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  • Clostridium formicoaceticum  (2)
  • Alanine dehydrogenase  (1)
  • Antibiogram  (1)
  • 1
    Digitale Medien
    Digitale Medien
    Springer
    Archives of microbiology 134 (1983), S. 167-169 
    ISSN: 1432-072X
    Schlagwort(e): Nitrogenase ; Glutamine synthetase ; Glutamate synthase ; Glutamate dehydrogenase ; Asparagine synthetase ; Alanine dehydrogenase ; β-Methylaspartase ; Clostridium formicoaceticum
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie
    Notizen: Abstract Clostridium formicoaceticum possesses the following enzymes for the assimilation of N2 and NH 4 + : nitrogenase, glutamine synthetase, NADH- and NADPH-dependent glutamate synthase, NADH- and NADPH-dependent glutamate dehydrogenase, NADPH-dependent alamine dehydrogenase, and NH 4 + -dependent asparagine synthetase. Nitrogenase and glutamine synthetase are repressed and alanine dehydrogenase is induced by NH 4 + , while the synthesis of the other enzymes is not influenced by the extracellular NH 4 + level. Glutamate is degraded via glutamate mutase and β-methylaspartase.
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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  • 2
    Digitale Medien
    Digitale Medien
    Springer
    Archives of microbiology 119 (1978), S. 7-11 
    ISSN: 1432-072X
    Schlagwort(e): Clostridium formicoaceticum ; Fumarate reductase ; Peripheral enzyme ; Membrane protein
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie
    Notizen: Abstract When Clostridium formicoaceticum was grown on fumarate or l-malate crude cell extracts contained a high fumarate reductase activity. Using reduced methyl viologen as electron donor the specific activity amounted to 2–3.5 U per mg of protein. Reduced benzyl viologen, FMNH2 and NADH could also serve as electron donors but the specific activities were much lower. The NADH-dependent activity was strictly membrane-bound and rather labile. Its specific activity did not exceed 0.08 U per mg of particle protein. Fumarate reductase activity was also found in cells of C. formicoaceticum grown on fructose, gluconate, glutamate and some other substrates. The methyl viologen-dependent fumarate reductase activity could almost completely be measured with intact cells whereas only about 25% of the cytoplasmic acetate kinase activity was detected with cell suspensions. The preparation of spheroplasts from cells of C. formicoaceticum in 20 mM HEPES-KOH buffer containing 0.6 M sucrose and 1 mM dithioerythritol resulted in the specific release of 88% of the fumarate reductase activity into the spheroplast medium. Only small amounts of the cytoplasmic proteins malic enzyme and acetate kinase were released during this procedure. These results indicate a peripheral location of the fumarate reductase of C. formicoaceticum on the membrane.
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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  • 3
    Digitale Medien
    Digitale Medien
    Springer
    Archives of microbiology 138 (1984), S. 345-353 
    ISSN: 1432-072X
    Schlagwort(e): Clostridium acidiurici ; Clostridium cylindrosporum ; Clostridium purinolyticum ; Purine metabolism ; Selenite ; Antibiogram ; DNA homology ; Taxonomy
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie
    Notizen: Abstract Eleven strains of obligately purinolytic clostridia have been studied with respect to their assignment to the three type strains of Clostridium acidiurici, C. cylindrosporum, and C. purinolyticum. DNA/DNA-hybridization proved to be the method of choice for differentiation whereas phenotypic characteristics such as spore morphology, substrate spectra, nutritional requirements, product formation, and sensitivity against various antibiotics did not allow unequivocal identification. All strains depended on selenite for growth.
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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