New aerobic benzoate oxidation pathway via benzoyl-coenzyme A and 3-hydroxybenzoyl-coenzyme A in a denitrifying Pseudomonas sp

Altenschmidt, Uwe; Oswald, B; Steiner, E; Herrmann, Heinz; Fuchs, Georg

doi:10.1128/jb.175.15.4851-4858.1993

Cited by 61 publications

(52 citation statements)

References 34 publications

(18 reference statements)

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“…Other sources of aromatic compounds include those produced from human activities such as agriculture (insecticides, herbicides, swine waste), domestic sources (sewage sludge), and industry (solvents, wood preservatives, detergents, oil) (Yi et al, 2000). The presence of these aromatic compounds in the environment presents significant problems, such as; they present a challenge to wastewater treatment plants, and they pollute groundwater and surface water (Altenschmidt et al, 1993). The most effective and economic way to clean up contaminated soil or groundwater in situ is biodegradation, provided that all contaminants (aliphatic or aromatic compounds) are mineralized in this process.…”

Section: Introductionmentioning

confidence: 99%

Optimizing the Biodegradation of 3,4-Dichlorobenzoic Acid by Corynebacterium jeikeium

Alqudah¹,

Tarawneh²,

Alkafaween³

et al. 2014

IJB

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Chlorinated benzoic acids (CBA) have been intentionally released to the environment due to their use in agriculture as herbicides or pesticides, or unintentionally because they are common metabolites in the aerobic transformation of many chlorinated pollutants. The biodegradation of 3,4-dichlorobenzoic acid compound was investigated by using Corynebacterium jeikeium bacteria, which was isolated from Petra wastewater plant in Jordan. 3,4-dichlorobenzoic acid compound (3,4-DCBA) was used as a sole carbon and energy source in minimal salt media (MSM). 3,4-DCBA was the most degradable compound among the Chlorobenzoic acid compounds tested by this bacteria. Different conditions such as substrate concentration, temperature, pH, agitation rate, carbon starvation and carbon adaptation were used to obtain optimal Biodegradation. The optimal conditions for the biodegradation were 3mM as substrate concentration and the culture conditions were also showed a significant impact on the ability of these cells to remove 3,4-DCBA. The optimum solution, temperature and agitation rate were 7.5, 37 °C and 150 rpm, respectively. Adaptation of the cells to 3,4-DCBA for 24 hr and 48 hr and cells starvation for 24 hr and 48 hr increased the initial degradation rate. The degradation ability was monitored through disappearance of the substrate from the medium and the measuring the accompanying chloride release. Corynebacterium jeikeium dioxygenases were physiologically induced by 3,4-DCBA compound. They were analyzed for both ortho or meta ring-cleavage of this aromatic compound. Only 1,2-dioxygenase activity was detected which mean that the cleavage is through the ortho pathway. This microorganism can be a valuable and promising candidate for use in the biotreatment of wastewater samples contaminated with 3,4-DCBA.

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Section: Introductionmentioning

confidence: 99%

Optimizing the Biodegradation of 3,4-Dichlorobenzoic Acid by Corynebacterium jeikeium

Alqudah¹,

Tarawneh²,

Alkafaween³

et al. 2014

IJB

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“…3-Hydroxybenzoate and gentisate are growth substrates of the strain, but catechol or protocatechuate are not. Cells grown with benzoate immediately used 3-hydroxybenzoate and gentisate [2]. In contrast, cells grown with 3-hydroxybenzoate or gentisate utilized instantaneously both 3-hydroxybenzoate and gentisate, whereas benzoate was consumed only after a lag phase.…”

Section: Properties Of the New Enzymementioning

confidence: 99%

“…NAD(P)H oxidation was followed spectrophotometrically at 380 nm. Samples (50 pl) were retrieved when the individual reactions were almost completed and [U-14C]benzoate and 14C-labelled products were analysed by HPLC as described [2]. The absorbance was monitored at 230 nm, radioactivity in the eluate was detected on-line by solidphase scintillation counting with a radioactivity monitoring analyzer.…”

Section: Methodsmentioning

confidence: 99%

“…3-Hydroxybenzoyl-CoA [9], 4-hydroxybenzoylCoA [lo] and 2-aminobenzoyl-CoA [11] were synthesized enzymically or chemically and purified as described. The purity of the CoA thioesters was checked by HPLC as described [2]. Cyclohex-1-ene-I-carboxyl-CoA was synthesized according to the general method described by Stockigt and Zenk [12].…”

