2 papers analyzed
These studies suggest Asp-50 is involved in the binding and deprotonation of NH4+ to form NH3 in Escherichia coli glutamine synthetase.
Asp-50 is a critical residue in the enzyme Escherichia coli glutamine synthetase, playing a significant role in the binding and catalysis of ammonium ions (NH4+). Understanding how Asp-50 interacts with NH4+ is essential for elucidating the enzyme's mechanism and function.
Role in Substrate Binding and Catalysis:
Metal Ion Dependency:
Deprotonation Role:
Asp-50 in Escherichia coli glutamine synthetase is essential for the binding and catalysis of NH4+. It significantly influences substrate binding, catalytic efficiency, and the enzyme's interaction with metal ions. Additionally, Asp-50 may facilitate the deprotonation of NH4+, further underscoring its critical role in the enzyme's function.
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