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. 1987 Oct;169(10):4692–4695. doi: 10.1128/jb.169.10.4692-4695.1987

Role of glutamate dehydrogenase in ammonia assimilation in nitrogen-fixing Bacillus macerans.

K Kanamori 1, R L Weiss 1, J D Roberts 1
PMCID: PMC213841  PMID: 2888750

Abstract

Pathways of ammonia assimilation into glutamic acid in Bacillus macerans were investigated by measurements of the specific activities of glutamate dehydrogenase (GDH), glutamine synthetase, and glutamate synthase. In ammonia-rich medium, GDH was the predominant pathway of ammonia assimilation. In nitrogen-fixing cells in which the intracellular NH4+ concentration was 1.4 +/- 0.5 mM, the activity of GDH with a Km of 2.2 mM for NH4+ was found to be severalfold higher than that of glutamate synthase. The result suggests that GDH plays a significant role in the assimilation of NH4+ in N2-fixing B. macerans.

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Selected References

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