Section: Methodsmentioning

confidence: 99%

“…[U-'4C]Benzoyl-CoA was synthesized enzymically and purified as described previously [2]. Benzoyl-CoA was synthesized from 50 mg coenzyme A and 17 mg benzoic acid anhydride by the method of Schachter and Taggert [8].…”

Section: Methodsmentioning

confidence: 99%

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Benzoyl‐Coenzyme‐A 3‐Monooxygenase, a Flavin‐Dependent Hydroxylase

Niemetz

Altenschmidt

Brucker

et al. 1995

European Journal of Biochemistry

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A new variant of aerobic benzoate degradation has been found in a denitrifying bacterium in which benzoyl‐CoA is the first intermediate [Altenschmidt, U., Oswald, B., Steiner, E., Herrmann, H. & Fuchs, G. (1993) New aerobic benzoate oxidation pathway via benzoyl‐coenzyme A and 3‐hydroxybenzoyl‐coenzyme A in a denitrifying Pseudomonas sp, J. Bacteriol. 175, 4851–4858)]. The initial reaction is catalyzed by benzoate‐CoA ligase (AMP‐forming), converting benzoate into benzoyl‐CoA. The next step is 3‐hydroxylation of benzoyl‐CoA to 3‐hydroxybenzoyl‐CoA catalyzed by a flavin‐nucleotide‐dependent monooxygenase, benzoyl‐CoA 3‐monooxygenase. This novel enzyme has been purified and studied. It is specific for NADPH and requires the presence of a flavin nucleotide for activity; both FAD or FMN function similarly well as cofactor. Only benzoyl‐CoA, but not benzoate, is hydroxylated. The protein is a monomer of Mr 65 000 and is induced when cells are grown aerobically with benzoate. 3‐Hydroxybenzoyl‐CoA is further hydroxylated para to the hydroxyl group affording 2,5‐dihydroxybenzoate (gentisate). This reaction requires another monooxygenase, 3‐hydroxybenzoyl‐CoA 6‐monooxygenase, which is unspecific with respect to the pyridine nucleotide. Cells contain a second 6‐monooxygenase activity which acts on free 3‐hydroxybenzoate. Based on these and other data, the outlines of the new aerobic benzoate pathway have been deduced. The proposed intermediates are benzoyl‐CoA, 3‐hydroxybenzoyl‐CoA, gentisate, maleylpyruvate, fumarylpyruvate and fumarate plus pyruvate.

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Thauera

Heider¹,

Fuchs²

2015

Bergey's Manual of Systematics of Archaea and Bacteria

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Thau' e.ra . M.L. fem. n. Thauera named after R.K. Thauer, a German microbiologist. Proteobacteria / Betaproteobacteria / Rhodocyclales / Rhodocyclaceae / Thauera Rods 0.5–1.4 × 1.4–3.7 μm , usually occurring singly. Some species exhibit great variability of cell form, from rods to coccoid forms of different sizes. Gram negative. Most species are motile . No resting stages known. Oxidase positive . Catalase positive. Colonies on minimal medium are nonpigmented. Aerobic , having a strictly respiratory type of metabolism; never fermentative. Molecular oxygen, nitrate, nitrite, and nitrous oxide are used as terminal electron acceptors , and the nitrogen oxides are reduced to N 2 O or N 2 ; one species also uses selenate, which is reduced to elemental Se. Optimal temperature 28–40°C. All species grow at pH 7.5; pH optima of different species range from 7.2 to 8.4. Chemoorganotrophic, using various organic acids, amino acids, and aromatic and aliphatic compounds as sole substrates. Only a few carbohydrates are utilized . Ammonium and nitrate salts can be used as sole nitrogen sources. No N 2 fixation known. Not proteolytic on casein or gelatin. Starch, cellulose, chitin, and agar are not hydrolyzed. Occur in polluted freshwater and wet soil environments and wastewater treatment plants. The mol % G + C of the DNA is : 64–69. Type species : Thauera selenatis Macy, Rech, Auling, Dorsch, Stackebrandt and Sly 1993, 140.

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New aerobic benzoate oxidation pathway via benzoyl-coenzyme A and 3-hydroxybenzoyl-coenzyme A in a denitrifying Pseudomonas sp

Cited by 61 publications

References 34 publications

Optimizing the Biodegradation of 3,4-Dichlorobenzoic Acid by Corynebacterium jeikeium

Optimizing the Biodegradation of 3,4-Dichlorobenzoic Acid by Corynebacterium jeikeium

Benzoyl‐Coenzyme‐A 3‐Monooxygenase, a Flavin‐Dependent Hydroxylase

Thauera

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