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At least 19 recordsLinked to original sources
PubMed1978

Carbon substrate utilization studies of some cultures of Alcaligenes denitrificans, Alcaligenes faecalis, and Alcaligenes odorans isolated from clinical specimens.

One hundred and sixty-two cultures of Alcaligenes species (A. denitrificans, A. faecalis, and A. odorans) of clinical origin were characterized by routine diagnostic and carbon substrate utilization techniques. The microorganisms were tested for their ability to utilize a total of 188 substrates. Substrate utilization was assayed by (i) growth stimulation and (ii) substrate alkalinization. The A. denitrificans and A. odorans cultures had unique substrate utilization profiles for each species. The A. faecalis isolates were redefined by colonial morphology into two biotypes: (i) biotype I, morphologically and biochemically similar to the A. denitrificans cultures and (ii) biotype II, morphologically similar to the A. odorans cultures.

Alcaligenes↗
PubMed1990

Isolation and sequencing of the Alcaligenes denitrificans azurin-encoding gene: comparison with the genes encoding blue copper proteins from Pseudomonas aeruginosa and Alcaligenes faecalis.

The gene (azu) encoding azurin from Alcaligenes denitrificans has been cloned and sequenced. The gene codes for a pre-protein with a 19-aa signal peptide. Comparison with the sequences coding for the blue copper proteins from Pseudomonas aeruginosa and Alcaligenes faecalis reveals the presence of ntrA and fnr boxes in front of all three genes, instead of a regular [-10, -35]-promoter. In P. aeruginosa, the azu gene is terminated by a bidirectional terminator and flanked by open reading frames on the opposite strand.

Alcaligenes↗
PubMedDate not supplied

Mineralization of 2,4-dichlorophenoxyacetic acid (2,4-D) in soil inoculated with Pseudomonas cepacia DBO1(pRO101), Alcaligenes eutrophus AEO106(pRO101) and Alcaligenes eutrophus JMP134(pJP4): effects of inoculation level and substrate concentration.

Mineralization of 2,4-dichlorophenoxyacetic acid (2,4-D) by two Alcaligenes eutrophus strains and one Pseudomonas cepacia strain containing the 2,4-D degrading plasmids pJP4 or pRO101 (= pJP4::Tn1721) was tested in 50 g (wet wt) samples of non-sterile soil. Mineralization was measured as 14C-CO2 evolved during degradation of uniformly-ring-labelled 14C-2,4-D. When the strains were inoculated to a level of approximately 10(8) CFU/g soil, between 20 and 45% of the added 2,4-D (0.05 ppm, 10 ppm or 500 ppm) was mineralized within 72 h. Mineralization of 0.05 ppm and 10 ppm 2,4-D by the two A. eutrophus strains was identical and rapid whereas mineralization by P. cepacia DBO1(pRO101) occurred more slowly. In contrast, mineralization of 500 ppm 2,4-D by the two A. eutrophus strains was very slow whereas mineralization by P. cepacia DBO1 was more rapid. Comparison of 2,4-D mineralization at different levels of inoculation with P. cepacia DBO1(pRO101) (6 x 10(4), 6 x 10(6) and 1 x 10(8) CFU/g soil) revealed that the maximum mineralization rate was reached earlier with the high inoculation levels than with the low level. The kinetics of mineralization were evaluated by nonlinear regression analysis using five different models. The linear or the logarithmic form of a three-half-order model were found to be the most appropriate models for describing 2,4-D mineralization in soil. In the cases in which the logarithmic form of the three-half-order model was the most appropriate model we found, in accordance with the assumptions of the model, a significant growth of the inoculated strains.

2,4-Dichlorophenoxyacetic Acid↗
PubMed1991

Pyrimidine base and ribonucleoside utilization by the Pseudomonas alcaligenes group.

