Versatility of acyl-acyl carrier protein synthetases [electronic resource].
- Washington, D.C. : United States. Dept. of Energy. Office of Energy Efficiency and Renewable Energy, 2014. and Oak Ridge, Tenn. : Distributed by the Office of Scientific and Technical Information, U.S. Dept. of Energy
- Physical Description:
- pages 1,293-1,299 : digital, PDF file
- Additional Creators:
- United States. Department of Energy. Office of Energy Efficiency and Renewable Energy and United States. Department of Energy. Office of Scientific and Technical Information
- Restrictions on Access:
- Free-to-read Unrestricted online access
- The acyl carrier protein (ACP) requires posttranslational modification with a 4'-phosphopantetheine arm for activity, and this thiol-terminated modification carries cargo between enzymes in ACP-dependent metabolic pathways. In this paper, we show that acyl-ACP synthetases (AasSs) from different organisms are able to load even, odd, and unnatural fatty acids onto <i>E. coli</i> ACP in vitro. <i>Vibrio harveyi</i> AasS not only shows promiscuity for the acid substrate, but also is active upon various alternate carrier proteins. AasS activity also extends to functional activation in living organisms. We show that exogenously supplied carboxylic acids are loaded onto ACP and extended by the <i>E. coli</i> fatty acid synthase, including unnatural fatty acid analogs. These analogs are further integrated into cellular lipids. Finally, in vitro characterization of four different adenylate-forming enzymes allowed us to disambiguate CoA-ligases and AasSs, and further in vivo studies show the potential for functional application in other organisms.
- Published through SciTech Connect., 10/09/2014., ": S107455211400297X", Chemistry & Biology 21 10 ISSN 1074-5521 AM, Joris Beld; Kara Finzel; Michael D. Burkart., and Univ. of California, San Diego, CA (United States)
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