scholarly journals Induction of primary alkylsulphatases and metabolism of sodium hexan-1-yl sulphate by Pseudomonas C12B

1974 ◽  
Vol 138 (1) ◽  
pp. 63-69 ◽  
Author(s):  
John W. Fitzgerald ◽  
Kenneth S. Dodgson ◽  
William J. Payne
Keyword(s):  
Sole Source ◽  
Bacterial Degradation ◽  
Alkyl Sulphate ◽  
Cell Extracts ◽  
The Media

Sodium hexan-1-yl sulphate and certain related alkyl sulphate esters have been shown to serve as inducers of the formation of primary alkylsulphatases (designated as P1 and P2) in Pseudomonas C12B. When the organism is grown on sodium hexan-1-yl [35S]sulphate as the sole source of sulphur or as the sole source of carbon and sulphur only the P2 alkylsulphatase is formed and inorganic 35SO42- is liberated into the media. Cell extracts contain this anion as the major 35S-labelled metabolite although two unidentified labelled metabolites as well as choline O-[35S]sulphate occur in trace quantities in some extracts. Dialysed cell extracts are capable of liberating inorganic 35SO42- from sodium hexan-1-yl [35S]sulphate without the need to include cofactors known to be required for the bacterial degradation of n-alkanes. The collective results suggest that sodium hexan-1-yl sulphate can act as an inducer of P1 alkylsulphatase formation without the need for prior metabolic modification of the carbon moiety of the ester.

scholarly journals The isolation and identification of 6-hydroxycyclohepta-1,4-dione as a novel intermediate in the bacterial degradation of atropine

1993 ◽  
Vol 293 (1) ◽  
pp. 115-118 ◽  
Author(s):  
B A Bartholomew ◽  
M J Smith ◽  
M T Long ◽  
P J Darcy ◽  
P W Trudgill ◽  
...  
Keyword(s):  
Growth Medium ◽  
Sole Source ◽  
Bacterial Degradation ◽  
Diauxic Growth ◽  
Growth Substrate ◽  
Isolation And Identification ◽  
Carbon And Nitrogen ◽  
Tropic Acid ◽  
Cell Extracts

Growth of Pseudomonas AT3 on the alkaloid atropine as its sole source of carbon and nitrogen is nitrogen-limited and proceeds by degradation of the tropic acid part of the molecule, with the metabolism of the tropine being limited to the point of release of its nitrogen. A nitrogen-free compound accumulated in the growth medium and was isolated and identified as 6-hydroxycyclohepta-1,4-dione. This novel compound is proposed as an intermediate in tropine metabolism. It served as a growth substrate for the organism and was also the substrate for an NAD(+)-linked dehydrogenase present in cell extracts. The enzyme was induced during the tropine phase of diauxic growth on atropine or during growth on tropine alone.

scholarly journals AzeR, a transcriptional regulator that responds to azelaic acid in Pseudomonas nitroreducens

Microbiology ◽  
2020 ◽  
Vol 166 (1) ◽  
pp. 73-84 ◽  
Author(s):  
Cristina Bez ◽  
Sree Gowrinadh Javvadi ◽  
Iris Bertani ◽  
Giulia Devescovi ◽  
Corrado Guarnaccia ◽  
...  
Keyword(s):  
Azelaic Acid ◽  
Type Species ◽  
Isocitrate Lyase ◽  
Model Organism ◽  
Transcriptional Regulator ◽  
Sole Source ◽  
Bacterial Degradation ◽  
Content Type ◽  
Link Type ◽  
Pseudomonas Nitroreducens

Azelaic acid is a dicarboxylic acid that has recently been shown to play a role in plant-bacteria signalling and also occurs naturally in several cereals. Several bacteria have been reported to be able to utilize azelaic acid as a unique source of carbon and energy, including Pseudomonas nitroreducens . In this study, we utilize P. nitroreducens as a model organism to study bacterial degradation of and response to azelaic acid. We report genetic evidence of azelaic acid degradation and the identification of a transcriptional regulator that responds to azelaic acid in P. nitroreducens DSM 9128. Three mutants possessing transposons in genes of an acyl-CoA ligase, an acyl-CoA dehydrogenase and an isocitrate lyase display a deficient ability in growing in azelaic acid. Studies on transcriptional regulation of these genes resulted in the identification of an IclR family repressor that we designated as AzeR, which specifically responds to azelaic acid. A bioinformatics survey reveals that AzeR is confined to a few proteobacterial genera that are likely to be able to degrade and utilize azelaic acid as the sole source of carbon and energy.

