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A Molecular View of Fatty Acid Catabolism in Escherichia Coli WILLIAM D

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A Molecular View of Fatty Acid Catabolism in Escherichia Coli WILLIAM D MICROBIOLOGICAL REVIEWS, June 1986, p. 179-192 Vol. 50, No. 2 0146-0749/86/020179-14$02.00/0 Copyright C) 1986, American Society for Microbiology A Molecular View of Fatty Acid Catabolism in Escherichia coli WILLIAM D. NUNN Department of Molecular Biology and Biochemistry, University of California, Irvine, Irvine, California 92717 INTRODUCTION ........................................................... 179 GENETIC AND BIOCHEMICAL ANALYSIS OF FATTY ACID OXIDATION ................................. 179 Studies with the FAO Enzyme System ........................................................... 179 Studies with the ATO Enzyme System ........................................................... 181 TRANSPORT OF FATTY ACIDS ........................................................... 182 MCFA and LCFA Transport ........................................................... 182 SCFA Transport ........................................................... 185 REGULATION OF FATTY ACID DEGRADATION ........................................................... 185 fad Regulation ........................................................... 185 ato System ........................................................... 186 GENETIC AND BIOCHEMICAL FEATURES OF ACETATE METABOLISM ................................. 187 Glyoxylate Shunt ........................................................... 187 Other Ace Enzymes ........................................................... 188 Regulation of ace System(s) ........................................................... 189 CONCLUSIONS ........................................................... 189 ACKNOWLEDGMENTS ........................................................... 190 LITERATURE CITED ........................................................... 190 INTRODUCTION GENETIC AND BIOCHEMICAL ANALYSIS OF FATTY ACID OXIDATION Gram-negative bacteria such as Escherichia coli can uti- Most of our knowledge of the genetics and biochemistry of lize fatty acids and acetate as sole carbon and energy sources fatty acid degradation is derived from studies with E. coli. (30, 51, 76). After entry into the cell, fatty acids are either Growth of wild-type E. coli strains on fatty acids as sole catabolized or directly incorporated into complex lipids. carbon sources occurs only when the chain length of the Fatty acid degradation occurs by the cyclic 1-oxidation and fatty acid is 12 or more carbon atoms (long-chain fatty acids thiolytic cleavage of fatty acids, yielding several moles of [LCFAs]), and then only after a distinct lag period. The acetyl-coenzyme A (CoA). The acetyl-CoA produced is synthesis of at least five fatty acid-oxidative (FAO) enzymes further metabolized, yielding energy and precursors for (Fig. 1) is coordinately induced when LCFAs (C12 to C18) are cellular biosynthesis. A considerable body of information present in the growth media (51, 52, 76). The genetic studies regarding the physiology, genetics, and molecular biology of of Overath and co-workers (25, 30, 52) provided the first fatty acid and acetate metabolism has been amassed from evidence that the structural genes encoding the FAO en- studies with E. coli. These studies have enabled workers to zymes are located at several sites on the E. coli chromosome define the structural and regulatory genes required for the (Fig. 2) and make up a regulon (referred to as the fad and acetate. Studies the regulon). The fad regulon is primarily responsible for the catabolism of fatty acids involving transport, acylation, and 1-oxidation of medium-chain fatty use of recombinant DNA technology, coupled with studies acids (MCFAs) (C7 to C1l) and LCFAs. Growth of E. coli on that involve the purification and characterization of en- short-chain fatty acids (SCFAs) (C4 to C6) requires, in zymes, have enabled workers to correlate the structural addition to the FAO enzymes, two degradative enzymes genes (fad) with their respective gene products. One conse- (Fig. 3) encoded by the atoA and atoB genes (56). These quence of these efforts is that our understanding of fatty acid genes appear to be regulated by the atoC gene (56). transport processes has been significantly enhanced. These In this section we shall examine the genetic and molecular studies have also uncovered a regulatory interaction among information regarding the FAO and SCFA-degradative fatty acid degradation, acetate metabolism, and unsaturated (ATO) enzymes. In addition, we shall describe how SCFAs, fatty acid biosynthesis. MCFAs, and LCFAs are taken up by E. coli. Following the The purpose of this review is to illuminate studies that description of the FAO and ATO enzymes and transport have involved