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  • 1
    Electronic Resource
    Electronic Resource
    Novel NADP-linked isocitrate dehydrogenase present in peroxisomes of n-alkane-utilizing yeast, Candida tropicalis: comparison with mitochondrial NAD-linked isocitrate dehydrogenase (1995)
    Springer
    Archives of microbiology 163 (1995), S. 104-111 
    Details
    ISSN: 1432-072X
    Keywords: Key words Peroxisomal NADP-linked isocitrate ; dehydrogenase ; NAD-linked isocitrate dehydrogenase ; Candida tropicalis ; Peroxisomes ; Mitochondria ; Cytosol
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Peroxisomal NADP-linked isocitrate dehydrogenase (Ps-NADP-IDH) was purified for the first time from Candida tropicalis cells grown on n-alkane as a carbon source, which was effective in proliferation of peroxisomes. The properties of Ps-NADP-IDH were compared with those of mitochondrial NAD-linked isocitrate dehydrogenase (Mt-NAD-IDH) purified from the cells grown on acetate, in which peroxisomes did not proliferate. Ps-NADP-IDH was a homod imer of identical subunits (45 kDa), while Mt-NAD-IDH was suggested to be a heterooctamer composed of two types of subunits with different molecular masses (41 and 38 kDa). Kinetic studies revealed that Ps-NADP-IDH gave Michaelis-Menten saturation curves against isocitrate and NADP concentrations, whereas Mt-NAD-IDH was an allosteric enzyme regulated by ATP, AMP, and citrate. Inhibition by 2-oxoglutarate, a precursor of glutamate, was observed only for Ps-NADP-IDH. Both enzymes were inhibited by concomitant addition of oxalacetate and glyoxylate. The function of Ps-NADP-IDH seems to be completely discriminated from that of Mt-NAD-IDH as reflected by their distinct subcellular localizations. Furthermore, the properties of Ps-NADP-IDH were also compared with those of other mitochondrial and cytosolic IDHs from sources reported previously.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00381783
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  • 2
    Electronic Resource
    Electronic Resource
    The upstream region of the isocitrate lyase gene (UPR-ICL) of Candida tropicalis induces gene expression in both Saccharomyces cerevisiae and Escherichia coli by acetate via two distinct promoters (1995)
    Springer
    Archives of microbiology 163 (1995), S. 322-328 
    Details
    ISSN: 1432-072X
    Keywords: Key words Isocitrate lyase ; n-Alkane-utilizable yeast ; Candida tropicalis ; Saccharomyces cerevisiae ; Promoters
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The upstream region of the isocitrate lyase gene (UPR-ICL, 1530bp) of an n-alkane-utilizable yeast, Candida tropicalis, induced gene expression in another yeast, Saccharomyces cerevisiae, when the yeasts were grown on acetate. Surprisingly, UPR-ICL displayed the same regulatory function in the bacterium Escherichia coli when grown on acetate. We determined the interesting nucleotide sequence of UPR-ICL. The deletion analysis of UPR-ICL in both cells revealed the presence of two distinct promoters: one was localized at –394 to –379 and regulated gene expression in S. cerevisiae; the other was located near the initiation codon and regulated gene expression in E. coli. The two promoter sequences were similar, but not identical to regulatory elements that have been previously reported in S. cerevisiae and E. coli, respectively. Accordingly, the possibility of novel regulatory mechanisms could not be excluded. This is an interesting example of the presence of distinct cis-acting regulatory elements responsible for the induction of gene expression in one gene by acetate in both S. cerevisiae and E. coli. Preservation of such promoters through evolution is also discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00404204
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  • 3
    Electronic Resource
    Electronic Resource
    Genes encoding peroxisomal enzymes are not necessarily assigned on the same chromosome of an n-alkane-utilizable yeast Candida tropicalis
    Amsterdam : Elsevier
    FEBS Letters 286 (1991), S. 61-63 
    Details
    ISSN: 0014-5793
    Keywords: Candida tropicalis ; Contour-clamped homogeneous electric field gel electrophoresis (CHEF) ; Coordinated expression. ; Peroxisome ; n-Alkane-assimilating yeast
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Physics
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/0014-5793(91)80940-5
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  • 4
    Electronic Resource
    Electronic Resource
    Peroxisomes of alkane-utilizing yeasts metabolic functions and practical aspectsPaper given at the Leipzig Symposium on Biotechnology 1982 Leipzig 21.-25. 9. 1982. (1983)
    Berlin : Wiley-Blackwell
    Acta Biotechnologica 3 (1983), S. 327-337 
    Details
    ISSN: 0138-4988
    Keywords: Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: One of the most striking features of alkane-grown yeast cells is conspicuous appearance of peroxisomes in harmony with a high level of catalase. This unique phenomenon was first demonstrated in the authors′ laboratory, and the metabolic functions of peroxisomes in yeasts utilizing alkanes has been estabilished with intact peroxisomes isolated by density gradient centrifugation. The organelles participate in the degradation of fatty acids derived from alkanes to C2-units and the synthesis of gluconeogenic intermediates from C2-units. The abundant appearance of peroxisomes in alkane-utilizing cells has allowed successful production of several useful enzymes including catalase, D-amino acid oxidase, uricase, acyl-CoA oxidase etc. Yeast cells will be an excellent system for investigation the functions and development of peroxisomes because biogenesis of the organelles is induced only by transferring the cells into alkane medium from glucose or ethanol medium.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/abio.370030405
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  • 5
    Electronic Resource
    Electronic Resource
    Bioconversion of lipophilic compounds by immobilized microbial cells in organic solvents (1981)
    Berlin : Wiley-Blackwell
    Acta Biotechnologica 1 (1981), S. 339-350 
    Details
    ISSN: 0138-4988
    Keywords: Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Microbial cells were gel-entrapped with photo-crosslinkable resin prepolymers or urethane prepolymers, respectively. The resulting gels have different tailor-made hydrophobic or hydrophilic character. They were used for successful bioconversion of hydrophobic steroids and terpenoids in watersaturated mixtures of organic solvents. The experiments show the influence of the hydrophobicity of the gels and the polarity of the solvent mixtures, respectively. Use of hydrophobic gels and less polar solvents is preferable for bioconversion of hydrophobic compounds. The selective formation of a desired product among diverse products from a single substrate by appropriate use of hydrophobic or hydrophilic gels is possible. In each case, tests should be made to select the appropriate gel and solvent mixture. Bioconversions tested are: dehydroepiandrosterone to 4-androstene-3,17-dione; cholesterol to cholestenone; β-sitosterol to β-sitostenone; stigmasterol to stigmastenone; pregnenolone to progesterone; testosterone to Δ1-dehydrotestosterone or 4-androstene-3,17-dione, respectively; all with immobilized cells of Nocardia rhodocrous; and stereoselective hydrolysis of dl-menthyl-succinate to yield l-menthol with immobilized cells of Rhodotorula minuta var. texensis.
    Additional Material: 10 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/abio.370010406
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