Kinetic and mutagenic studies of the role of the active site residues Asp-50 and Glu-327 of Escherichia coli glutamine synthetase
Author:
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi00169a008
Reference24 articles.
1. Effect of metal ions and adenylylation state on the internal thermodynamics of phosphoryl transfer in the Escherichia coli glutamine synthetase reaction
2. Novel subunit—subunit interactions in the structure of glutamine synthetase
3. Characterization of a gene, glnL, the product of which is involved in the regulation of nitrogen utilization in Escherichia coli
4. Isotope-exchange enhancement studies of Escherichia coli glutamine synthetase
5. Studies of the mechanism of glutamine synthetase utilizing pH-dependent behavior in catalysis and binding.
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