Control of Fatty Acid Metabolism I. Induction of the Enzymes of Fatty Acid Oxidation in
            <i>Escherichia coli</i>

Weeks, Gerald; Shapiro, Martin A.; Burns, R. O.; Wakil, Salih J.

doi:10.1128/jb.97.2.827-836.1969

Cited by 144 publications

(82 citation statements)

References 19 publications

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“…In bacteria, the production of methyl ketones via β‐oxidation and decarboxylase activity has not been demonstrated. The β‐oxidation pathway has been reported for many species, such as Pseudomonas fragi , Caulobacter crescentus , Corynebacterium , Escherichia coli and Lactobacillus leichmanii [22–25]. The only β‐decarboxylase enzymes described for bacteria related with the production of ketones are those of Clostridium acetobutylicum [26] and methylobacteria[27].…”

Section: Discussionmentioning

confidence: 99%

Decarboxylase activity involved in methyl ketone production byStaphylococcus carnosus833, a strain used in sausage fermentation

Fadda

Lebert

Leroy-Sétrin

et al. 2002

FEMS Microbiology Letters

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Staphylococcus carnosus strain 833, inoculated into sausage, increased the levels of methyl ketones which contributed to the cured aroma. These ketones were predicted to arise from incomplete beta-oxidation followed by a decarboxylation. To check this hypothesis, we measured the beta-decarboxylase activity in resting cells of S. carnosus grown in complex or in synthetic medium, using as substrate a beta-ketoacid, which can be an intermediate of the beta-oxidation pathway. This activity was present throughout the growth period. The enzyme appeared to be constitutive because no induction was observed. High aeration, a pH of 5 and the presence of nitrate promoted the production of methyl ketones.

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Section: Discussionmentioning

confidence: 99%

Decarboxylase activity involved in methyl ketone production byStaphylococcus carnosus833, a strain used in sausage fermentation

Fadda

Lebert

Leroy-Sétrin

et al. 2002

FEMS Microbiology Letters

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“…However, the measurement of acetyl-CoA was di¤cult because of the presence of thioesterase which hydrolysed the acetyl-CoA. The presence of a L-oxidation system has been described in Pseudomonas fragi [14], Caulobacter crescentus [15] Corynebacterium [8], E. coli [16] and L. leichmanii [12]. As in S. carnosus, the L-oxidation enzymes were induced by fatty acids.…”

Section: E¡ect Of Chain Length Of Methyl Esters On the L-oxidation Anmentioning

confidence: 99%

“…As in S. carnosus, the L-oxidation enzymes were induced by fatty acids. In E. coli and L. leichmanii, the enzymes are induced by fatty acids with 12 carbons [12,16] and in P. fragi by six carbons [14].…”

Section: E¡ect Of Chain Length Of Methyl Esters On the L-oxidation Anmentioning

confidence: 99%

Identification of β-oxidation and thioesterase activities in Staphylococcus carnosus 833 strain

Engelvin¹

2000

FEMS Microbiology Letters

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Staphylococcus carnosus 833, inoculated into sausage meat, increased the level of methyl ketones, which contributed to the cured aroma. These ketones can arise from incomplete L-oxidation followed by two enzymatic activities: a thioesterase and a decarboxylase. In this study we identified the L-oxidative pathway (through the measure of 3-hydroxyacyl-CoA dehydrogenase activity) and the thioesterase activity in extracts of S. carnosus cells grown in the presence of different methyl esters. The L-oxidative system was induced by methyl esters and highest induction was found with a 12-carbon substrate. It was specific for medium chain length fatty acyl CoA substrates. Its maximal activity was observed at the end of stationary growth phase. HPLC analyses of acyl-CoA after incubation of cell extracts with palmitoyl-CoA showed that the L-oxidation system released preferentially long chain hydroxyacyl-CoAs, enoyl-CoAs, and acyl-CoAs. The timecourse of intermediate formation indicated a precursor^product relationship indicative of a model of free intermediates which could be further deacylated by a thioesterase. The thioesterase activity was enhanced when S. carnosus was grown in the presence of methyl esters with at least 12 carbons and this enzyme was specific for short chain acyl-CoAs. The maximal activity was reached at the stationary growth phase. ß 2000 Published by Elsevier Science B.V. on behalf of the Federation of European Microbiological Societies. : S 0 3 7 8 -1 0 9 7 ( 0 0 ) 0 0 3 0 2 -5 * Corresponding author.

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“…FadR was first thought to be only a straightforward and rather boring repressor that regulated the ␤-oxidation pathway of Escherichia coli. FadR was detected genetically by Overath et al (1967; and Weeks et al (1969), who isolated mutants of E. coli that grew on a fatty acid of 10 carbon atoms (called decanoate). Wildtype E. coli strains fail to grow on these acids, while longer chain acids readily support growth.…”

Section: Fadrmentioning

confidence: 99%

FadR, transcriptional co‐ordination of metabolic expediency

Cronan

Subrahmanyam

1998

Molecular Microbiology

115

120

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SummaryFadR is an Escherichia coli transcriptional regulator that optimizes fatty acid metabolism in response to exogenously added fatty acids. Many bacteria grow well on long-chain fatty acids as sole carbon source, but at the expense of consuming a useful structural material. Exogenous fatty acids are readily incorporated into membrane phospholipids in place of the acyl chains synthesized by the organism, and phospholipids composed of any of a large variety of exogenously derived acyl chains make biologically functional membranes. It would be wasteful for bacteria to degrade fatty acids to acetyl-CoA and then use this acetyl-CoA to synthesize the same (or functionally equivalent) fatty acids for phospholipid synthesis. This line of reasoning suggests that bacteria might shut down endogenous fatty acid synthesis on the addition of long-chain fatty acids to the growth medium. Moreover, this shutdown could be closely coupled to fatty acid degradation, such that a bacterial cell would use a portion of the exogenous fatty acid for phospholipid synthesis while degrading the remainder to acetyl-CoA. To a degree, the bacterium could both have its cake (the acyl chains for phospholipid synthesis) and eat it (to form acetylCoA). This scenario turns out to be true in E. coli. The key player in this regulatory gambit is FadR, a transcription factor that acts both as a repressor of the fatty acid degradation and as an activator of fatty acid biosynthesis.

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Control of Fatty Acid Metabolism I. Induction of the Enzymes of Fatty Acid Oxidation in Escherichia coli

Cited by 144 publications

References 19 publications

Decarboxylase activity involved in methyl ketone production byStaphylococcus carnosus833, a strain used in sausage fermentation

Decarboxylase activity involved in methyl ketone production byStaphylococcus carnosus833, a strain used in sausage fermentation

Identification of β-oxidation and thioesterase activities in Staphylococcus carnosus 833 strain

FadR, transcriptional co‐ordination of metabolic expediency

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