EC Number   |
Reaction |
Reference |
|---|
    6.3.1.2 | ATP + L-glutamate + NH3 = ADP + phosphate + L-glutamine |
in the first step of catalysis, a tightly bound, activated intermediate, gamma-glutamyl phosphate, is formed when the terminal phosphate of ATP is transferred to the carboxylate side chain of the substrate glutamate. In the second step, an enzyme-bound ammonium ion is deprotonated, forming ammonia that attacks the carbonyl carbon of gamma-glutamyl phosphate to form a tetrahedral intermediate. The enzyme subsequently releases free phosphate and glutamine |
-, 745816 |
| 6.3.1.2 | ATP + L-glutamate + NH3 = ADP + phosphate + L-glutamine |
ordered three-reactant system with the binding order: NH4+, L-Glu and ATP |
37518 |
| 6.3.1.2 | ATP + L-glutamate + NH3 = ADP + phosphate + L-glutamine |
random catalysis mechanism where the binding order of certain substrates is kinetically preferred by the enzyme |
706610 |
| 6.3.1.2 | ATP + L-glutamate + NH3 = ADP + phosphate + L-glutamine |
reaction mechanism |
-, 694057 |
| 6.3.1.2 | ATP + L-glutamate + NH3 = ADP + phosphate + L-glutamine |
reaction mechanism and transition state analogue, overview |
694057 |
| 6.3.1.2 | ATP + L-glutamate + NH3 = ADP + phosphate + L-glutamine |
structure-function relationship and catalytic mechanism, overview |
-, 727970 |