Pyrimidine base and ribonucleoside utilization was investigated in the two type strains of the Pseudomonas alcaligenes group. As sole sources of nitrogen, the pyrimidine bases uracil, thymine and cytosine as well as the dihydropyrimidine bases dihydrouracil and dihydrothymine supported the growth of Pseudomonas pseudoalcaligenes ATCC 17440 but neither these bases nor pyrimidine nucleosides supported Pseudomonas alcaligens ATCC 14909 growth. Ribose, deoxyribose, pyrimidine and dihydropyrimidine bases as well as pyrimidine nucleosides failed to be utilized by either P. pseudoalcaligenes or P. alcaligenes as sole carbon sources. The activities of the pyrimidine salvage enzymes nucleoside hydrolase, cytosine deaminase, dihydropyrimidine dehydrogenase and dihydropyrimidinase were detected in cell-free extracts of P. pseudoalcaligenes and P. alcaligenes. In P. pseudoalcaligenes, the levels of cytosine deaminase, dihydropyrimidine dehydrogenase and dihydropyrimidinase could be affected by the nitrogen source present in the culture medium.

Amidohydrolases↗
PubMed1975

Cellular fatty acids of Alcaligenes and Pseudomonas species isolated from clinical specimens.

The cellular fatty acid composition of 25 clinical isolates of Alcaligenes and Pseudomonas was determined by gas-liquid chromatography (GLC). The GLC fatty acid profiles of three species of Pseudomonas were markedly different from those of Alcaligenes. The most significant differences were the presence and relative amounts of hydroxy, branched-chain, and cyclopropane fatty acids. One of the major fatty acids in A. faecalis was a 17-carbon cyclopropane (17 delta) acid, whereas a 15-carbon branched-chain acid (13-methyl tetradecanoate) characterized isolates of P. putrefaciens. The determination of these fatty acids by GLC provides a rapid and specific means of distinguishing clinical isolates of Pseudomonas and Alcaligenes.

Alcaligenes↗
PubMed1978

Studies of relationship among terrestrial Pseudomonas, Alcaligenes, and enterobacteria by an immunological comparison of glutamine synthetase.

Antibody to purified glutamine synthetase from Escherichia coli was prepared and used for an immunological comparison of glutamine synthetases from species of Salmonella, Citrobacter, Enterobacter, Serratia, Proteus, Erwinia, Aeromonas, Pseudomonas, Acinetobacter, Xanthomonas, Alcaligenes, and Paracoccus. The results of Ouchterlony double diffusion experiments and quantitative microcomplement fixation studies indicated that the amino acid sequence of this enzyme was highly conserved in different organisms. The order of relationship to E. coli was found to be similar to that derived from immunological investigations of other enzymes. In addition, congruence was observed between ribosomal RNA homology and the results of the microcomplement fixation experiments. The results also suggested that some species of Alcaligenes were more closely related to species of Pseudomonas than to each other. Immunological comparisons of glutamine synthetases appear to be very useful for the elucidation of relationships among distantly related species and genera.

Alcaligenes↗
PubMed1978

The properties of adenosine triphosphatase from exponential and synchronous cultures of Alcaligenes eutrophus H16.

The properties of Alcaligenes eutrophus ATPase (adenosine triphosphatase) were investigated by using subcellular fractions prepared from cells growing in exponential and synchronous cultures. Both the soluble and membrane-bound forms of the ATPase were inhibited non-competitively (K(i) 142mum) by Nbf-Cl (4-chloro-7-nitrobenzofurazan), whereas only the membrane-bound enzyme was inhibited (non-competitive; K(i) 750mum) by NN'-dicyclohexylcarbodi-imide. Neither the activity of the ATPase nor its sensitivity to these two inhibitors varied during exponential growth. However, marked variations in ATPase activity were observed during synchronous growth, which were characterized by maxima at approx. 0.4 and 0.9 of a cell cycle and minima at approx. 0.1 and 0.6 of a cycle. Sensitivity to Nbf-Cl and NN'-dicyclohexylcarbodi-imide also varied during the cell cycle; maximum inhibition by the former occurred at approx. 0.4 and 0.9 of a cell cycle, whereas maximum inhibition by the latter was located at approx. 0.1 and 0.6 of a cell cycle. Proton conductance by whole cells was also periodic during the cell cycle, the lowest rates occurring at approx. 0.15 and 0.55 of a cycle and the highest rates at approx. 0.4 and 0.9 of a cycle, but -->H(+)/O quotients for the oxidation of endogenous substrates remained relatively constant and indicated the presence of four proton-translocating respiratory segments throughout the cell cycle. These results are discussed in terms of ATPase and respiratory-chain structure and function during the cell cycle of Alcaligenes eutrophus.

4-Chloro-7-nitrobenzofurazan↗
PubMed1992

Derived amino acid sequences of the nosZ gene (respiratory N2O reductase) from Alcaligenes eutrophus, Pseudomonas aeruginosa and Pseudomonas stutzeri reveal potential copper-binding residues. Implications for the CuA site of N2O reductase and cytochrome-c oxidase.

The nosZ genes encoding the multicopper enzyme nitrous oxide reductase of Alcaligenes eutrophus H16 and the type strain of Pseudomonas aeruginosa were cloned and sequenced for structural comparison of their gene products with the homologous product of the nosZ gene from Pseudomonas stutzeri [Viebrock, A. & Zumft, W. G. (1988) J. Bacteriol. 170, 4658-4668] and the subunit II of cytochrome-c oxidase (COII). Both types of enzymes possess the CuA binding site. The nosZ genes were identified in cosmid libraries by hybridization with an internal 1.22-kb PstI fragment (NS220) of nosZ from P. stutzeri. The derived amino acid sequences indicate unprocessed gene products of 70084 Da (A. eutrophus) and 70695 Da (P. aeruginosa). The N-terminal sequences of the NosZ proteins have the characteristics of signal peptides for transport. A homologous domain, extending over at least 50 residues, is shared among the three derived NosZ sequences and the CuA binding region of 32 COII sequences. Only three out of nine cysteine residues of the NosZ protein (P. stutzeri) are invariant. Cys618 and Cys622 are assigned to a binuclear center, A, which is thought to represent the CuA site of NosZ and is located close to the C terminus. Two conserved histidines, one methionine, one aspartate, one valine and two aromatic residues are also part of the CuA consensus sequence, which is the domain homologous between the two enzymes. The CuA consensus sequence, however, lacks four strictly conserved residues present in all COII sequences. Cys165 is likely to be a ligand of a second binuclear center, Z, for which we assume mainly histidine coordination. Of 23 histidine residues in NosZ (P. stutzeri), 14 are invariant, 7 of which are in regions with a degree of conservation well above the 50% positional identity between the Alcaligenes and Pseudomonas sequences. Conserved tryptophan residues are located close to several potential copper ligands. Trp615 may contribute to the observed quenching of fluorescence when the CuA site is occupied.

Alcaligenes↗
PubMed1976

Alcaligenes faecalis septicaemia.

A case of Alcaligenes faecalis septicaemia occurring after appendicectomy is described, and previous reports of this condition are briefly reviewed. Alcaligenes is frequently found in the faeces of healthy people and systemic infections appear to be very uncommon. Nevertheless, if the organism is cultured from the blood it should not be dismissed as a contaminant without careful investigation.

Adolescent↗
PubMed1991

[Intracellular L-aspartate-beta-decarboxylase of Pseudomonas sp. and Alcaligenes sp. and its immobilization].

Intracellular L-aspartate-beta-decarboxylase of Pseudomonas sp. and Alcaligenes sp. was isolated, purified and characterized. The cells were destroyed by ultrasonic treatment; the enzymes were precipitated by ammonium sulfate fractionation, dialyzed and lyophylized using Biogel P-150. After gel electrophoresis homogeneous enzyme preparations were obtained. The activity of L-aspartate-beta-decarboxylase is rather high--up to 92.1 U/min/mg of protein and is maximal at pH 5.5 and at temperatures of 45-55 degrees C. The Km and Vmax values for the Pseudomonas sp. enzyme are 0.1 M and 0.33 mM/min, respectively: those for the Alcaligenes sp. enzyme are 0.15 M and 1.0 mM/min, respectively. The results of amino acid analysis suggest that the enzymes slightly differ from one another with regard to aspartic and glutamic acid, alanine, valine and isoleucine content. Immobilization of the enzymes on various carriers was performed.

