Chemical activators of HS3ST5 include a variety of inorganic salts and biomolecules that can enhance the protein's enzymatic activity through different biochemical mechanisms. Sodium chloride, for example, can raise the ionic strength of the cellular milieu, which may lead to conformational changes in HS3ST5, thereby increasing its enzymatic activity. Similarly, magnesium chloride and zinc sulfate serve as essential cofactors for many enzymes, including sulfotransferases like HS3ST5. The presence of these divalent cations can stabilize the enzyme's active site and promote substrate binding, leading to an increase in HS3ST5 activity. Manganese(II) sulfate can also serve as an activator by assisting in the catalytic process or stabilizing the enzyme structure. Potassium chloride, like sodium chloride, can optimize the ionic strength and pH, thus creating conditions favorable for HS3ST5 activity by affecting enzyme structure and substrate interactions.
The activation of HS3ST5 can also be influenced by organic molecules that play roles in cellular metabolism and enzyme regulation. PAPS, or 3'-Phosphoadenosine 5'-phosphosulfate, is the universal sulfonate donor in sulfation reactions and provides the sulfate group that HS3ST5 transfers to its substrates. ATP, through its involvement in phosphorylation processes, can activate HS3ST5 by altering its phosphorylation state, which may change the enzyme's conformation and enhance its activity. Dithiothreitol (DTT) can maintain the enzyme in its reduced and active form by breaking down disulfide bonds. Uridine 5'-diphosphate (UDP) is implicated in glycosylation reactions where HS3ST5 may be necessary, thus leading to increased enzymatic function. Glycerol contributes by stabilizing the three-dimensional structure of HS3ST5 during purification, which can enhance its activity. Lastly, Nicotinamide adenine dinucleotide (NAD+) can indirectly increase the activity of HS3ST5 through its role in redox reactions, creating an environment conducive to the optimal function of the sulfotransferase.
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| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
Sodium Chloride | 7647-14-5 | sc-203274 sc-203274A sc-203274B sc-203274C | 500 g 2 kg 5 kg 10 kg | $19.00 $30.00 $60.00 $110.00 | 15 | |
Sodium chloride can enhance the ionic strength of the cellular environment, which can lead to conformational changes in proteins, thereby potentially increasing the enzymatic activity of HS3ST5. | ||||||
Magnesium chloride | 7786-30-3 | sc-255260C sc-255260B sc-255260 sc-255260A | 10 g 25 g 100 g 500 g | $28.00 $35.00 $48.00 $125.00 | 2 | |
Magnesium ions serve as essential cofactors for many enzymes, including sulfotransferases like HS3ST5. The presence of magnesium ions can stabilize the active site and promote the binding of substrates. | ||||||
Adenosine 5′-Triphosphate, disodium salt | 987-65-5 | sc-202040 sc-202040A | 1 g 5 g | $39.00 $75.00 | 9 | |
ATP can be involved in phosphorylation processes that may activate HS3ST5 by altering its phosphorylation state, which may lead to a conformational change and enhanced activity of the enzyme. | ||||||
Zinc | 7440-66-6 | sc-213177 | 100 g | $48.00 | ||
Zinc ions can act as a cofactor and are known to stabilize the structure of many enzymes, which may lead to an increase in HS3ST5 activity by promoting proper folding and substrate alignment. | ||||||
Manganese(II) sulfate monohydrate | 10034-96-5 | sc-203130 sc-203130A | 100 g 500 g | $41.00 $107.00 | ||
Manganese ions can serve as activators for various enzymes by assisting in the catalytic process or by stabilizing enzyme structure, potentially enhancing HS3ST5 activity. | ||||||
Sodium sulfate anhydrous | 7757-82-6 | sc-212945 sc-212945A | 500 g 1 kg | $63.00 $91.00 | ||
Sodium sulfate may contribute to the optimal ionic environment that is required for sulfotransferases like HS3ST5 to function effectively, potentially increasing enzyme activity. | ||||||
Potassium Chloride | 7447-40-7 | sc-203207 sc-203207A sc-203207B sc-203207C | 500 g 2 kg 5 kg 10 kg | $55.00 $155.00 $285.00 $455.00 | 5 | |
Potassium chloride can adjust the ionic strength and pH of the solution, which might lead to optimal conditions for HS3ST5 activity by affecting enzyme structure and substrate interactions. | ||||||
Uridine 5′-diphosphate sodium salt | 21931-53-3 | sc-222401 sc-222401A | 25 mg 100 mg | $38.00 $79.00 | ||
UDP is involved in glycosylation reactions and could be part of the cellular pathways where HS3ST5 activity is necessary, thus potentially leading to an increase in HS3ST5 function. | ||||||
Glycerol | 56-81-5 | sc-29095A sc-29095 | 100 ml 1 L | $56.00 $153.00 | 12 | |
Glycerol is often used as a stabilizing agent for enzymes during purification and can assist in maintaining the three-dimensional structure of HS3ST5, thereby possibly enhancing its activity. | ||||||
NAD+, Free Acid | 53-84-9 | sc-208084B sc-208084 sc-208084A sc-208084C sc-208084D sc-208084E sc-208084F | 1 g 5 g 10 g 25 g 100 g 1 kg 5 kg | $57.00 $191.00 $302.00 $450.00 $1800.00 $3570.00 $10710.00 | 4 | |
NAD+ may indirectly increase the activity of HS3ST5 through its role in cellular redox reactions, which can create a cellular environment conducive to the optimal function of sulfotransferase enzymes. | ||||||