Editor: Diego de Mendoza
Fatty acid biosynthesis in actinomycetes
Article first published online: 19 JAN 2011
© 2011 Federation of European Microbiological Societies. Published by Blackwell Publishing Ltd. All rights reserved
FEMS Microbiology Reviews
Volume 35, Issue 3, pages 475–497, May 2011
How to Cite
Gago, G., Diacovich, L., Arabolaza, A., Tsai, S.-C. and Gramajo, H. (2011), Fatty acid biosynthesis in actinomycetes. FEMS Microbiology Reviews, 35: 475–497. doi: 10.1111/j.1574-6976.2010.00259.x
- Issue published online: 4 APR 2011
- Article first published online: 19 JAN 2011
- Accepted manuscript online: 19 NOV 2010 09:43AM EST
- Received 2 July 2010; revised 19 October 2010; accepted 7 November 2010., Final version published online 19 January 2011.
- lipid biosynthesis;
- acyl-CoA carboxylase;
- lipid homeostasis
All organisms that produce fatty acids do so via a repeated cycle of reactions. In mammals and other animals, these reactions are catalyzed by a type I fatty acid synthase (FAS), a large multifunctional protein to which the growing chain is covalently attached. In contrast, most bacteria (and plants) contain a type II system in which each reaction is catalyzed by a discrete protein. The pathway of fatty acid biosynthesis in Escherichia coli is well established and has provided a foundation for elucidating the type II FAS pathways in other bacteria (White et al., 2005). However, fatty acid biosynthesis is more diverse in the phylum Actinobacteria: Mycobacterium, possess both FAS systems while Streptomyces species have only the multienzyme FAS II system and Corynebacterium species exclusively FAS I. In this review, we present an overview of the genome organization, biochemical properties and physiological relevance of the two FAS systems in the three genera of actinomycetes mentioned above. We also address in detail the biochemical and structural properties of the acyl-CoA carboxylases (ACCases) that catalyzes the first committed step of fatty acid synthesis in actinomycetes, and discuss the molecular bases of their substrate specificity and the structure-based identification of new ACCase inhibitors with antimycobacterial properties.