Degradation of 4-hydroxyphenylacetate by Xanthobacter 124X

Tweel, W.J.J. van den; Janssens, Rick; Bont, J.A.M. de

doi:10.1007/bf00428642

Cited by 25 publications

(6 citation statements)

References 21 publications

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“…Xanthobacter sp. strain 124X was isolated from an enrichment culture with sewage as the inoculum and with styrene as the carbon source (15). Pseudomonas putida LW4 was isolated on D-phenylglycine and has been described previously (16).…”

Section: Methodsmentioning

confidence: 99%

Metabolism of Styrene Oxide and 2-Phenylethanol in the Styrene-Degrading Xanthobacter Strain 124X

Hartmans¹,

Smits²,

Werf³

et al. 1989

Appl Environ Microbiol

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363

190

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Styrene oxide and 2-phenylethanol metabolism in the styrene-degrading Xanthobacter sp. strain 124X was shown to proceed via phenylacetaldehyde and phenylacetic acid. In cell extracts 2-phenylethanol was oxidized by a phenazine methosulfate-dependent enzyme, probably a pyrroloquinoline quinone enzyme. Xanthobacter sp. strain 124X also contains a novel enzymatic activity designated as styrene oxide isomerase. Styrene oxide isomerase catalyzes the isomerization of styrene oxide to phenylacetaldehyde. The enzyme was partially purified and shown to have a very high substrate specificity. Of the epoxides tested, styrene oxide was the only substrate transformed. The initial step in styrene metabolism in Xanthobacter sp. strain 124X is oxygen dependent and probably involves oxidation of the aromatic nucleus.

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Section: Methodsmentioning

confidence: 99%

Metabolism of Styrene Oxide and 2-Phenylethanol in the Styrene-Degrading Xanthobacter Strain 124X

Hartmans¹,

Smits²,

Werf³

et al. 1989

Appl Environ Microbiol

Self Cite

363

190

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“…The presence of homogentisic acid in the pathway has been confirmed by the high activity of homogentisate dioxygenase in the crude extract. It is known that homogentisic acid is degraded to maleylacetoacetate which isomerises to fumarylacetoacetate [14,18]. A good activity of glutathione dependent maleylacetoacetate isomerase was shown in the crude extract.…”

Section: Discussionmentioning

confidence: 97%

“…One unit of enzyme activity was defined as the amount of enzyme catalysing the conversion of 1 ~mol of homophthalate per minute under assay conditions. Phenylacetate hydroxylase, m-and p-hydroxy-phenylacetate hydroxylase were assayed spectrophotometrically by the NADH oxidation at 340 nm [14]. The reaction mixture (1 ml) contained 25 ~xl of crude extract, NADH (1 mM), FAD (1 raM), phosphate buffer (pH 7.00; 50 mM).…”

Section: Preparation Of Crude Extract and Enzyme Assaysmentioning

confidence: 99%

“…Homogentisate dioxygenase was assayed spectrophotometrically by measuring the increase in absorbance at 330 nm due to the formation of maleylacetoacetate [15]. Maleylacetoacetate isomerase was assayed according to the known method [14]. Homoprotocatechuate dioxygenase was assayed as described by Cooper and Skinner [16].…”

Section: Preparation Of Crude Extract and Enzyme Assaysmentioning

confidence: 99%

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Metabolic pathway of homophthalic acid in Pseudomonas alcaligenes

Karigar

1993

FEMS Microbiology Letters

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A microorganism capable of degrading homophthalic acid as a sole carbon source was isolated from garden soil. The strain was identified as Pseudomonas alcaligenes. The organism degraded homophthalate by a pathway which involved phenylacetate and p-hydroxyphenylacetate as intermediates. The intermediates have been identified by physico-chemical methods. A tentative pathway for the degradation of homophthalate is proposed based on isolation of intermediates, oxygen uptake studies and presence of enzymes involved in the degradation.

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“…The enzyme, which is also present in other bacteria, such as Xanthobacter spp. (59), and in higher organisms, catalyzes the formation of homogentisate from 4-hydrophenylpyruvate, a product which is formed following transamination of L-tyrosine (16,36). The finding that the presence of tyrosine increases the rate of pigment formation in Lly-positive Legionella strains and E. coli clones suggests that Lly and 4-hydroxyphenylpyruvate dioxygenase have similar functions.…”

Section: Discussionmentioning

confidence: 99%

Sequence determination and mutational analysis of the lly locus of Legionella pneumophila

et al. 1994

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The lly (legiolysin) locus codes for a 39-kDa protein which confers hemolysis, pigment production, and fluorescence on recombinant Escherichia coli K-12 clones carrying the lly gene. The nucleotide sequences of the lly genes from two Legionella pneumophila isolates were determined. The lly loci exhibited identical nucleotide sequences. They contained open reading frames of 348 amino acid residues, encoding proteins with a deduced molecular mass of 38.9 kDa. N-terminal amino acid sequencing further confirmed that the Lly protein corresponds to the open reading frame sequenced. The amino acid sequence of the Lly protein exhibits a high degree of homology with the sequences of the MelA protein responsible for melanin production in the freshwater bacterium Shewanella colwelliana and the 4-hydroxyphenylpyruvate dioxygenase of Pseudomonas spp. 4-Hydroxyphenylpyruvate dioxygenase is involved in the degradation of aromatic amino acids in various organisms. An Lly-negative mutant of L. pneumophila Philadelphia I derivative JR32 and an Lly-positive transcomplementant were constructed. The Lly-negative mutant lost the ability to produce brown pigment and to confer fluorescence but retained hemolysis. Introduction of a plasmid carrying the lly locus restored pigment production and fluorescence. Intracellular survival of L. pneumophila in U937 macrophage-like cells and in Acanthamoeba castellanii was not affected by mutagenization of the lly locus.

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Degradation of 4-hydroxyphenylacetate by Xanthobacter 124X

Cited by 25 publications

References 21 publications

Metabolism of Styrene Oxide and 2-Phenylethanol in the Styrene-Degrading Xanthobacter Strain 124X

Metabolism of Styrene Oxide and 2-Phenylethanol in the Styrene-Degrading Xanthobacter Strain 124X

Metabolic pathway of homophthalic acid in Pseudomonas alcaligenes

Sequence determination and mutational analysis of the lly locus of Legionella pneumophila

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