the examination of the molecular details of systems, we shall relate what is known about the mechanism fatty acid and acetate catabolism in E. coli. Although no by which the fad and ato structural genes are regulated. major reviews of the catabolism of fatty acids or acetate or both by this organism have been written, this article will not Studies with the FAO Enzyme System provide a comprehensive review on all aspects of these The basic features by which E. coli degrades fatty acids processes in E. coli. Instead, we will examine the literature are substantially similar to the ,B-oxidative pathways present on fatty acid and acetate catabolism, with emphasis on in mammalian and other eucaryotic organisms. This pathway studies in which genetic and biochemical manipulations were is a classic example of the oxidation of a series of homolo- used to define the structural and regulatory components of gous substrates through a series of homologous intermedi- these reactions. ates. Certain features of the pathway are illustrated in Fig. 1. With each turn of the ,8-oxidation cycle, the fatty acyl-CoA 179 180 NUNN MICROBIOL. REV. one molecule each of adenosine triphosphate (ATP) and CoA per molecule of free fatty acid activated. Overath et al. (51) suggested that E. coli has one acyl-CoA synthetase with out _ acd (X L) in _ ty anspor ---_ broad specificity for MCFAs and LCFAs. As supporting evidence, they showed that afadD mutant isolated in their '., I R _ OH laboratory lacks acyl-CoA synthetase activity for MCFAs ATP4X9 and LCFAs (51). In contrast to the hypothesis of Overath et AMP.PPtfacylCoA syfih (M D) al. (51), Samuel et al. (63), on the basis of their studies with R SCo partially purified acyl-CoA synthetase, suggested that the FAD y-O_A @hydrag (g E) acyl-CoA synthetase is a complex of two enzymes, one that activates MCFAs and another that activates LCFAs. To resolve whether E. coli has a single acyl-CoA synthetase cids-A3-trans-A'-en oAC heme with broad substrate specificity or multiple acyl-CoA H,anoyl-CoA hydra0aM (g B) synthetases with limited substrate specificity, Kameda and Nunn (29) purified to homogeneity the E. coli acyl-CoA OH 0 j R_.LS~WOH(D)-E ______-RRSCOA synthetase and found that the purified enzyme had broad substrate specificity for MCFAs and LCFAs. Although 3-hyW*C .dmgosue ( B) acyl-CoA synthetase was previously believed to be a mem- brane-associated protein, Kameda and Nunn demonstrated that over 90% of this enzyme was present in cytoplasmic CLASH 3-ke"*C bail (b A) fractions. The molecular weight of the native enzyme was approximately 130,000 and the subunit molecular weight O O determined by polyacrylamide gel electrophoresis in the -R_%-- SCtA+-Q presence of sodium dodecyl sulfate was 47,000. These ex- FIG. 1. Cyclic pathway of fatty acid degradation. Principle en- periments suggested that the enzyme may be a dimer or a zymes of the pathway are listed on the right, along with the of identical subunits respective structural genes ofthefad regulon. Acetyl-CoA is further trimer composed apparently (29). metabolized in the TCA Very little is known about the enzyme in E. coli respon- cycle. sible for the next step, acyl-CoA dehydrogenase. Although mutants (fadE) lacking this activity have been isolated and loses a two-carbon fragment as acetyl-CoA and reduces one their mutations have been mapped (30), it is not certain molecule of flavin adenine dinucleotide (FAD) (during the whether the loss of the dehydrogenase protein or that of an acyl-CoA dehydrogenase reaction) and one molecule of associated flavoprotein is responsible for the observed loss nicotinamide adenine dinucleotide (NAD) (during the 3- of activity. hydroxyacyl-CoA dehydrogenase reaction). Acetyl-CoA, The other ,3-oxidation enzymes are also cytoplasmic in E. produced in the CoA-dependent thiolytic cleavage, is further coli. The remaining 1-oxidation enzymes (Fig. 1) are part of metabolized in the tricarboxylic acid (TCA) cycle. The other a multienzyme complex that has broad substrate specificity. product of the cleavage step, a shortened fatty acyl-CoA In E. coli two proteins in the ,B-oxidative pathway are molecule, reenters the degradation cycle without further associated with a multienzyme complex which has a molec- activation (51). ular weight of 260,000 (4, 18, 50, 57, 58). Five FAO enzyme The first step of fatty acid degradation is the activation of the free fatty acid to an acyl-CoA thioester by acyl-CoA synthetase (fatty acid:CoA ligase, adenosine monophos- 0 0 phate [AMP]-forming; EC 6.2.1.3). This reaction requires * U 0 CH3CCH2C. CH3CH2CH2C0O Acetoacetate Butyrate out, ace - in short chain fatty acid transport? . fad_ ABe Acetoacety-CoA transferase (atoA& ato K) R CHkCSC CA 'I I 0 On v CH3CcHH2CSc CH3CH,cH2 Cc Thiolase (IQ B) 1IVCoASH11:CaAS-oxidation, enzymesc 0 ( EE, f B) u- FIG. 2. Genetic linkage map ofE. coli K-12
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