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Title: Versatility of acyl-acyl carrier protein synthetases

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 E. coli ACP in vitro. Vibrio harveyi 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 E. coli 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.
Authors:
 [1] ;  [1] ;  [1]
  1. Univ. of California San Diego, La Jolla, CA (United States)
Publication Date:
OSTI Identifier:
1224136
Grant/Contract Number:
EE0003373
Type:
Published Article
Journal Name:
Chemistry & Biology
Additional Journal Information:
Journal Volume: 21; Journal Issue: 10; Journal ID: ISSN 1074-5521
Publisher:
Elsevier
Research Org:
Univ. of California, San Diego, CA (United States)
Sponsoring Org:
USDOE Office of Energy Efficiency and Renewable Energy (EERE), Bioenergy Technologies Office (EE-3B)
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES