Published October 1987
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Journal Article
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Role of glutamate dehydrogenase in ammonia assimilation in nitrogen-fixing Bacillus macerans
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
Published - KANjbact87.pdf
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KANjbact87.pdf
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Identifiers
- PMCID
- PMC213841
- Eprint ID
- 6696
- Resolver ID
- CaltechAUTHORS:KANjbact87
Related works
- Describes
- http://jb.asm.org/cgi/content/abstract/169/10/4692 (URL)
Funding
- NSF
- DMB85-01617
Dates
- Created
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2006-12-18Created from EPrint's datestamp field
- Updated
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2019-10-02Created from EPrint's last_modified field
Caltech Custom Metadata
- Other Numbering System Name
- Caltech Gates and Crellin Laboratories of Chemistry
- Other Numbering System Identifier
- 7563