INVESTIGADORES
GRAMAJO Hugo Cesar
artículos
Título:
Fatty acid biosíntesis in actinomycetes
Autor/es:
GAGO G, DIACOVICH L, ARABOLAZA A, TSAI SC, GRAMAJO H
Revista:
FEMS MICROBIOLOGY REVIEWS
Editorial:
WILEY-BLACKWELL PUBLISHING, INC
Referencias:
Lugar: Londres; Año: 2011 p. 475 - 497
ISSN:
0168-6445
Resumen:
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.