proteins (ACPs) loaded with substrate mimetics and cross-linkers to visualize and trap interactions with partner enzymes, and we continue to expand the tools for studying these pathways. We now describe application of the slow-onset, tight-binding inhibitor triclosan to explore the interactions between the type II fatty acid ACP from Escherichia coli, AcpP,, and its corresponding enoyl-ACP Teductase, FabI. We show that the AcpP-triclosan complex demonstrates nM binding, inhibits in vitro activity, and can be used to isolate FabI in complex proteomes.
Bibliografie:	NIH RePORTER ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23
ISSN:	0002-7863 1520-5126
DOI:	10.1021/jacs.5b13456