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  • 1
    Electronic Resource
    Electronic Resource
    The smcL gene of Listeria ivanovii encodes a sphingomyelinase C that mediates bacterial escape from the phagocytic vacuole (1999)
    Oxford BSL : Blackwell Science Ltd
    Molecular microbiology 33 (1999), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: The ruminant pathogen Listeria ivanovii differs from Listeria monocytogenes in that it causes strong, bizonal haemolysis and a characteristic shovel-shaped co-operative haemolytic (‘CAMP-like’) reaction with Rhodococcus equi. We cloned the gene responsible for the differential haemolytic properties of L. ivanovii, smcL. It encodes a sphingomyelinase C (SMase) highly similar (〉 50% identity) to the SMases from Staphylococcus aureus (β-toxin), Bacillus cereus and Leptospira interrogans. smcL was transcribed monocistronically and was expressed independently of PrfA. Low-stringency Southern blots demonstrated that, within the genus Listeria, smcL was present only in L. ivanovii. We constructed an smcL knock-out mutant. Its phenotype on blood agar was identical to that of L. monocytogenes (i.e. weak haemolysis and no shovel-shaped CAMP-like reaction with R. equi ). This mutant was less virulent for mice, and its intracellular proliferation was impaired in the bovine epithelial-like cell line MDBK. The role of SmcL in intracellular survival was investigated using an L. monocytogenes mutant lacking the membrane-damaging determinants hly, plcA and plcB, being thus unable to grow intracellularly. Complementation of this mutant with smcL on a plasmid was sufficient to promote bacterial intracellular proliferation in MDBK cells. Transmission electron microscopy showed that SmcL mediates the disruption of the phagocytic vacuole and the release of bacteria into the cytosol. Therefore, L. ivanovii possesses a third phospholipase with membrane-damaging activity that, together with PlcA and PlcB, may act in concert with the pore-forming toxin Hly to mediate efficient escape from the vacuolar compartment. The 5′ end of smcL is contiguous with the internalin locus i-inlFE, which is also specific to L. ivanovii and is required for full virulence in mice. Thus, smcL forms part of a novel virulence gene cluster in Listeria that is species specific.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1365-2958.1999.01486.x
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  • 2
    Electronic Resource
    Electronic Resource
    Modeling Natural Attenuation of Total BTEX and Benzene Plumes with Different Kinetics (2004)
    Oxford, UK : Blackwell Publishing Ltd
    Ground water monitoring & remediation 24 (2004), S. 0 
    Details
    ISSN: 1745-6592
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Energy, Environment Protection, Nuclear Power Engineering , Geosciences
    Notes: Natural attenuation has emerged as a potential alternative for remediation of sites contaminated with fuel hydrocarbons. This paper compares the results from modeling the natural attenuation of BTEX (benzene, toluene, ethylbenzene, and xylene) at a coastal site to the results from a benzene model at the same site. Field data for total BTEX and benzene were used to develop model parameters for the Bioplume III site model. A first-order kinetics expression was used for benzene and an instantaneous expression for BTEX. Modeling results showed shorter cleanup timeframes for benzene than for BTEX. Natural attenuation cleanup times using BTEX and assimilative capacity are 47% to 90% higher than those for benzene alone. Cleanup times for benzene of ∼100 years were estimated from model predictions, whereas predicted cleanup times for BTEX varied between 150 and 200 years.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1745-6592.2004.tb01292.x
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  • 3
    Electronic Resource
    Electronic Resource
    Evaluation of BTEX Remediation by Natural Attenuation at a Coastal Facility (2002)
    Oxford, UK : Blackwell Publishing Ltd
    Ground water monitoring & remediation 22 (2002), S. 0 
    Details
    ISSN: 1745-6592
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Energy, Environment Protection, Nuclear Power Engineering , Geosciences
