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  • 1
    Electronic Resource
    Electronic Resource
    Na+-dependent succinate uptake in Corynebacterium glutamicum (1991)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 77 (1991), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Succinate is effectively taken up by washed cells of Corynebacterium glutamicum. The apparent Km value of uptake is about 150 μM and the Vmax 4–7 nmol (mg dry weight)−1 min−1 and uptake can be competetively inhibited by fumarate and oxaloacetate. The activation energy was determined to be 50 kJ/mol. The transport activity is clearly dependent on the presence of Na+ ions in the incubation medium and on the membrane potential and has a pH optimum around 8.5. It is concluded that succinate is taken up in C. glutamicum via a specific carrier by a secondary active, Na+ coupled mechanism.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1991.tb04322.x
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  • 2
    Electronic Resource
    Electronic Resource
    Characterization of a secondary uptake system for l-glutamate in Corynebacterium glutamicum (1996)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 136 (1996), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract A new transport system for the uptake of l-glutamate was characterized in Corynebacterium glutamicum strain Δglu, in which the previously described binding protein-dependent glutamate uptake system is not present. Kinetic characterization revealed a highly specific secondary transport system, dependent on sodium ions. Glutamate uptake showed Michaelis-Menten kinetics, with a Km of 0.6 mM and a Vmax of 15 nmol min−1 (mg dw)−1. For the co-transported sodium ions, a relatively low Km of 3.3 mM was determined.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1996.tb08044.x
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  • 3
    Electronic Resource
    Electronic Resource
    Isoleucine excretion in Corynebacterium glutamicum: evidence for a specific efflux carrier system (1989)
    Springer
    Applied microbiology and biotechnology 31 (1989), S. 184-190 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary Corynebacterium glutamicum effectively secretes isoleucine when the precursor 2-ketobutyrate is added to the medium. Isoleucine secretion was studied under different conditions with respect to various parameters, i.e. rate of isoleucine excretion and uptake, concentration gradients of isoleucine, other amino acids and ions, and membrane potential. By comparing these parameters in the presence and absence of the amino acid precursor it has been shown that the efflux of isoleucine in C. glutamicum can neither be explained by a passive diffusion mechanism nor by a process involving functional inversion of the isoleucine uptake carrier. Based on our results concerning the distribution of metabolites and the kinetics of excretion we conclude that isoleucine is excreted in C. glutamicum by a separate, presumably active efflux carrier system.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00262460
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  • 4
    Electronic Resource
    Electronic Resource
    Glutamine uptake by a sodium-dependent secondary transport system in Corynebacterium glutamicum (1995)
    Springer
    Archives of microbiology 164 (1995), S. 98-103 
    Details
    ISSN: 1432-072X
    Keywords: Key words Glutamine ; Amino acid transport ; Solute ; uptake ; Corynebacterium glutamicum
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Corynebacterium glutamicum took up glutamine by a sodium-dependent secondary transport system. Both the membrane potential and the sodium gradient were driving forces. Glutamine uptake showed Michaelis-Menten kinetics, with a K m of 36 μM and a V max of 12.5 nmol min–1 (mg dry weight)–1 at pH 7. Despite a pH optimum in the alkaline range around pH 9, it was shown that uncharged glutamine is the transported species. The affinity for the cotransported sodium was relatively low; an apparent K m of 1.4 mM was determined. Among various substrates tested, only asparagine, when added in 50-fold excess, led to an inhibition of glutamine transport. It was concluded that glutamine uptake occurs via a specific transport system in symport with at least one sodium ion.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002030050240
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  • 5
    Electronic Resource
    Electronic Resource
    Transport of branched-chain amino acids in Corynebacterium glutamicum (1989)
    Springer
    Archives of microbiology 151 (1989), S. 238-244 
    Details
    ISSN: 1432-072X
    Keywords: Branched-chain amino acids ; Corynebacterium glutamicum ; Uptake ; Na+-symport ; Secondary active transport
