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  • Glycine decarboxylase  (2)
  • Xanthine dehydrogenase  (2)
  • Clostridium purinolyticum  (1)
  • 1
    Electronic Resource
    Electronic Resource
    Selenium requirement for active xanthine dehydrogenase from Clostridium acidiurici and Clostridium cylindrosporum (1979)
    Springer
    Archives of microbiology 121 (1979), S. 255-260 
    Details
    ISSN: 1432-072X
    Keywords: Purine fermentation ; Xanthine dehydrogenase ; Selenium ; Tungsten ; Molybdenum ; Clostridium acidiurici ; Clostridium cylindrosporum
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The xanthine dehydrogenase of Clostridium acidiurici and C. cylindrosporum was assayed with methyl viologen as acceptor. In C. acidiurici the basal activity level was about 0.3 μmol/min x mg of protein. Cells grown on uric acid in the presence of 10-7 M selenite showed a 14-fold increase in xanthine dehydrogenase activity, which decreased with higher selenite concentrations (10-5 M). The supplementation with 10-7 M molybdate or tungstate was without effect. High concentrations of tungstate decreased the xanthine dehydrogenase if selenite was also present. In comparison, high concentrations of molybdate affected only a small decrease in activity level at the optimal concentration for selenite and relieved to some degree the inhibitory effect of 10-5 M selenite. With hypoxanthine and xanthine as substrates for growth again only the addition of selenite was necessary to show a similar increase in xanthine dehydrogenase activity. C. acidiurici could be grown in a mineral medium. Both xanthine dehydrogenase and formate dehydrogenase exhibited the highest level of activity if selenite and tungstate were present in that medium. In C. cylindrosporum the basal activity level of xanthine dehydrogenase was about 0.95 μmol/min x mg of protein. The addition of 10-7 M selenite to the growth medium increased the activity level about 3-fold, but the highest level (3.7 U/mg) was reached if 10-7 M molybdate was also added. The presence of tungstate resulted in a decreased enzyme activity.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00425064
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Comparative studies on physiology and taxonomy of obligately purinolytic clostridia (1984)
    Springer
    Archives of microbiology 138 (1984), S. 345-353 
    Details
    ISSN: 1432-072X
    Keywords: Clostridium acidiurici ; Clostridium cylindrosporum ; Clostridium purinolyticum ; Purine metabolism ; Selenite ; Antibiogram ; DNA homology ; Taxonomy
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: 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.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00410902
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Eubacterium angustum sp. nov., a Gram-positive anaerobic, non-sporeforming, obligate purine fermenting organism (1984)
    Springer
    Archives of microbiology 140 (1984), S. 2-8 
    Details
    ISSN: 1432-072X
    Keywords: Eubacterium angustum ; Purine metabolism ; Xanthine dehydrogenase ; Selenium
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A strictly anaerobic, uric acid, xanthine, and guanine fermenting bacterium was isolated from sewage sludge requiring thiamine as a vitamin. Acetate, formate, ammonia and CO2 were products. Cells were Gram-positive, straight rods, 3 to 6.5 μm long and 1.1 to 1.5 μm wide. They were non-motile, however, possessed flagella. Spore formation could not be obtained. The guanine-plus-cytosine content (G+C) of its deoxyribonucleic acid was 40.3 mol%. Based on these features, the organism belongs to the genus Eubacterium. Due to its restricted substrate spectrum and its inability to utilize arginine or to form cytochromes like E. lentum, this organism did not resemble any of the previously described species of Eubacterium. Therefore, it is proposed to form a new species Eubacterium angustum sp. nov.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00409763
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    Paper (German National Licenses)
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  • 4
    Electronic Resource
    Electronic Resource
    Peripheral localization of the dihydrolipoamide dehydrogenase in the purinolytic anaerobe Clostridium cylindrosporum (1991)
    Springer
    Archives of microbiology 155 (1991), S. 412-414 
    Details
    ISSN: 1432-072X
    Keywords: Clostridium cylindrosporum ; Dihydrolipoamide dehydrogenase ; Glycine decarboxylase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Immunocytochemical localization experiments were performed with antibodies raised against the dihydrolipoamide dehydrogenase protein (P3) of the glycine decarboxylase complex from clostridium cylindrosporum using the low-temperature procedure and protein A-gold technique. An association with the cytoplasmic membrane was indicated to about 65 (±10) % when cells were analyzed from the logarithmic growth phase. The unusual peripheral localization is discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00243464
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    Paper (German National Licenses)
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  • 5
    Electronic Resource
    Electronic Resource
    Immunocytochemical localization of proteins P1, P2, P3 of glycine decarboxylase and of the selenoprotein PA of glycine reductase, all involved in anaerobic glycine metabolism of Eubacterium acidaminophilum (1989)
    Springer
    Archives of microbiology 152 (1989), S. 182-188 
    Details
    ISSN: 1432-072X
    Keywords: Glycine decarboxylase ; Glycine reductase ; Lipoamide dehydrogenase ; Selenoprotein PA ; Eubacterium acidaminophilum
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Antibodies raised against the glycine decarboxylase proteins P1, P2, P3, and the selenoprotein PA, a component of the glycine reductase complex, were used for immunocytochemical localization experiments. Cells of Eubacterium acidaminophilum from logarithmic growth phase were fixed in the growth media with paraformaldehyde and glutaraldehyde. Fixed cells were embedded by the low-temperature procedure using Lowicryl K4M resin, and the protein A-gold technique was applied for the localization experiments. The vicinity of the cytoplasmic membrane contained about 27% of all gold particles when proteins P1 and P2 were to be localized, 50% for protein PA, and 61% for protein P3. Double immunocytochemical labeling experiments gave evidence for the existence of a protein P1/P2 complex located predominantly in the cytoplasm, and a P3/PA complex located at the cytoplasmic membrane. Only in very few instances the labels for proteins P3 and P1 were seen very close together in respective doublelabeling experiments. These results indicate that glycine decarboxylase does not occur in this organism as a complex consisting of all four proteins, but that protein P3, the atypical lipoamide dehydrogenase, takes part in both the glycine decarboxylase as well as in the glycine reductase reaction.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00456099
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    Paper (German National Licenses)
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