    Notes: Natural attenuation has emerged as a potential alternative for remediating sites contaminated with fuel hydrocarbons. This paper examines the viability of using attenuation through natural processes to remediate ground water at an industrial facility. The research combined field assessments with data analysis and modeling to evaluate plume stability and predict remediation times. Field data on natural attenuation indicate that BTEX contamination at the site is being attenuated at rates that vary within the range of 0.0001 to 0.0073/day. Stability analyses confirm that the BTEX plume has reached steady state. An analysis on mass flux showed that between 1979 and 1996, 95,000 pounds of BTEX were lost via biodegradation, while 8000 pounds were lost through other mechanisms. A first-order biodegradation rate of 0.0002/day for BTEX was obtained from the change in the total mass of dissolved BTEX with time. Cleanup times in excess of 200 years for the site were estimated using analytical modeling of natural attenuation, which agreed well with the remediation times estimated using the attenuation rates calculated for the site.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1745-6592.2002.tb00655.x
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  • 4
    Electronic Resource
    Electronic Resource
    Shelf space assigned to store and national brands: A neural networks analysis (2005)
    Bingley : Emerald
    International journal of retail and distribution management 33 (2005), S. 858-878 
    Details
    ISSN: 0959-0552
    Source: Emerald Fulltext Archive Database 1994-2005
    Topics: Economics
    Notes: Purpose - To empirically analyse the relationship between the shelf space assigned to brands and several factors related to store management. Design/methodology/approach - The data come from a study of 40 product categories in a sample of superstores in Spain. The variables are: shelf space occupied by private labels, private labels market share, number of promotions, assortment (number of brands and number of varieties) and prices gap between private labels and national brands. A neural network analysis is then applied to the data. Methodologically, this method is shown to have better predictive power than a multiple regression. Findings - There is a direct relationship between the space occupied by store brands and the market share, and an indirect relationship between the space and the price differential gap, the number of national brands and the range of choice. Research limitations/implications - The main limitation of this research is the time spent on collecting the data. Another limitation is that some variables have not been included in the study such as inventory. The conclusion can be used to account for behaviour of retailers in their outlets and could be used by manufacturers to determine which factors have an influence on the location of their brands on the shelves. Practical implications - It has practical implications for retailers because their "over-merchandizing" of own brands can damage the overall profitability of the category. On the other hand, national leading brands will have to invest more resources in advertising to sustain customer loyalty. Originality/value - This article shows the impact that store brand shelf space has on different variables related to profitability, market share, and assortment. It has value for three agents: academic researchers, manufacturers and retailers.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1108/09590550510629437
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  • 5
    Electronic Resource
    Electronic Resource
    Purification and biochemical characterization of gentisate 1,2-dioxygenase from Klebsiella pneumoniae M5a1 (1996)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 143 (1996), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract Gentisate 1,2-dioxygenase (E.C.I.14.13) was purified to homogeneity from Klebsiella pneumoniae M5a1, a soil bacterium able to degrade a great variety of aromatic compounds. The molecular mass of the purified holoenzyme was 159 kDa and its structure was deduced to be a tetramer with 38 kDa per subunit. Gentisate 1,2-dioxygenase appears to contain Fe2+ in its active site. The optimum temperature for enzyme activity was estimated to be 30 °C, the optimum pH values varied between 8 and 9 and the isoelectric point was 4.7. Gentisate dioxygenase exhibited typical saturation kinetics and had an apparent Km of 52 μM for gentisate. Its amino acid content was determined to be very similar to that of the enzyme from Pseudomonas acidovorans.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1996.tb08466.x
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  • 6
    Electronic Resource
    Electronic Resource
    Purification and characterization of the 3-hydroxybenzoate-6-hydroxylase from Klebsiella pneumoniae (1995)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 126 (1995), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract We isolated 3-hydroxybenzoate-6-hydroxylase (E.C. 1.14.13.), an inducible enzyme that catalyzed the para-hydroxylation of 3-hydroxybenzoate (3-HBA) to 2,5-dihydroxybenzoate, from Klebsiella pneumoniae. Although the enzyme was found to be mainly induced by its substrate, a coordinated induction of 3-hydroxybenzoate hydroxylase and gentisate dioxygenase was also observed in the presence of the product of the reaction. The purified enzyme was a monomer with a molecular mass of 42 000. It contained FAD as a prosthetic group, utilized NADH or NADPH with similar efficiencies and its activity was inhibited by Cu2+, Fe2+ and Hg2+. Other properties, such as induction mechanism and kinetic parameters were also studied. Moreover, for the first time the amino acid composition of a 3-hydroxybenzoate-6-hydroxylase was determined.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1995.tb07431.x