Alcaligenes↗
PubMedDate not supplied

[Attempt to establish genome similarity between Alcaligenes faecalis and several Gram-negative bacteria using the method of molecular hybridization of DNA to DNA].

The technique of DNA-DNA molecular hybridization was used to demonstrate the absence of genome similarity between Alcaligenes faecalis and gram-negative bacteria belonging to the genera Pseudomonas, Enterobacterium, Comamonas producing alkalis, and vibrions. Some similarity in the polynucleotide sequences was found between the DNA of the reper strain of Alcaligenes faecalis 45 (5--10% of homology) and the DNA of the culture belonging to the Achromobacter genus; therefore, the two genera may belong to one and the same family.

Alcaligenes↗
PubMed1990

Initial steps in the degradation of benzene sulfonic acid, 4-toluene sulfonic acids, and orthanilic acid in Alcaligenes sp. strain O-1.

Alcaligenes sp. strain O-1 grew with benzene sulfonate (BS) as sole carbon source for growth with either NH4+ or NH4+ plus orthanilate (2-aminobenzene sulfonate, OS) as the source(s) of nitrogen. The intracellular desulfonative enzyme did not degrade 3- or 4-aminobenzene sulfonates in the medium, although the enzyme in cell extracts degraded these compounds. We deduce the presence of a selective permeability barrier to sulfonates and conclude that the first step in sulfonate metabolism is transport into the cell. Cell-free desulfonation of BS in standard reaction mixtures required 2 mol of O2 per mol. One mol of O2 was required for a catechol 2,3-dioxygenase. When meta ring cleavage was inhibited with 3-chlorocatechol in desalted extracts, about 1 mol each of O2 and of NAD(P)H per mol of BS were required for the reaction, and SO3(2-) and catechol were recovered in high yield. Catechol was shown to be formed by dioxygenation in an experiment involving 18O2. 4-Toluene sulfonate was subject to NAD(P)H-dependent dioxygenation to yield SO3(2-) and 4-methylcatechol, which was subject to meta cleavage. OS also required 2 mol of O2 per mol and NAD(P)H for degradation, and SO3(2-) and NH4+ were recovered quantitatively. Inhibition of ring cleavage with 3-chlorocatechol reduced the oxygen requirement to 1 mol per mol of OS SO3(2-) (1 mol) and an unidentified organic intermediate, but no NH4+, were observed.

Alcaligenes↗
PubMed1991

Biodegradation of 4-chlorophenol by adsorptive immobilized Alcaligenes sp. A 7-2 in soil.

Alcaligenes sp. A 7-2 immobilized on granular clay has been applied in a percolator to degrade 4-chlorophenol in sandy soil. Good adsorption rates on granular clay were achieved using cell suspensions with high titres and media at pH 8.0. The influence of various parameters such as aeration rate, pH, temperature, concentration of 4-chlorophenol and size of inoculum on the degradation rate were investigated. During fed-batch fermentations under optimal culture conditions, concentrations of 4-chlorophenol up to 160 mg.l-1 could be degraded. Semicontinuous culture experiments demonstrated that the degradation potential in soil could be well established and enhanced by the addition of immobilized bacteria. Continuous fermentation was performed with varying 4-chlorophenol concentrations in the feed and different input levels. The maximum degradation rate was 1.64 g.l-1.day-1.

Alcaligenes↗
PubMed1992

Cloning and heterologous expression of a novel arylmalonate decarboxylase gene from Alcaligenes bronchisepticus KU 1201.

