Published October 1987
| Published
Journal Article
Open
Role of glutamate dehydrogenase in ammonia assimilation in nitrogen-fixing Bacillus macerans
Chicago
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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.
Additional Information
© 1987 American Society for Microbiology. Received 23 March 1987/Accepted 17 July 1987 This work was supported by National Science Foundation grant DMB85-01617. Contribution no. 7563 from the Gates and Crellin Laboratories of Chemistry, California Institute of Technology.Attached Files
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Additional details
- PMCID
- PMC213841
- Eprint ID
- 6696
- Resolver ID
- CaltechAUTHORS:KANjbact87
- NSF
- DMB85-01617
- Created
-
2006-12-18Created from EPrint's datestamp field
- Updated
-
2019-10-02Created from EPrint's last_modified field
- Other Numbering System Name
- Caltech Gates and Crellin Laboratories of Chemistry
- Other Numbering System Identifier
- 7563