Abstract
Inorganic nitrogen metabolism in the obligate anaerobic thermophiles Chlostridium thermosaccharolyticum and Clostridium thermoautotrophicum differs in several respects. C. thermosaccharolyticum contains a nitrogenase as inferred from NH +4 repressible C2H2 reduction, a glutamine synthetase which is partially repressed by ammonium, very labile glutamate synthase activities with both NADH and NADPH, NADPH-dependent glutamate dehydrogenase, and NH +4 -dependent asparagine synthetase. C. thermoautotrophicum contains no nitrogenase, but glutamine synthetase, no glutamate synthase, no glutamate dehydrogenase, but a NADH-dependent alanine dehydrogenase and a NH +4 -dependent asparagine synthetase.
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Abbreviations
- GOGAT:
-
glutamine-oxoglutarate amidotransferase amidotransferase (glutamate synthase)
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Bogdahn, M., Kleiner, D. N2 fixation and NH +4 assimilation in the thermophilic anaerobes Clostridium thermosaccharolyticum and Clostridium thermoautotrophicum . Arch. Microbiol. 144, 102–104 (1986). https://doi.org/10.1007/BF00454964
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DOI: https://doi.org/10.1007/BF00454964