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  • 1
    Electronic Resource
    Electronic Resource
    Purification and characterization of dihydroorotase from Pseudomonas putida (1995)
    Springer
    Archives of microbiology 164 (1995), S. 353-357 
    Details
    ISSN: 1432-072X
    Keywords: Key words Dihydroorotase ; Pyrimidine biosynthesis ; Pyrimidine degradation ; Pseudomonas putida
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Dihydroorotase was purified to homogeneity from Pseudomonas putida. The relative molecular mass of the native enzyme was 82 kDa and the enzyme consisted of two identical subunits with a relative molecular mass of 41 kDa. The enzyme only hydrolyzed dihydro-l-orotate and its methyl ester, and the reactions were reversible. The apparent K m and V max values for dihydro-l-orotate hydrolysis (at pH 7.4) were 0.081 mM and 18 μmol min–1 mg–1, respectively; and those for N-carbamoyl-dl-aspartate (at pH 6.0) were 2.2 mM and 68 μmol min–1 mg–1, respectively. The enzyme was inhibited by metal ion chelators and activated by Zn2+. However, excessive Zn2+ was inhibitory. The enzyme was inhibited by sulfhydryl reagents, and competitively inhibited by N-carbamoylamino acids such as N-carbamoylglycine, with a K i value of 2.7 mM. The enzyme was also inhibited noncompetitively by pyrimidine-metabolism intermediates such as dihydrouracil and orotate, with a K i value of 3.4 and 0.75 mM, respectively, suggesting that the enzyme activity is regulated by pyrimidine-metabolism intermediates and that dihydroorotase plays a role in the control of pyrimidine biosynthesis.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002030050274
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  • 2
    Electronic Resource
    Electronic Resource
    Synthesis of optically active ethyl 4-chloro-3-hydroxybutanoate by microbial reduction (1999)
    Springer
    Applied microbiology and biotechnology 51 (1999), S. 847-851 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract  A total of 400 yeast strains were examined for the ability to reduce ethyl 4-chloroacetoacetate (COBE) to ethyl 4-chloro-3-hydroxybutyrate (CHBE) by using acetone-dried cells in the presence of a coenzyme-recycling system in water/n-butyl acetate. We discovered some yeast strains that reduced COBE to (S)-CHBE. Heating of acetone-dried cells of the selected yeast strains increased the optical purity of the product. There may be several enzymes that can reduce COBE stereoselectively in the same yeast cells. The cultured broth of Candida magnoliae accumulated 90 g/l (S)-CHBE (96.6% enantiomeric excess, e.e.) in the presence of glucose, NADP and glucose dehydrogenase in n-butyl acetate. When these cells were heated, the stereoselectivity of the reduction increased to 99% e.e. (S)-CHBE is one of the useful chiral building blocks applicable to the synthesis of some pharmaceuticals. We expect that the cheap and industrial production of this important chiral compound will follow the discovery of this yeast strain.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002530051472
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  • 3
    Electronic Resource
    Electronic Resource
    Production of (R)-3-pentyn-2-ol through stereoinversion of racemic 3-pentyn-2-ol by Nocardia fusca AKU 2123 (1999)
    Springer
    Applied microbiology and biotechnology 52 (1999), S. 327-331 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract Wet cells of Nocardia fusca AKU 2123 are good catalysts for the production of (R)-3-pentyn-2-ol (PYOH) from (RS)-PYOH through a stereoinversion reaction. Under optimal conditions (350 mM potassium phosphate buffer, pH 8.0, 30% (w/v) wet cells, 0.12% NADPH, 10% glucose, and 30 U/ml glucose dehydrogenase) (R)-PYOH of high optical purity (98.7% e.e.) was produced from 2% (v/v) (RS)-PYOH with a yield of 70.4% by 140 h incubation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002530051527
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  • 4
    Electronic Resource
    Electronic Resource
    Gene cloning and overproduction of low-specificity d-threonine aldolase from Alcaligenes xylosoxidans and its application for production of a key intermediate for parkinsonism drug (2000)
    Springer
