Fatty acids, polyketides and non-ribosomal peptides are biosynthesized by pathways that resemble an assembly line, building their substrates along an enzymatic conveyor belt. While an ideal target for metabolic engineering, the lack in understanding of the fundamental protein - protein interactions between the enzymatic ensembles has become one of the major hurdles in successfully adapting these synthetic biological tools. Recently, our laboratory has developed methods to prepare acyl carrier proteins (ACPs) loaded with substrate mimetics and crosslinkers and used these <i>crypto</i>-CPs to trap interactions with select partner proteins, such as the ketosynthase (KS) and dehydratase (DH). We now describe the expansion of these methods to explore the interaction between fatty acid ACP, AcpP, and its corresponding enoyl ACP reductase (ER), FabI.

Trapping of the enoyl-acyl carrier protein reductase and acyl carrier protein interaction

251st National Meeting (2016)

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