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  • Digitale Medien  (2)
  • Alanine dehydrogenase  (1)
  • Arginine  (1)
  • 1
    Digitale Medien
    Digitale Medien
    Pathways and regulation of N2, ammonium and glutamate assimilation by Clostridium formicoaceticum (1983)
    Springer
    Archives of microbiology 134 (1983), S. 167-169 
    Details
    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
    URL: http://dx.doi.org/10.1007/BF00407953
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  • 2
    Digitale Medien
    Digitale Medien
    Glycine fermentation by Clostridium histolyticum (1988)
    Springer
    Archives of microbiology 150 (1988), S. 11-14 
    Details
    ISSN: 1432-072X
    Schlagwort(e): Clostridium histolyticum ; Glycine ; Arginine ; Threonine ; Selenium ; Glycine reductase
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie
    Notizen: Abstract Clostridium histolyticum grew on glycine, arginine, or threonine as sole substrate. Arginine degradation preceded that of glycine and partially inhibited that of threonine when two amino acids were present. Each amino acid seemed to be individually catabolized, not by a Stickland type of reaction. Glycine fermentation required the presence of complex ingredients. Therefore, an effect of selenite on glycine catabolism could only be demonstrated after scavenging selenium contamination by preculturing Peptostreptococcus glycinophilus in that medium. C. acidiurici was not suited as selenium accumulating organism as C. histolyticum was inhibited by the residual uric acid. Arginine catabolism was unaffected by seleniuum depriviation. The labelling pattern obtained in acetate after incubation of C. histolyticum with [1-14C]- or [2-14C]glycine strongly indicated the metabolism of glycine via the glycine reductase pathway.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF00409710
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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