Phenylacetate-coenzyme A ligase is induced during growth on phenylacetic acid in different bacteria of several genera

Vitovski, S

doi:10.1016/0378-1097(93)90477-j

Cited by 16 publications

(24 citation statements)

References 13 publications

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“…coli W and K-12, but not E. coli B and C, mineralize PA (Table 2) through a novel catabolic pathway which does not follow the conventional routes for the aerobic catabolism of aromatic compounds (such as those of E. coli for HPA, 3HPP, and PP degradation) and whose first step is the activation of PA to phenylacetyl-coenzyme A (PA-CoA) by the action of a PA-CoA ligase (94,328,182) (Fig. 5B).…”

Section: Pa Catabolic Pathwaymentioning

confidence: 99%

Biodegradation of Aromatic Compounds by Escherichia coli

Dı́az

Ferrández

Prieto

et al. 2001

Microbiol Mol Biol Rev

322

235

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Although Escherichia coli has long been recognized as the best-understood living organism, little was known about its abilities to use aromatic compounds as sole carbon and energy sources. This review gives an extensive overview of the current knowledge of the catabolism of aromatic compounds by E. coli. After giving a general overview of the aromatic compounds that E. coli strains encounter and mineralize in the different habitats that they colonize, we provide an up-to-date status report on the genes and proteins involved in the catabolism of such compounds, namely, several aromatic acids (phenylacetic acid, 3- and 4-hydroxyphenylacetic acid, phenylpropionic acid, 3-hydroxyphenylpropionic acid, and 3-hydroxycinnamic acid) and amines (phenylethylamine, tyramine, and dopamine). Other enzymatic activities acting on aromatic compounds in E. coli are also reviewed and evaluated. The review also reflects the present impact of genomic research and how the analysis of the whole E. coli genome reveals novel aromatic catabolic functions. Moreover, evolutionary considerations derived from sequence comparisons between the aromatic catabolic clusters of E. coli and homologous clusters from an increasing number of bacteria are also discussed. The recent progress in the understanding of the fundamentals that govern the degradation of aromatic compounds in E. coli makes this bacterium a very useful model system to decipher biochemical, genetic, evolutionary, and ecological aspects of the catabolism of such compounds. In the last part of the review, we discuss strategies and concepts to metabolically engineer E. coli to suit specific needs for biodegradation and biotransformation of aromatics and we provide several examples based on selected studies. Finally, conclusions derived from this review may serve as a lead for future research and applications

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Section: Pa Catabolic Pathwaymentioning

confidence: 99%

Biodegradation of Aromatic Compounds by Escherichia coli

Dı́az

Ferrández

Prieto

et al. 2001

Microbiol Mol Biol Rev

322

235

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“…Genetic studies have identified the genes involved in the upper pathway conversion of styrene to PAA in a number of styrene degraders of the genus Pseudomonas (Panke et al, 1998 ;Beltrametti et al, 1997 ;Marconi et al, 1996 ;Velasco et al, 1998). However, information regarding the lower pathway involved in PAA degradation is limited despite the identification of the first gene which encodes a phenylacetate-CoA (PACoA) ligase enzyme in a number of different Pseudomonas strains (Martinez-Blanco et al, 1990 ;Vitovski, 1993 ;Minambres et al, 1996 ;Velasco et al, 1998 ;Ferrandez et al, 1998). Potential regulatory genes styS and styR have also been isolated and sequence homology analyses have suggested strong links between these genes and those involved in other two-component regulatory systems (Velasco et al, 1998).…”

Section: Introductionmentioning

confidence: 99%

Transcriptional regulation of styrene degradation in Pseudomonas putida CA-3 The GenBank accession number for the sequence determined in this work is AF257095.

et al. 2001

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The styrene degradative pathway in Pseudmonas putida CA-3 has previously been shown to be divided into an upper pathway involving the conversion of styrene to phenylacetic acid and a lower pathway for the subsequent degradation of phenylacetic acid. It is reported here that expression of the regulatory genes styS and styR is essential for transcription of the upper pathway, but not for degradation of the lower pathway inducer, phenylacetic acid. The presence of phenylacetic acid in the growth medium completely repressed the upper pathway enzymes even in the presence of styrene, the upper pathway inducer. This repression is mediated at the transcription level by preventing expression of the styS and styR regulatory genes. Finally, an examination was made of the various stages of the diauxic growth curve obtained when P. putida CA-3 was grown on styrene together with an additional carbon source and it is reported that catabolite repression may involve a different mechanism to transcriptional repression by an additional carbon source.