scholarly journals Novel Pathway for Alcoholic Fermentation of δ-Gluconolactone in the Yeast Saccharomyces bulderi

2002 ◽  
Vol 184 (3) ◽  
pp. 672-678 ◽  
Author(s):  
Johannes P. van Dijken ◽  
Arjen van Tuijl ◽  
Marijke A. H. Luttik ◽  
Wouter J. Middelhoven ◽  
Jack T. Pronk
Keyword(s):  
Pentose Phosphate Pathway ◽  
Alcoholic Fermentation ◽  
Kinase Activity ◽  
Glucose Dehydrogenase ◽  
Sole Source ◽  
Pentose Phosphate ◽  
Anaerobic Growth ◽  
Ph Values ◽  
Cell Extracts ◽  
Dehydrogenase Reaction

ABSTRACT Under anaerobic conditions, the yeast Saccharomyces bulderi rapidly ferments δ-gluconolactone to ethanol and carbon dioxide. We propose that a novel pathway for δ-gluconolactone fermentation operates in this yeast. In this pathway, δ-gluconolactone is first reduced to glucose via an NADPH-dependent glucose dehydrogenase (EC 1.1.1.47). After phosphorylation, half of the glucose is metabolized via the pentose phosphate pathway, yielding the NADPH required for the glucose-dehydrogenase reaction. The remaining half of the glucose is dissimilated via glycolysis. Involvement of this novel pathway in δ-gluconolactone fermentation in S. bulderi is supported by several experimental observations. (i) Fermentation of δ-gluconolactone and gluconate occurred only at low pH values, at which a substantial fraction of the substrate is present as δ-gluconolactone. Unlike gluconate, the latter compound is a substrate for glucose dehydrogenase. (ii) High activities of an NADP+-dependent glucose dehydrogenase were detected in cell extracts of anaerobic, δ-gluconolactone-grown cultures, but activity of this enzyme was not detected in glucose-grown cells. Gluconate kinase activity in cell extracts was negligible. (iii) During anaerobic growth on δ-gluconolactone, CO2 production exceeded ethanol production by 35%, indicating that pyruvate decarboxylation was not the sole source of CO2. (iv) Levels of the pentose phosphate pathway enzymes were 10-fold higher in δ-gluconolactone-grown anaerobic cultures than in glucose-grown cultures, consistent with the proposed involvement of this pathway as a primary dissimilatory route in δ-gluconolactone metabolism.

scholarly journals Characterization of S-Triazine Herbicide Metabolism by a Nocardioides sp. Isolated from Agricultural Soils

2000 ◽  
Vol 66 (8) ◽  
pp. 3134-3141 ◽  
Author(s):  
Edward Topp ◽  
Walter M. Mulbry ◽  
Hong Zhu ◽  
Sarah M. Nour ◽  
Diane Cuppels
Keyword(s):  
Agricultural Soils ◽  
Sole Source ◽  
Bacterial Strains ◽  
Corn Production ◽  
Whole Cells ◽  
Carbon And Nitrogen ◽  
Cell Extracts ◽  
Hydrolytic Reaction ◽  
Central Canada

ABSTRACT Atrazine, a herbicide widely used in corn production, is a frequently detected groundwater contaminant. Nine gram-positive bacterial strains able to use this herbicide as a sole source of nitrogen were isolated from four farms in central Canada. The strains were divided into two groups based on repetitive extragenic palindromic (rep)-PCR genomic fingerprinting with ERIC and BOXA1R primers. Based on 16S ribosomal DNA sequence analysis, both groups were identified as Nocardioides sp. strains. None of the isolates mineralized [ring-U-14C]atrazine. There was no hybridization to genomic DNA from these strains usingatzABC cloned from Pseudomonas sp. strain ADP or trzA cloned from Rhodococcus corallinus. S-Triazine degradation was studied in detail inNocardioides sp. strain C190. Oxygen was not required for atrazine degradation by whole cells or cell extracts. Based on high-pressure liquid chromatography and mass spectrometric analyses of products formed from atrazine in incubations of whole cells with H2 18O, sequential hydrolytic reactions converted atrazine to hydroxyatrazine and then to the end productN-ethylammelide. Isopropylamine, the putative product of the second hydrolytic reaction, supported growth as the sole carbon and nitrogen source. The triazine hydrolase from strain C190 was isolated and purified and found to have a Km for atrazine of 25 μM and a V max of 31 μmol/min/mg of protein. The subunit molecular mass of the protein was 52 kDa. Atrazine hydrolysis was not inhibited by 500 μM EDTA but was inhibited by 100 μM Mg, Cu, Co, or Zn. Whole cells and purified triazine hydrolase converted a range of chlorine or methylthio-substituted herbicides to the corresponding hydroxy derivatives. In summary, an atrazine-metabolizingNocardioides sp. widely distributed in agricultural soils degrades a range of s-triazine herbicides by means of a novel s-triazine hydrolase.

