EC Number |
Reaction |
Reference |
---|
6.3.5.4 | ATP + L-aspartate + L-glutamine + H2O = AMP + diphosphate + L-asparagine + L-glutamate |
a model for the role of the catalytic triad in transferring nitrogen from Gln to Asp. An alternative catalytic mechanism is proposed, which obviates the participation of a histidine residue in the reaction |
1699 |
6.3.5.4 | ATP + L-aspartate + L-glutamine + H2O = AMP + diphosphate + L-asparagine + L-glutamate |
Arg325 is involved in stabilization of a pentacovalent intermediate leading to the formation of beta-aspartyl-AMP |
1701 |
6.3.5.4 | ATP + L-aspartate + L-glutamine + H2O = AMP + diphosphate + L-asparagine + L-glutamate |
hybrid uni uni bi ter ping pong Theorell-Chance mechanism where the glutaminase reaction occurs first and Asp binds to the enzyme before ATP in the sequential segment. Diphosphate is the first product released in the Theorell-Chance reaction, which is followed by the ordered release of AMP and Asn |
1680 |
6.3.5.4 | ATP + L-aspartate + L-glutamine + H2O = AMP + diphosphate + L-asparagine + L-glutamate |
mechanism |
649482 |
6.3.5.4 | ATP + L-aspartate + L-glutamine + H2O = AMP + diphosphate + L-asparagine + L-glutamate |
NH4+ is bound to the enzyme followed by MgATP causing Asn release |
1684 |
6.3.5.4 | ATP + L-aspartate + L-glutamine + H2O = AMP + diphosphate + L-asparagine + L-glutamate |
overall ping-pong mechanism |
- |
6.3.5.4 | ATP + L-aspartate + L-glutamine + H2O = AMP + diphosphate + L-asparagine + L-glutamate |
ping-pong reaction mechanism. Glutamine is the first substrate to bind to the enzyme and Asn is the last product released |
- |
6.3.5.4 | ATP + L-aspartate + L-glutamine + H2O = AMP + diphosphate + L-asparagine + L-glutamate |
reaction mechanism, structure-function relationship |
745375 |
6.3.5.4 | ATP + L-aspartate + L-glutamine + H2O = AMP + diphosphate + L-asparagine + L-glutamate |
the enzyme forms a crucial beta-aspartyl-AMP-Mg2+ intermediate, which then undergoes a nucleophilic attack of ammonia, forming Asn and releasing AMP and diphosphate. Ammonia can be free or glutamine-derived |
-, 746172 |
6.3.5.4 | ATP + L-aspartate + L-glutamine + H2O = AMP + diphosphate + L-asparagine + L-glutamate |
uni-uni-bi-ter ping-pong mechanism without abortive complexes. Gln binds first, followed by Glu release, and Asp and ATP bind in order followed by ordered release of diphosphate, AMP and Asn. In the presence of 0.5-2.0 mM excess Mg2+ over ATP the binding of substrates after the release of Glu is in a rapid equilibrium system |
1673 |