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“…CoA ligase activities against PA have also been reported for other bacterial species (45). Moreover, there is evidence for a role of aromatic-CoA thioesters in the aerobic metabolism of 2-aminobenzoate (1), benzoate (B) (2), and 4-chlorobenzoate (26,37).…”

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confidence: 73%

Biochemical and Molecular Characterization of Phenylacetate-Coenzyme A Ligase, an Enzyme Catalyzing the First Step in Aerobic Metabolism of Phenylacetic Acid in Azoarcus evansii

Mohamed

2000

J Bacteriol

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Phenylacetate-coenzyme A ligase (PA-CoA ligase; AMP forming, EC 6.2.1.30), the enzyme catalyzing the first step in the aerobic degradation of phenylacetate (PA) in Azoarcus evansii, has been purified and characterized. The gene (paaK) coding for this enzyme was cloned and sequenced. The enzyme catalyzes the reaction of PA with CoA and MgATP to yield phenylacetyl-CoA (PACoA) plus AMP plus PPi. The enzyme was specifically induced after aerobic growth in a chemically defined medium containing PA or phenylalanine (Phe) as the sole carbon source. Growth with 4-hydroxyphenylacetate, benzoate, adipate, or acetate did not induce the synthesis of this enzyme. This enzymatic activity was detected very early in the exponential phase of growth, and a maximal specific activity of 76 nmol min ؊1 mg of cell protein ؊1 was measured. After 117-fold purification to homogeneity, a specific activity of 48 mol min ؊1 mg of protein Phenylacetic acid and its mono-or dihydroxylated derivatives are formed in nature from a wide variety of natural as well as synthetic compounds. Their microbial biodegradation and biotransformation have received the attention of many research groups for a long time. A number of bacteria and fungi have been isolated and studied to reveal the metabolic pathways of these acids under both aerobic and anaerobic growth conditions. Recently, the complete anaerobic metabolism of phenylacetic acid in the bacterium Thauera aromatica has been shown to follow a novel ␣-oxidation of the side chain of the coenzyme A (CoA)-activated acid, leading to the formation of the central intermediate benzoyl-CoA (Fig. 1). Further metabolism of benzoyl-CoA subsequently leads to the formation of three acetyl-CoA molecules and one CO 2 molecule (21,22,24,31,35,38,39).It has been established that the aerobic metabolism of most aromatic compounds starts by ring hydroxylation reactions carried out by mono-and dioxygenases. These oxic reactions, which are widely distributed in microorganisms, bring the aromatic rings of many aromatic compounds to the redox state present in catechol, protochatechuic and homoprotochatechuic acids, and gentisic and homogentisic acids. These compounds are considered common intermediates in the aerobic metabolism of most aromatic compounds (14,17).The aerobic metabolism of the hydroxylated derivatives of phenylacetic acid in many bacterial species follows this general pattern of oxic attack of the aromatic ring, leading to the formation of homogentisic acid (2,5-dihydroxyphenylactate) or homoprotocatechuic acid (3,4-dihydroxyphenylacetate) (4,5,12,13,28,34,41). However, none of the possible routes which might be expected for phenylacetic acid catabolism by analogy to those of its hydroxy derivatives appears to operate in phenylacetate (PA)-degrading bacteria. The inability to demonstrate the hydroxylation of PA by cell extracts of different bacteria in the presence of different cofactors has been reported by several research groups (7,8,10,15,25,41,43). Therefore, there is still uncertainty about the aerobic ...

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Phenylacetate-coenzyme A ligase is induced during growth on phenylacetic acid in different bacteria of several genera

Cited by 16 publications

References 13 publications

Biodegradation of Aromatic Compounds by Escherichia coli

Biodegradation of Aromatic Compounds by Escherichia coli

Transcriptional regulation of styrene degradation in Pseudomonas putida CA-3 The GenBank accession number for the sequence determined in this work is AF257095.

Biochemical and Molecular Characterization of Phenylacetate-Coenzyme A Ligase, an Enzyme Catalyzing the First Step in Aerobic Metabolism of Phenylacetic Acid in Azoarcus evansii

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