scholarly journals Chemically defined inducers of alkylsulphatases present in Pseudomonas C12B

1974 ◽  
Vol 138 (1) ◽  
pp. 53-62 ◽  
Author(s):  
Kenneth S. Dodgson ◽  
John W. Fitzgerald ◽  
William J. Payne
Keyword(s):  
Secondary Alcohol ◽  
Sodium Dodecyl ◽  
Nutrient Broth ◽  
Phase Cell ◽  
Alkyl Sulphate ◽  
Cell Extracts ◽  
Complex Process ◽  
Commercial Detergent ◽  
Process Studies ◽  
Long Chain

When Pseudomonas C12B is grown on nutrient broth to the stationary phase, cell extracts contain two secondary alkylsulphatases (S1 and S2) active towards potassium decan-5-yl sulphate but not towards potassium pentan-3-yl sulphate and one primary alkylsulphatase (P1) active towards sodium dodecan-1-yl sulphate (sodium dodecyl sulphate). When 10mm-sodium hexan-1-yl sulphate is included in the nutrient broth an additional primary alkylsulphatase (P2) is produced. The S1, S2, P1 and P2 enzymes are also present in extracts of cells grown on broth containing the commercial detergent Oronite, together with an additional secondary alkylsulphatase (S3) active towards pentan-3-yl sulphate as well as decan-5-yl sulphate. The P2 primary alkylsulphatase can be induced by a number of primary and secondary alkyl sulphate esters but the induction of the S3 enzyme appears to be a more specific and complex process. Studies on the ability of different fractions separated from Oronite to act as inducers suggest that the combination of a long-chain secondary alkyl sulphate(s) and a long-chain secondary alcohol(s) is responsible for the appearance of the S3 enzyme. Potassium hexadecan-2-yl sulphate or potassium tetradecan-2-yl sulphate, in combination with either hexadecan-2-ol or tetradecan-2-ol, can serve as inducers for the enzyme. Some characteristics of these specific inducer systems have been elucidated.

scholarly journals The influence of the culture media composition on the white phosphorus biodegradation by Aspergillus niger

2019 ◽  
Vol 58 (5) ◽  
pp. 1-23
Author(s):  
Anton Z. Mindubaev ◽  
◽  
Elena K. Badeeva ◽  
Salima T. Minzanova ◽  
Lubov G. Mironova ◽  
...  
Keyword(s):  
Aspergillus Niger ◽  
Culture Medium ◽  
Culture Media ◽  
Sole Source ◽  
Growth Conditions ◽  
White Phosphorus ◽  
The Media ◽  
Potential Basis ◽  
Living Organisms ◽  
First Time

The biodegradation of white phosphorus is undoubtedly an amazing illustration of the adaptability of living organisms to adverse environmental factors. In addition, it is a potential basis for the creation of new, breakthrough methods for detoxifying substances of the first class danger. However, establishing the fact of biological destruction is only half the battle. It is essential to optimize the growth conditions of microbial cultures and P4 biodegradation for industrial cultivation. The presented study compared the growth of Aspergillus niger strain AM1 in culture media varying in composition but containing P4 as the sole source of phosphorus. Of the ten media, two in which Aspergillus grew the fastest were selected. These media were concluded to be optimal for growth. Comparing the compositions of the media and the growth rate of Aspergillus in them, we found a key component that is a favorable factor for the growth of AM1 and the biodegradation of white phosphorus. This component was sodium nitrate (NaNO3). It has also been shown that copper sulphate (CuSO4) has no effect on the growth of Aspergillus in media with white phosphorus, regardless of the composition of these media. This result is in harmony with our previous findings. Furthermore, in the present work, attempts to increase the concentration of white phosphorus in the culture medium to values above 1% are described for the first time. For this purpose, we added the following solvents to the culture media: dimethyl sulfoxide (DMSO) and diesel, in which white phosphorus dissolves relatively well. Apparently, the presence of these substances adversely affects the growth of Aspergill. Therefore, the problem of further increasing the concentration of P4 remains an unanswered.

