Adad2 Activators

Chemical activators of adenosine deaminase domain containing 2 can engage in various molecular interactions that enhance the enzyme's activity. Adenosine, a natural substrate of the enzyme, binds to the adenosine receptor, which in turn can increase the intracellular cAMP levels. Elevated cAMP levels can enhance the hydrolytic activity of adenosine deaminase domain containing 2 on its substrate. Zinc Sulfate and Magnesium Chloride serve as cofactors for the enzyme; the presence of zinc or magnesium ions can alter the conformation of the enzyme or facilitate the correct positioning of the substrate within the active site, respectively, thereby increasing enzymatic activity. Dipyridamole, by inhibiting adenosine uptake and catabolism, raises the extracellular adenosine concentration, providing more substrate for deamination. Sodium Metabisulfite can indirectly increase substrate availability by damaging cells, leading to the breakdown of ATP and release of adenosine.

In addition, Inosine presents an alternative substrate for adenosine deaminase domain containing 2, potentially activating the enzyme by increasing its opportunities to catalyze a reaction. Certain inhibitors such as Coformycin, Deoxycoformycin, and Pentostatin can, at lower concentrations, paradoxically enhance the efficiency of substrate binding to the enzyme, thus promoting catalytic activity. Erythro-9-(2-hydroxy-3-nonyl)adenine (EHNA) similarly increases levels of adenosine, the enzyme's substrate, leading to activation due to a higher availability for deamination. Theophylline, an adenosine receptor antagonist, indirectly leads to increased adenosine levels by reducing adenosine receptor-mediated clearance of this substrate. Lastly, Adenine contributes to the formation of adenosine through salvage pathways, bolstering the amount of substrate available for the enzyme to act upon, thereby facilitating its activation.