    Applied microbiology and biotechnology 54 (2000), S. 44-51 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract The dtaAX gene encoding a pyridoxal 5′-phosphate (pyridoxal-P)-dependent low-specificity d-threonine aldolase was cloned from the chromosomal DNA of Alcaligenes xylosoxidans IFO 12669. It contains an open reading frame consisting of 1,134 nucleotides corresponding to 377 amino acid residues. The predicted amino acid sequence displayed 54% identity with that of d-threonine aldolase from gram-positive bacteria Arthrobacter sp. DK-38, but showed no significant similarity with those of other known pyridoxal-P enzymes. This gram-negative bacterial enzyme was highly overproduced in recombinant Escherichia coli cells, and the specific activity of the enzyme in the cell extract was as high as 18 U/mg (purified enzyme 38.6 U/mg), which was 6,000 times higher than that from the wild-type Alcaligenes cell extract. The recombinant enzyme was thus feasibly purified to homogeneity by ammonium sulfate fractionation and DEAE-Toyopearl chromatography steps. The recombinant low-specificity d-threonine aldolase was shown to be an efficient biocatalyst for resolution of l-β-3,4-methylenedioxyphenylserine, an intermediate for production of a therapeutic drug for Parkinson's disease.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002539900301
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  • 5
    Electronic Resource
    Electronic Resource
    Reversible colour change in sputter-deposited Cu-Al-Ni film (1987)
    Springer
    Journal of materials science 6 (1987), S. 1267-1269 
    Details
    ISSN: 1573-4811
    Source: Springer Online Journal Archives 1860-2000
    Topics: Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01794584
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  • 6
    Electronic Resource
    Electronic Resource
    Ultrastructural visualization of concanavalin A binding sites using alkaline phosphatase-labeled Con A and ultrathin glycol methacrylate sections (1980)
    Springer
    Histochemistry and cell biology 67 (1980), S. 31-41 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary A method for the visualization of concanavalin A (Con A) binding sites by electron microscopy of glycol methacrylate sections is presented. This method, which is an application of the alkaline phosphatase-labeled Con A conjugate technique, solves the problems not only of limited penetration of chemicals into tissue blocks but also of injuries to tissue sections due to irritative reagents experienced in Con A-peroxidase staining. Glycol methacrylate sections are incubated successively with an alkaline phosphatase-labeled Con A solution and a lead citrate medium for the enzyme activity. Different kinds of tissues from adult rats have been used to test the method; tracheal cartilage, aorta and jejunum. The localization of Con A binding sites demonstrated by this method is consistent with the results of other published studies. Appropriate controls have been performed (ie., omission of the conjugated lectin, lectin plus its inhibitor) and these substantiate the specificity of the method.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00490085
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  • 7
    Electronic Resource
    Electronic Resource
    Lactonohydrolase-catalyzed optical resolution of pantoyl lactone: selection of a potent enzyme producer and optimization of culture and reaction conditions for practical resolution (1995)
    Springer
    Applied microbiology and biotechnology 44 (1995), S. 333-338 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract  A fungal lactonohydrolase catalyzes the stereospecific hydrolysis of the intramolecular ester bond of D-pantoyl lactone and is useful for optical resolution of racemic pantoyl lactone. High activity of this stereospecific hydrolysis reaction was found in several filamentous fungi belonging to the genera Fusarium, Gibberella and Cylindrocarpon through the screening in a variety of microorganisms. Fusarium oxysporum AKU 3702 showed high productivity of the enzyme and the cells containing the enzyme could be used repeatedly for this hydrolysis reaction. On incubation with the mycelia of this fungus, which had been cultivated in 3% glycerol, 0.5%Polypepton, 0.5% yeast extract and 0.5%corn steep liquor, pH 6.0, 46.0% of the racemic pantoyl lactone (700 mg/ml) was hydrolyzed and the optical purity of the pantoic acid formed was 96% enantiomeric excess for the D-isomer.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002530050563
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  • 8
