EC Number   |
Reaction |
Reference |
|---|
    2.7.4.3 | ATP + AMP = 2 ADP |
associative mechanism for phosphoryl transfer |
677011 |
| 2.7.4.3 | ATP + AMP = 2 ADP |
binding of ATP induces a dynamic equilibrium in which the ATP binding motif populates both the open and the closed conformations with almost equal populations. A similar scenario is observed for AMP binding, which induces an equilibrium between open and closed conformations of the AMP binding motif. Simultaneous binding of AMP and ATP is required to force both substrate binding motifs to close cooperatively. Unidirectional energetic coupling between the ATP and AMP binding sites |
692742 |
| 2.7.4.3 | ATP + AMP = 2 ADP |
coarse-grained models and nonlinear normal mode analysis. Intrinsic structural fluctuations dominate LID domain motion, whereas ligand-protein interactions and local unfolding are more important during NMP domain motion. LID-NMP domain interactions are indispensable for efficient catalysis. LID domain motion precedes NMP domain motion, during both opening and closing, providing mechanistic explanation for the observed 1:1:1 correspondence between LID domain closure, NMP domain closure, and substrate turnover |
693617 |
| 2.7.4.3 | ATP + AMP = 2 ADP |
induced-fit and change between open and closed conformation, random Bi-Bi reaction mechanism, the conformational change of the ADK enzyme very much follows two parallel stepwise pathways as a functional requirement for the double substrate catalysis |
738750 |
| 2.7.4.3 | ATP + AMP = 2 ADP |
iso-random bi-bi mechanism |
642605 |
| 2.7.4.3 | ATP + AMP = 2 ADP |
mechanism |
642556, 642558, 642560, 642561, 642566, 642569, 642570, 642571, 642572, 642573, 642597, 642617, 642622 |
| 2.7.4.3 | ATP + AMP = 2 ADP |
overview: mechanism |
642623 |
| 2.7.4.3 | ATP + AMP = 2 ADP |
thermodynamics and kinetics |
642604 |
| 2.7.4.3 | ATP + AMP = 2 ADP |
triphosphate can also act as donor |
- |
