Sandbox Reserved 957: Difference between revisions
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** The crucial <scene name='60/604476/Asp764/1'>Asp764</scene> [3] and the conserved His617 and 653[4], which bind one Zinc ion, are fundamental for the catalytic activity.<br \> | ** The crucial <scene name='60/604476/Asp764/1'>Asp764</scene> [3] and the conserved His617 and 653[4], which bind one Zinc ion, are fundamental for the catalytic activity.<br \> | ||
** <scene name='60/604476/Zn/1'>Zinc</scene> is critical for catalytic activity, but it isn't implied in the formation of the hydrophobic pocket. In fact, even if <scene name='60/604476/His653_his617/1'>the His617and 653</scene> are lost and so the Zn not bound, a massive addition of Manganese[4] in the medium allows a reactivation of catalysis.<br \> | ** <scene name='60/604476/Zn/1'>Zinc</scene> is critical for catalytic activity, but it isn't implied in the formation of the hydrophobic pocket. In fact, even if <scene name='60/604476/His653_his617/1'>the His617and 653</scene> are lost and so the Zn not bound, a massive addition of Manganese[4] in the medium allows a reactivation of catalysis.<br \> | ||
* W2 binds | * W2 binds <scene name='60/604476/Mg_zn/1'>Zn and Mg</scene> [24],<br \> | ||
<scene name='60/604476/Mg_zn/1'>Zn and Mg</scene> [24],<br \> | * And there are 3 hydrogen bonds between 3 H2O and the conserved resides <scene name='60/604476/His657glu682his685/1'>His657, Asp682 and His685</ scene> [24].<br \> | ||
* And there are 3 hydrogen bonds between 3 H2O and the conserved resides His657, Asp682 and His685 [24].<br \> | |||
Q site contains:<br \> | Q site contains:<br \> | ||
* In particular the conserved residues | * In particular the conserved residues Gln817, Phe820, Val782 and Tyr612. [24]<br \> | ||
* The hydrogen bonds, between | * The hydrogen bonds, between Gln817 and 775, Gln775 and Ala767, Gln775 and Trp853, imply an interaction between Gln817 and the cGMP purine. Thus, it improves the specificity for the cGMP, against cAMP. [24]<br \> | ||
* And | * And Tyr612, Val782, Leu785 an Phe820 bind the cGMP through this pyrazol ring and π-π interactions between Gln817 and the phenyl ring. [24]<br \> | ||
** So, the conserved hydrophobic residue | ** So, the conserved hydrophobic residue Tyr 612 is critical in the maintaining of the affinity. [3]<br \> | ||
H site:<br \> | H site:<br \> | ||
* In particular the residues | * In particular the residues Phe786, Ala783, Leu804, Val782. [24]<br \> | ||
L site:<br \> | L site:<br \> | ||
* In particular the hydrophobic residues | * In particular the hydrophobic residues Tyr664, Met816, Ala823, Gly819. [24]<br \> | ||
Besides, the kcat of the catalytic fragment decreases 40-fold and 8-fold if the residues His603 and Asp644 are mutated, and so there are important in the catalytic activity [5,3]. Two others residues are significant: the Gln778 which is important for cGMP affinity but have no impact on cAMP affinity H-loop [8] and the conserved Gly659 which is important for substrate affinity and catalytic activity because it determinates H-loop conformation [21] (see below).<br \> | Besides, the kcat of the catalytic fragment decreases 40-fold and 8-fold if the residues His603 and Asp644 are mutated, and so there are important in the catalytic activity [5,3]. Two others residues are significant: the Gln778 which is important for cGMP affinity but have no impact on cAMP affinity H-loop [8] and the conserved Gly659 which is important for substrate affinity and catalytic activity because it determinates H-loop conformation [21] (see below).<br \> |