scholarly journals Degradation of Morpholine by an EnvironmentalMycobacterium Strain Involves a Cytochrome P-450

1998 ◽  
Vol 64 (1) ◽  
pp. 159-165 ◽  
Author(s):  
P. Poupin ◽  
N. Truffaut ◽  
B. Combourieu ◽  
P. Besse ◽  
M. Sancelme ◽  
...  
Keyword(s):  
Specific Inhibitor ◽  
Direct Analysis ◽  
Difference Spectrum ◽  
Sole Source ◽  
Spectrophotometric Analysis ◽  
Treatment Unit ◽  
H Nmr ◽  
Cell Extracts ◽  
Cytochrome P 450

A Mycobacterium strain (RP1) was isolated from a contaminated activated sludge collected in a wastewater treatment unit of a chemical plant. It was capable of utilizing morpholine and other heterocyclic compounds, such as pyrrolidine and piperidine, as the sole source of carbon, nitrogen, and energy. The use of in situ1H nuclear magnetic resonance (1H NMR) spectroscopy allowed the determination of two intermediates in the biodegradative pathway, 2-(2-aminoethoxy)acetate and glycolate. The inhibitory effects of metyrapone on the degradative abilities of strain RP1 indicated the involvement of a cytochrome P-450 in the biodegradation of morpholine. This observation was confirmed by spectrophotometric analysis and1H NMR. Reduced cell extracts from morpholine-grown cultures, but not succinate-grown cultures, gave rise to a carbon monoxide difference spectrum with a peak near 450 nm, which indicated the presence of a soluble cytochrome P-450. 1H NMR allowed the direct analysis of the incubation medium containing metyrapone, a specific inhibitor of cytochrome P-450. The inhibition of morpholine degradation was dependent on the morpholine/metyrapone ratio. The heme-containing monooxygenase was also detected in pyrrolidine- and piperidine-grown cultures. The abilities of different compounds to support strain growth or the induction of a soluble cytochrome P-450 were assayed. The results suggest that this enzyme catalyzes the cleavage of the C—N bond of the morpholine ring.

scholarly journals Dissimilation of cysteate via 3-sulfolactate sulfo-lyase and a sulfate exporter in Paracoccus pantotrophus NKNCYSA

Microbiology ◽  
2005 ◽  
Vol 151 (3) ◽  
pp. 737-747 ◽  
Author(s):  
Ulrike Rein ◽  
Ronnie Gueta ◽  
Karin Denger ◽  
Jürgen Ruff ◽  
Klaus Hollemeyer ◽  
...  
Keyword(s):  
Sole Source ◽  
Bacterial Spores ◽  
Utilization Rate ◽  
Transmembrane Helices ◽  
Terminal Electron Acceptor ◽  
Cell Extracts ◽  
Reverse Strand ◽  
Paracoccus Pantotrophus ◽  
High Level ◽  
Current Annotation

Paracoccus pantotrophus NKNCYSA utilizes (R)-cysteate (2-amino-3-sulfopropionate) as a sole source of carbon and energy for growth, with either nitrate or molecular oxygen as terminal electron acceptor, and the specific utilization rate of cysteate is about 2 mkat (kg protein)−1. The initial degradative reaction is catalysed by an (R)-cysteate : 2-oxoglutarate aminotransferase, which yields 3-sulfopyruvate. The latter was reduced to 3-sulfolactate by an NAD-linked sulfolactate dehydrogenase [3·3 mkat (kg protein)−1]. The inducible desulfonation reaction was not detected initially in cell extracts. However, a strongly induced protein with subunits of 8 kDa (α) and 42 kDa (β) was found and purified. The corresponding genes had similarities to those encoding altronate dehydratases, which often require iron for activity. The purified enzyme could then be shown to convert 3-sulfolactate to sulfite and pyruvate and it was termed sulfolactate sulfo-lyase (Suy). A high level of sulfite dehydrogenase was also induced during growth with cysteate, and the organism excreted sulfate. A putative regulator, OrfR, was encoded upstream of suyAB on the reverse strand. Downstream of suyAB was suyZ, which was cotranscribed with suyB. The gene, an allele of tauZ, encoded a putative membrane protein with transmembrane helices (COG2855), and is a candidate to encode the sulfate exporter needed to maintain homeostasis during desulfonation. suyAB-like genes are widespread in sequenced genomes and environmental samples where, in contrast to the current annotation, several presumably encode the desulfonation of 3-sulfolactate, a component of bacterial spores.

