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Visualizing the chain-flipping mechanism in fatty acid biosynthesis
Journal article   Open access   Peer reviewed

Visualizing the chain-flipping mechanism in fatty acid biosynthesis

Joris Beld, Hu Cang, Michael D. Burkart and Univ. of California, San Diego, CA (United States)
Angewandte Chemie (International ed.), v 53(52), pp 14456-14461
22 Dec 2014
DOI: https://doi.org/10.1002/anie.201408576
PMID: 25354391
Featured in Collection :   UN Sustainable Development Goals @ Drexel
url
https://europepmc.org/articles/pmc4425425?pdf=renderView
Accepted (AM)Open Access (License Unspecified),  Open

Abstract

acyl carrier protein chain-flipping mechanism fatty acid synthase fatty acids solvatochromism
In the fatty acid biosynthesis of plants and bacteria, the acyl carrier protein (ACP) is known to sequester elongating products within its hydrophobic core, but this dynamic mechanism remains poorly understood. In this paper we exploit solvatochromic pantetheine probes attached to ACP that fluoresce when sequestered. Addition of a catalytic partner lures the cargo out of the ACP and into the active site of the enzyme, enhancing fluorescence to reveal the elusive chain-flipping mechanism. This activity is confirmed by demonstration of a dual solvatochromic-crosslinking probe and solution-phase NMR. The chain-flipping mechanism can be visualized by single molecule fluorescent techniques, demonstrating specificity between the Escherichia coli ACP and its ketoacyl synthase catalytic partner KASII.

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42 citations in Web of Science
42 citations in Scopus

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UN Sustainable Development Goals (SDGs)

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Collaboration types
Domestic collaboration
Web of Science research areas
Chemistry, Multidisciplinary
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