We have cloned and sequenced a DNA fragment that encodes the arylmalonate decarboxylase (AM-Dase) gene from Alcaligenes bronchisepticus KU 1201. The AMDase gene consists of an open reading frame of 720 nucleotides, which specifies a 240-amino-acid protein of relative molecular mass (M(r)) 24734. The M(r) deduced from the AMDase gene is in good agreement with that of the AMDase isolated from A. bronchisepticus. No TATA or TTGA sequence was observed within the cloned DNA fragment, but the fragment was expressed in Escherichia coli by the lac promoter of pUC19. The enzyme produced in E. coli has the same M(r) and the same enzyme activity as that purified from A. bronchisepticus. Comparison of the DNA sequence and the deduced amino acid sequence of AMDase with available DNA and amino acid sequence data bases revealed that there are no significant sequence homologies.

Alcaligenes↗
PubMed1992

Nucleotide sequence of the rpoN (hno) gene region of Alcaligenes eutrophus: evidence for a conserved gene cluster.

The nucleotide sequence of the rpoN gene, formerly designated hno, and flanking DNA regions of the aerobic hydrogen bacterium Alcaligenes eutrophus has been determined; rpoN codes for the RNA polymerase sigma factor sigma 54 involved in nitrogen regulation and diverse physiological functions of gram-negative bacteria. In A. eutrophus hydrogen metabolism is under control of rpoN. The Tn5-Mob insertion in a previously isolated pleiotropic mutant was mapped within the rpoN gene. The derived amino acid sequence of the A. eutrophus RpoN protein shows extensive homology to the RpoN proteins of other organisms. Sequencing revealed four other open reading frames: one upstream (ORF280) and three downstream (ORF130, ORF99 and ORF greater than 54) of the rpoN gene. A similar arrangement of homologous ORFs is found in the rpoN regions of other bacteria and is indicative of a conserved gene cluster.

Alcaligenes↗
PubMed1990

DNA topoisomerase I from Alcaligenes eutrophus H16.

Molecular and functional properties of DNA topoisomerase I isolated from a hydrogen-oxidizing bacterium, Alcaligenes eutrophus H16, were investigated. Under native conditions the enzyme forms a monomer with a relative molar mass of 98,500. A rod-like shape of the molecule was derived from the calculated frictional coefficient. The isoelectric point of the enzyme was determined to be in the range of 7.6-8.0. The enzyme activity is strictly Mg2+ dependent with an optimum at 3 mM Mg2+. The pH optimum ranges within 7.5-9.0. A. eutrophus DNA topoisomerase I activity is inhibited by M13 ssDNA, high ionic strength, polyamines, heparin and by a number of intercalating drugs.

Alcaligenes↗
PubMed1990

On the operon structure of the cfx gene clusters in Alcaligenes eutrophus.

Three transposon Tn5-induced mutants deficient in autotrophic CO2 fixation were isolated from a megaplasmid pHG1-cured strain of Alcaligenes eutrophus H16. Their phenotypes were initially characterized by their ability to form both key enzymes of the Calvin cycle, ribulose-1,5-bisphosphate carboxylase (Rubisco) and phosphoribulokinase (PRK). Since the transposon insertions were at different sites within the chromosomal cluster of cfx genes encoding Calvin cycle enzymes, the individual mutants showed different inactivation patterns for Rubisco and PRK synthesis. These data together with already known sequence data and the arrangement of cfx genes suggested that the Rubisco, fructose-1,6-bisphosphatase/sedoheptulose-1,7-bisphosphatase and PRK genes are constituents of the same operon. This was further confirmed by trans complementation analyses which indicated that the very similarly organized pHG1-encoded cfx genes additionally present in wild-type strain H16 are functional and also form a common operon. Each operon may also include a glyceraldehyde-3-phosphate dehydrogenase gene. Thus, the duplicated cfx operons of A. eutrophus H16 are large transcriptional units comprising at least about 8 kilobase pairs (kb) and possibly as much as 11 kb.

Alcaligenes↗