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The transport of branched-chain amino acids was characterized in intact cells of Corynebacterium glutamicum ATCC 13032. Uptake and accumulation of these amino acids occur via a common specific carrier with slightly different affiniteis for each substrate (K m[Ile]=5.4 μM, K m[Leu]=9.0 μM, K m[Val]=9.5 μM). The maximal uptake rates for all three substrates were very similar (0.94–1.30 nmol/mg dw · min). The optimum of amino acid uptake was at pH 8.5 and the activation energy was determined to be 80 kJ/mol. The transport activity showed a marked dependence on the presence of Na+ ions and on the membrane potential, but was independent of an existing proton gradient. It is concluded, that uptake of branched-chain amino acid transport proceeds via a secondary active Na+-coupled symport mechanism.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00413136
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  • 6
    Electronic Resource
    Electronic Resource
    Carrier-mediated acetate uptake in Corynebacterium glutamicum (1991)
    Springer
    Archives of microbiology 155 (1991), S. 505-510 
    Details
    ISSN: 1432-072X
    Keywords: Acetate transport-uptake ; Corynebacterium glutamicum ; Secondary transport
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Acetate is effectively taken up by whole cells of Corynebacterium glutamicum via a specific carrier with a pH optimum of 8. The K m of acetate uptake was 50 μM and the V max 25–35 nmol/mg dw min. The activation energy was determined to be 70 kJ/mol. Acetate uptake was competitively inhibited by propionate with a K i of about 30 μM and blocked by addition of sulfhydryl reagents. The transport activity was clearly dependent on the membrane potential, but independent of the presence of Na+-ions. It is concluded that uptake of acetate proceeds by a secondary, proton coupled mechanism.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00244970
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  • 7
    Electronic Resource
    Electronic Resource
    Urea uptake and urease activity in Corynebacterium glutamicum (1998)
    Springer
    Archives of microbiology 169 (1998), S. 411-416 
    Details
    ISSN: 1432-072X
    Keywords: Key wordsCorynebacterium glutamicum ; Urea uptake ; Secondary transport ; Urease activity
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract When Corynebacterium glutamicum is grown with a sufficient nitrogen supply, urea crosses the cytoplasmic membrane by passive diffusion. A permeability coefficient for urea diffusion of 9 × 10–7 cm s–1 was determined. Under conditions of nitrogen starvation, an energy-dependent urea uptake system was synthesized. Carrier-mediated urea transport was catalyzed by a secondary transport system linked with proton motive force. With a K m for urea of 9 μM, the affinity of this uptake system was much higher than the affinity of urease towards its substrate (K m approximately 55 mM urea). The maximum uptake velocity depended on the expression level and was relatively low [2–3.5 nmol min–1 (mg dry wt.)–1].
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002030050591
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  • 8
    Electronic Resource
    Electronic Resource
    Glutamate excretion in Escherichia coli: dependency on the relA and spoT genotype (1995)
    Springer
    Archives of microbiology 164 (1995), S. 24-28 
    Details
    ISSN: 1432-072X
    Keywords: Key wordsEscherichia coli ; Stringent response ; Amino acid transport ; Glutamate excretion ; relA ; spoT
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Glutamate excretion due to amino acid starvation was investigated in "stringent" and "relaxed" strains of Escherichia coli. The observed excretion process is relA-dependent, carrier-mediated, and glutamate-specific. After induction, excretion was detected within less than 2 min and continued for more than 5 h with a rate of 7–10 nmol (mg dry weight)–1 min–1. Using carbonyl cyanide m-chlorophenylhydrazone or polymyxin B nonapeptide, together with valinomycin, it was shown that glutamate excretion is driven by the membrane potential.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002030050231
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  • 9
    Electronic Resource
    Electronic Resource
    Regulation of lysine excretion in the lysine producer strain Corynebacterium glutamicum MH 20-22B (1995)
    Springer
    Biotechnology letters 17 (1995), S. 927-932 
    Details
    ISSN: 1573-6776
    Source: Springer Online Journal Archives 1860-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary Lysine excretion by the producer strain Corynebacterium glutamicum MH 20-22B was analyzed in relation to the internal lysine concentration. In contrast to the wild-type, lysine excretion in the producer strain was allosterically regulated by internal lysine. The apparent Hill coefficient of 1.3 – 2.2 indicates the presence of at least two cooperatively interacting lysine binding sites.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00127428
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