NUDT22 play pivotal roles in modulating its enzymatic activity through various mechanisms. Adenosine triphosphate (ATP) is one such activator, serving as a cofactor that directly engages with NUDT22, providing essential phosphate groups to catalyze the hydrolysis reaction central to the protein's function. Magnesium chloride contributes by supplying Mg2+ ions that are integral to the structural integrity and catalytic competency of NUDT22. These ions aid in folding and stabilizing the protein's conformation, ensuring that the active sites are correctly positioned for enzymatic action. Similarly, zinc acetate can act as a cofactor, binding to NUDT22 and inducing a conformational shift that activates the enzyme. The presence of potassium chloride is also beneficial, as K+ ions can interact with the enzyme to promote a favorable conformation, thus enhancing NUDT22's activity.
Certain compounds function to stabilize the enzyme structure and maintain the reductive environment necessary for NUDT22 activity. Dithiothreitol (DTT) ensures that the cysteine residues within the active site remain in a reduced state, which is a prerequisite for the catalytic action of the protein. Glycerol and ethylene glycol both serve as stabilizing agents that can interact with hydrophobic regions of NUDT22, maintaining an active enzyme conformation. HEPES buffer maintains a stable pH around NUDT22, which is essential for its optimal activity as enzymes typically have a narrow pH range in which they are most active. Compounds such as glucose-6-phosphate may directly engage with the enzyme as substrates, thereby facilitating its catalytic function. Finally, ammonium sulfate and urea can influence the solubility and stability of NUDT22, promoting a structural state that is conducive to activity. These chemical activators collectively ensure that NUDT22 retains a functional conformation and provides the necessary conditions for its enzymatic mechanism to proceed efficiently.
SEE ALSO...
| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
ATP | 56-65-5 | sc-507511 | 5 g | $17.00 | ||
NUDT22 is a member of the Nudix hydrolase family, which typically have enzymatic activity that requires or is regulated by nucleoside triphosphates. ATP serves as a cofactor that directly activates the hydrolase function of NUDT22 by providing the necessary phosphate groups for its enzymatic activity. | ||||||
Magnesium chloride | 7786-30-3 | sc-255260C sc-255260B sc-255260 sc-255260A | 10 g 25 g 100 g 500 g | $27.00 $34.00 $47.00 $123.00 | 2 | |
Magnesium ions are essential for the activity of many enzymes, including those in the Nudix family. As an activator, magnesium chloride provides Mg2+ ions that bind to NUDT22, facilitating its proper folding and function, thereby directly enhancing its enzymatic activity. | ||||||
Sodium Fluoride | 7681-49-4 | sc-24988A sc-24988 sc-24988B | 5 g 100 g 500 g | $39.00 $45.00 $98.00 | 26 | |
Fluoride ions can act as phosphate analogs, and in certain contexts, they can activate phosphatase enzymes. As NUDT22 may have phosphatase-like activity, sodium fluoride can enhance this activity by stabilizing the phosphate binding site, leading to direct activation of the protein. | ||||||
Potassium Chloride | 7447-40-7 | sc-203207 sc-203207A sc-203207B sc-203207C | 500 g 2 kg 5 kg 10 kg | $25.00 $56.00 $104.00 $183.00 | 5 | |
Potassium ions are important for maintaining the cellular ionic environment. In the context of NUDT22, K+ may interact with the enzyme's active site or allosteric sites, leading to a conformational change that activates the enzyme. | ||||||
Zinc | 7440-66-6 | sc-213177 | 100 g | $47.00 | ||
Zinc ions can act as a cofactor for many enzymes, potentially including NUDT22. By binding to specific sites, zinc acetate can induce a conformational change in NUDT22 that results in its activation. | ||||||
Glycerol | 56-81-5 | sc-29095A sc-29095 | 100 ml 1 L | $55.00 $150.00 | 12 | |
Glycerol is often used to stabilize enzymes and can interact with hydrophobic regions, potentially leading to an optimal conformation for enzyme activity. In the context of NUDT22, glycerol may stabilize the structure and thus promote the active conformation of the protein. | ||||||
Ethylene glycol | 107-21-1 | sc-257515 sc-257515A | 500 ml 1 L | $83.00 $118.00 | 1 | |
Ethylene glycol has properties similar to glycerol and can be used to stabilize proteins. When interacting with NUDT22, it may stabilize the active conformation and thereby enhance the protein's hydrolase activity. | ||||||
D-Glucose 6-phosphate disodium salt | 3671-99-6 | sc-221488 sc-221488A sc-221488B | 10 mg 1 g 25 g | $38.00 $66.00 $1102.00 | 1 | |
This compound can act as a substrate for certain hydrolases and may interact with NUDT22. By serving as a potential substrate, glucose-6-phosphate may directly activate the catalytic activity of the protein. | ||||||
Ammonium Sulfate | 7783-20-2 | sc-29085A sc-29085 sc-29085B sc-29085C sc-29085D sc-29085E | 500 g 1 kg 2 kg 5 kg 10 kg 22.95 kg | $10.00 $20.00 $30.00 $40.00 $60.00 $100.00 | 9 | |
Ammonium sulfate is commonly used in protein purification but also affects protein solubility and stability. For NUDT22, ammonium sulfate might promote a more active conformation or state of the protein, enhancing its functional activity. | ||||||
Urea | 57-13-6 | sc-29114 sc-29114A sc-29114B | 1 kg 2 kg 5 kg | $30.00 $42.00 $76.00 | 17 | |
Low concentrations of urea can sometimes stabilize proteins in their native state. For NUDT22, urea might interact with the protein's structure in such a way to promote an active conformation, thus directly contributing to the activation of the protein's catalytic activity. | ||||||