Effect of naturally occurring apatites on growth and morphology of algae

1977 ◽  
Vol 23 (9) ◽  
pp. 1188-1196 ◽  
Author(s):  
E. A. H. Smith ◽  
C. I. Mayfield ◽  
P. T. S. Wong ◽  
B. A. Silverberg
Keyword(s):  
Fibrous Material ◽  
Phase Contrast ◽  
Algal Species ◽  
Sole Source ◽  
Naturally Occurring ◽  
High Nutrient ◽  
Marked Preference ◽  
The Media ◽  
Total P ◽  
Algal Cultures

Crystals (30–100 μm) of selected naturally occurring apatite (Ca10 (PO4)6(OH, F)2) samples were added to P-free (<0.001 μg/ml total P) Bristol's medium (1–1000 μg/ml of apatite) as the sole source of ortho-PO43− The media were inoculated with washed, non-axenic cells of three chlorophycean algal species cultivated under PO43−-deficient conditions. Phase-contrast and scanning electron microscopy revealed that at low slurry densities (1–10 μg/ml of apatite), Ankistrodesnuis braunii (ATCC 2744) cells were morphologically distorted. At concentrations of 100 and 1000 μg/ml of apatite, more than 85% of the cells had undergone autospore formation within 7–10 days of incubation at 20 °C. Most autospores formed failed to germinate under high nutrient conditions. Scenedesmus longus (No. 1236) formed colonies when cultivated in Bristol's medium but daughter ceils displayed a Chodatella-like unicellular morphology when grown in apatite media. Test algal species (Chlamydomonas dysosmos, S. longus, A. braunii) showed a marked preference for growth on apatite crystals over non-nutritive surfaces. Unialgal and mixed-algal cultures produced an extensive matrix of extracellular fibrous material in response to growth on crystals at concentrations greater than 10 μg/ml of apatite.

scholarly journals Four Bacillus sp. soil isolates capable of degrading phenol, toluene, biphenyl, naphthalene and other aromatic compounds exhibit different aromatic catabolic potentials

2011 ◽  
Vol 63 (4) ◽  
pp. 1057-1067 ◽  
Author(s):  
Lidija Djokic ◽  
Tanja Narancic ◽  
Jasmina Nikodinovic-Runic ◽  
Sanja Bajkic ◽  
Branka Vasiljevic
Keyword(s):  
Aromatic Compounds ◽  
Sole Source ◽  
Phenol Hydroxylase ◽  
Ph Effects ◽  
Bacillus Sp ◽  
Cell Extracts ◽  
Catechol 1,2 Dioxygenase ◽  
Similar Range ◽  
Specific Activities ◽  
Catechol Dioxygenases

Two novel Bacillus sp. were isolated from a soil sample from a bank of the Tamis river in close proximity to a petrochemical facility. They were capable of utilizing a broad range of aromatic compounds as a sole source of carbon and energy (including phenol, benzene, toluene, biphenyl, naphthalene). The isolates were designated as Bacillus sp. TN41 and TN42, based on their 16S rDNA sequence. Their catabolic potential was compared to two Bacillus sp. strains (PS1 and PS11) isolated from the rhizosphere of the endemorelict plant Ramonda serbica. Specific activities of phenol hydroxylase, catechol 1,2-dioxygenase and catechol 2,3-dioxygenase were analyzed from crude cell extracts of the isolates, as well as the temperature and pH effects on enzyme activity. Although all four isolates had the ability to degrade a similar range of aromatic compounds, the specific activities of the enzymes indicative of aromatic compound catabolism of TN isolates were 2 to 90-fold lower compared to the PS isolates. Phenol hydroxylase and catechol dioxygenases exhibited broad temperature (10?C-80?C) and pH (4-9) activity ranges in all four Bacillus isolates. While phenol inhibited both phenol hydroxylase and catechol dioxygenases in the TN strains, it was an inducer for phenol hydroxylase in the PS strains.

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