    Electronic Resource
    Electronic Resource
    Heat-inducible expression system for a foreign gene in cultured tobacco cells using the HSP18.2 promoter of Arabidopsis thaliana (1995)
    Springer
    Applied microbiology and biotechnology 44 (1995), S. 466-472 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract  A system for the controlled expression of a foreign gene in cultured tobacco cells (Nicotiana tabacum, BY2) by temperature shift was constructed. A 925-base-pair (bp) DNA fragment containing the 5′-flanking region of a low-molecular-mass heat-shock protein gene (HSP18.2) of Arabidopsis thaliana was inserted upstream of the β-glucuronidase reporter gene (GUS). The resulting HSP18.2-GUS construct was introduced into BY2 cells by electroporation or Agrobacterium-mediated transformation. Transient expression of the HSP18.2 promoter in protoplasts was very low regardless of the heat shock. Although expression of the HSP18.2-GUS chimeric gene in the stable transformants of BY2 was hardly detected in culture at 25°C, the expression increased rapidly on the transcriptional level when the incubation temperature was shifted to 35–37°C. The optimal temperature for heat-shock induction was 37°C. After a 2-h incubation at 37°C, GUS activity was about 1000-fold greater than that before heat shock. The amount of GUS mRNA was maximum 2 h after heat shock, and then decreased gradually.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002530050583
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  • 9
    Electronic Resource
    Electronic Resource
    Lactonohydrolase-catalyzed optical resolution of pantoyl lactone: selection of a potent enzyme producer and optimization of culture and reaction conditions for practical resolution (1995)
    Springer
    Applied microbiology and biotechnology 44 (1995), S. 333-338 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract A fungal lactonohydrolase catalyzes the stereospecific hydrolysis of the intramolecular ester bond of d-pantoyl lactone and is useful for optical resolution of racemic pantoyl lactone. High activity of this stereospecific hydrolysis reaction was found in several filamentous fungi belonging to the genera Fusarium, Gibberella and Cylindrocarpon through the screening in a variety of microorganisms. Fusarium oxysporum AKU 3702 showed high productivity of the enzyme and the cells containing the enzyme could be used repeatedly for this hydrolysis reaction. On incubation with the mycelia of this fungus, which had been cultivated in 3% glycerol, 0.5% Polypepton, 0.5% yeast extract and 0.5% corn steep liquor, pH 6.0, 46.0% of the racemic pantoyl lactone (700 mg/ml) was hydrolyzed and the optical purity of the pantoic acid formed was 96% enantiomeric excess for the d-isomer.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00169925
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  • 10
    Electronic Resource
    Electronic Resource
    Heat-inducible expression system for a foreign gene in cultured tobacco cells using the HSP18.2 promoter of Arabidopsis thaliana (1995)
    Springer
    Applied microbiology and biotechnology 44 (1995), S. 466-472 
    Details
    ISSN: 1432-0614
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract A system for the controlled expression of a foreign gene in cultured tobacco cells (Nicotiana tabacum, BY2) by temperature shift was constructed. A 925-base-pair (bp) DNA fragment containing the 5′-flanking region of a low-molecular-mass heat-shock protein gene (HSP18.2) of Arabidopsis thaliana was inserted upstream of the β-glucuronidase reporter gene (GUS). The resulting HSP18.2-GUS construct was introduced into BY2 cells by electroporation or Agrobacterium-mediated transformation. Transient expression of the HSP18.2 promoter in protoplasts was very low regardless of the heat shock. Although expression of the HSP18.2-GUS chimeric gene in the stable transformants of BY2 was hardly detected in culture at 25°C, the expression increased rapidly on the transcriptional level when the incubation temperature was shifted to 35–37°C. The optimal temperature for heat-shock induction was 37°C. After a 2-h incubation at 37°C, GUS activity was about 1000-fold greater than that before heat shock. The amount of GUS mRNA was maximum 2 h after heat shock, and then decreased gradually.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00169945
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