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At least 721 records · Page 40Linked to original sources
PubMed2005

Outlines of an "exploding" network of metabolites generated from the fluoroquinolone enrofloxacin by the brown rot fungus Gloeophyllum striatum.

Degradation of the veterinary fluoroquinolone antibiotic enrofloxacin (EFL) was studied with three strains of Gloeophyllum, basidiomycetous fungi thought to produce extracellular hydroxyl radicals. Metabolites generated in a mineral medium were analyzed by combined high-performance liquid chromatography/high-resolution electrospray ionization mass spectrometry. Their origin was inferred from peak doublets representing 12C and 14C isotopomers detected at a defined proportion. From each exact molecular mass, the molecular formula was derived for which the most probable chemical structure was postulated, using for guidance 18 known EFL metabolites. All supernatants provided similar metabolite patterns, with the most comprehensive consisting of 87 compounds. These metabolites belonged to five families headed by EFL, its oxidatively decarboxylated or defluorinated congeners, an isatin-, and an anthranilic acid-type derivative. Metabolites hydroxylated in the aromatic part suggested the formation of three catechols and two oxidizable ortho-aminophenol-type compounds. After oxidation to the respective ortho-quinones or ortho-quinone imines and oxidative ring cleavage at one of three alternative sites, the formation of various cis,cis-muconic acid-type derivatives is likely, one of which could be detected. Anthranilic acid-type compounds provided two additional sites for ortho-aminophenol formation and aromatic ring cleavage. An "exploding" network of diverse EFL congeners produced by Gloeophyllum suggests the broad utility of our model for studying biodegradation.

Basidiomycota↗
PubMedDate not supplied

[Azospirillum brasilense SP245 mutants in production of anthranilic and indolyl-3-acetic acids].

The mutants of Azospirillum brasilense Sp245 altered in the production of anthranilic (Ant) and indolyl-3-acetic (IAA) acids were selected after the chemical or transposon facilitated mutagenesis and divided into the following three classes: Ant+IAA+, Ant+IAA- and Ant-IAA-. A hypothesis on the existence of a pattern for tryptophan conversion to anthranilate that is different from the classic pattern, and on the connection of the indolyl-3-acetic synthesis with this process is suggested.

Azospirillum brasilense↗
PubMed1994

Structural characterization of polycyclic aromatic hydrocarbon dihydrodiol epoxide DNA adducts using matrix-assisted laser desorption/ionization Fourier transform mass spectrometry.

Matrix-assisted laser desorption/ionization (MALDI) Fourier transform ion cyclotron resonance mass spectrometry (FTMS) has been applied for the structural characterization of four polycyclic aromatic hydrocarbon dihydrodiol epoxide (PAHDE) adducts, including the 5,6-dimethylchrysene DE adduct of 2'-deoxyadenosine, the 5-methyl- and 5,6-dimethylchrysene DE adducts of 2'-deoxyguanosine, and the benzo[a]pyrene-DE adduct of 2'-deoxyguanosyl 3'-phosphate. Measurement of positive and negative ion mass spectra, accurate mass determinations, and CID experiments were carried out using 10-40 ng (20-70 pmol) of sample. An evaluation of five MALDI matrices showed that matrix selection can be used to control the degree of analyte fragmentation. Three MALDI matrices commonly used for the analysis of proteins (sinapinic acid, ferulic acid, 2,5-dihydroxybenzoic acid) gave positive ion adduct mass spectra showing protonated or sodiated molecular ions accompanied by abundant, structurally informative fragment ions. Fragmentation was significantly reduced when working with two matrices used for oligonucleotide analysis (an anthranilic-nicotinic acid mixture and 3-hydroxypicolinic acid). Using the CID capabilities of FTMS, isolation and activation of the MALDI-produced ions was used to provide additional structural information. While characteristic negative ions were not detected for the adenosyladduct, the guanosyl and guanosyl 3'-phosphate adducts gave [M-H]- ions when the anthranilic-nicotinic acid matrix mixture was used. The guanosyl adducts also showed [M-H-2H2O]- fragments. Compared with FAB or FAB-MS/MS for the analysis of underivatized PAH-DE adducts, MALDI-FTMS signals are long-lived, the direct MALDI-FT mass spectra show more structurally informative fragments, and accurate mass and CID experiments require lower sample quantities.

DNA↗
PubMed1986

[Participation of kynurenine and its derivatives in disorders of the cardiac rhythm].

The influence of tryptophan derivatives: L-kynurenine, 3-hydroxy-DL-kynurenine, kynurenic, xanthurenic, 3-hydroxy-anthranilic and quinolinic acids has been investigated in isolated frog heart. It has been established that L-kynurenine, 3-hydroxy-DL-kynurenine, xanthurenic acid and quinolinic acid at a concentration of 10(-6)-10(-3) mol/l initiate bradycardia. In some cases xanthurenic and quinolinic acids cause a one-minute cardiac arrest in early diastole. 3-hydroxy-anthranilic acid at a concentration of 10(-5) and 5 X 10(-5) mol/l produces premature beats and attacks of tachycardia. In the experiments, using 10(-6)-10(-3) mol/l of kynurenic acid, no impairment of the cardiac rhythm was observed in the isolated frog heart.

Animals↗
PubMed1980

Primary structure of Serratia marcescens anthranilate synthase component II.

The amino acid sequence of anthranilate synthase component II (AS II) from Serratia marcescens was determined. The cysteine residue essential for glutamine utilization was alkylated selectively by iodo [1-14C]acetamide prior to separation of the two protein components of anthranilate synthase. The isolated AS II then was subjected to cleavage by cyanogen bromide and by trypsin after citraconylation to obtain overlapping fragments. AS II is a single polypeptide chain of 192 residues having a calculated molecular weight of 20,956. The active site region is virtually identical to that of the Pseudomonas putida AS II enzyme (Kawamura, M., Keim, P.S., Goto, Y., Zalkin, H., and Heinrikson, R.L. (1978) J. Biol. Chem. 253, 4659-4668). Overall amino acid sequence similarity is 43%.

Amino Acid Sequence↗