Protein Variants | Comment | Organism |
---|---|---|
D50E | mutant D50E shows activity with Mn2+ but very low activity with Mg2+, and altered kcat/Km values for all three substrates. Mutant E327A has a decreased kcat/Km value for NH4+ compared to that of the wild-type enzyme. Asp-50 is likely involved in binding NH4+ and may also play a role in catalyzing deprotonation of NH4+ to form NH3. Glu-327 participates in lowering the free energy of the transition state involved in formation of the positively charged tetrahedral adduct resulting from the condensation of gamma-glutamyl phosphate and NH3 | Escherichia coli |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | Km-values of wild-type and mutant enzymes D50A, D50E, E327A | Escherichia coli | |
4.9 | - |
Gln | - |
Escherichia coli |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
wild-type and site-directed mutants | - |
Escherichia coli | - |
wild-type and site-directed mutants H4A, H4C, M8L, H12L, H12D | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + L-Glu + NH4+ | - |
Escherichia coli | ADP + phosphate + L-Gln | - |
? |