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  • 7
    Electronic Resource
    Electronic Resource
    Degradation of 3- and 4-hydroxybenzoate byKlebsiella pneumoniae (1991)
    Springer
    Applied microbiology and biotechnology 34 (1991), S. 677-682 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary Two different hydroxylases involved in benzenoid degradation have been isolated from Klebsiella pneumoniae and they can be differentially induced in the same strain. 3-Hydroxybenzoate-6-hydroxylase has an interesting biochemical mechanism and kinetic properties. 4-Hydroxybenzoate-1-hydroxylase activity is reported for the first time. The kinetic parameters of both enzymes have been studied.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00167922
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  • 8
    Electronic Resource
    Electronic Resource
    Purification and characterization of 4-hydroxybenzoate 3-hydroxylase from a Klebsiella pneumoniae mutant strain (1995)
    Springer
    Archives of microbiology 164 (1995), S. 70-77 
    Details
    ISSN: 1432-072X
    Keywords: Key words 4-Hydroxybenzoate ; Monooxygenase ; Hydroxylase ; Klebsiella pneumoniae
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Unlike the parent wild-type strain, the Klebsiella pneumoniae mutant strain MAO4 has a 4-HBA+ phenotype. The capacity of this mutant to take up and metabolize 4-hydroxybenzoate (4-HBA) relies on the expression of a permease and an NADPH-linked monooxygenase (4-HBA-3-hydroxylase). Both enzymes are normally expressed at basal levels, and only the presence of 4-HBA in the media enhances their activities. Strikingly, when the Acinetobacter calcoaceticus pobA gene encoding 4-hydroxybenzoate-3-hydroxylase was expressed in hydroxybenzoate K. pneumoniae wild-type, the bacteria were unable to grow on 4-HBA, suggesting that the main difference between the wild-type and the mutant strain is the capability of the latter to take up 4-HBA. 4-HBA-3-hydroxylase was purified to homogeneity by affinity, gel-filtration, and anion-exchange chromatography. The native enzyme, which appeared to be a dimer of identical subunits, had an apparent molecular mass of 80 kDa and a pI of 4.6. Steady-state kinetics were analyzed; the initial velocity patterns were consistent with a concerted substitution mechanism. The purified enzyme had 362 amino acid residues, and a tyrosine seemed to be involved in substrate activation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002030050237
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  • 9
    Electronic Resource
    Electronic Resource
    Molecular cloning and analysis of the genes encoding the 4-hydroxyphenylacetate hydroxylase from Klebsiella pneumoniae (1997)
    Springer
    Archives of microbiology 167 (1997), S. 160-166 
    Details
    ISSN: 1432-072X
    Keywords: Key words Catabolism ; Aromatic compounds ; Hydroxylases ; 4-Hydroxyphenylacetic acid ; 4-Hydroxyphenylacetate 3-hydroxylase ; Gene ; expression ; DNA sequence ; Amino acid sequence
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The Klebsiella pneumoniae genes encoding the hydroxylase involved in the meta-cleavage pathway of 4-hydroxyphenylacetic acid (4-HPA) were cloned, and the DNA fragment from the region essential for hydroxylase activity was sequenced. K. pneumoniae 4-HPA hydroxylase was composed of two proteins (HpaA and HpaH) with different molecular masses. HpaA seems to be a flavin-containing hydroxylase with a molecular mass of 58,781 Da. HpaH, with a molecular mass of 18,680 Da, seems to be a “helper” protein required for productive hydroxylation of the substrate. The hpa genes were expressed and the hydroxylase was active in Escherichia coli. Comparison of the enzyme with other monooxygenases indicates that K. pneumoniae 4-HPA hydroxylase is a member of a new family of hydroxylases.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002030050429
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  • 10
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    Purification and characterization of 4-hydroxybenzoate 3-hydroxylase from aKlebsiella pneumoniae mutant strain (1995)
    Springer
    Details
    Publication Date: 1995-07-01
    Print ISSN: 0302-8933
    Electronic ISSN: 1432-072X
    Topics: Biology
    Published by Springer
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