Chemical activators of Nucleotide-diphospho-sugar transferases superfamily proteins can significantly enhance enzyme activity by providing necessary cofactors or substrates for reactions. For example, manganese(II) chloride supplies manganese ions that serve as cofactors, stabilizing the enzyme structure or substrate binding, which can increase enzymatic function. Similarly, magnesium sulfate provides magnesium ions crucial for many enzymes, including this superfamily, helping to achieve the correct active site conformation for catalysis. Zinc acetate delivers zinc ions, known to enhance the catalytic efficiency of some glycosyltransferases by promoting proper folding and function of their catalytic domains. Calcium chloride contributes calcium ions, which may stabilize enzyme structures or substrate complexes, thus potentially enhancing enzyme activity. Cobalt(II) chloride supplies cobalt ions that could stabilize the enzyme structure or assist in substrate orientation, leading to increased activity.
Moreover, sodium orthovanadate acts as a phosphatase inhibitor, which can enhance the phosphorylation status of proteins, indirectly activating Nucleotide-diphospho-sugar transferases. Adenosine triphosphate (ATP) is indispensable for the activation of many enzymes and offers phosphate groups for the synthesis of nucleotide sugars, which are substrates for these enzymes. Uridine triphosphate (UTP), cytidine triphosphate (CTP), and guanosine triphosphate (GTP) serve as substrates and are integral for the biosynthesis of nucleotide sugars, facilitating glycosyl transfer reactions. Nickel(II) sulfate and copper(II) sulfate provide nickel and copper ions, respectively, which can act as cofactors, potentially increasing the activity of the enzymes by facilitating substrate binding or by maintaining the active site in an optimal conformation for enzymatic activity.
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| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
Manganese(II) chloride beads | 7773-01-5 | sc-252989 sc-252989A | 100 g 500 g | $19.00 $30.00 | ||
Manganese(II) chloride can serve as a cofactor for Nucleotide-diphospho-sugar transferases superfamily proteins, potentially increasing their enzymatic activity by stabilizing the structure or the binding of the substrate. | ||||||
Magnesium sulfate anhydrous | 7487-88-9 | sc-211764 sc-211764A sc-211764B sc-211764C sc-211764D | 500 g 1 kg 2.5 kg 5 kg 10 kg | $45.00 $68.00 $160.00 $240.00 $410.00 | 3 | |
Magnesium sulfate can act as a cofactor and is known to be critical for the activity of many enzymes. For Nucleotide-diphospho-sugar transferases superfamily proteins, magnesium ions can help in forming the correct active site conformation necessary for catalysis. | ||||||
Zinc | 7440-66-6 | sc-213177 | 100 g | $47.00 | ||
Zinc acetate can provide zinc ions, which can function as an essential cofactor for many enzymes, including some glycosyltransferases, thereby potentially enhancing the catalytic efficiency of Nucleotide-diphospho-sugar transferases superfamily proteins by promoting the correct folding and function of the catalytic domain. | ||||||
Calcium chloride anhydrous | 10043-52-4 | sc-207392 sc-207392A | 100 g 500 g | $65.00 $262.00 | 1 | |
Calcium chloride could contribute calcium ions that might serve as a secondary messenger or cofactor in various enzymatic reactions, thus potentially enhancing the activity of Nucleotide-diphospho-sugar transferases superfamily proteins by stabilizing the enzyme structure or substrate complex. | ||||||
Cobalt(II) chloride | 7646-79-9 | sc-252623 sc-252623A | 5 g 100 g | $63.00 $173.00 | 7 | |
Cobalt(II) chloride can supply cobalt ions which may act as a cofactor for certain enzymes. In the case of Nucleotide-diphospho-sugar transferases superfamily proteins, cobalt ions might stabilize the enzyme's structure or assist in the proper orientation of substrates, thereby leading to an increase in enzymatic activity. | ||||||
Sodium Orthovanadate | 13721-39-6 | sc-3540 sc-3540B sc-3540A | 5 g 10 g 50 g | $45.00 $56.00 $183.00 | 142 | |
Sodium orthovanadate is a potent phosphatase inhibitor that can enhance phosphorylation status of proteins within the cell. By inhibiting phosphatases, phosphorylation levels of glycosyltransferase enzymes, including Nucleotide-diphospho-sugar transferases, may increase. This elevation in phosphorylation can lead to an activation of enzyme activity. | ||||||
Adenosine 5′-Triphosphate, disodium salt | 987-65-5 | sc-202040 sc-202040A | 1 g 5 g | $38.00 $74.00 | 9 | |
ATP is the primary energy currency of the cell and is necessary for the activation of many enzymes. For Nucleotide-diphospho-sugar transferases superfamily proteins, ATP could provide the phosphate groups for the synthesis of nucleotide sugars, which are substrates for these enzymes, thus potentially enhancing their enzymatic activity. | ||||||
Uridine-5′-triphosphate, Trisodium Salt | 19817-92-6 | sc-301964 sc-301964A | 50 mg 1 g | $86.00 $118.00 | 2 | |
UTP is a substrate for Nucleotide-diphospho-sugar transferases superfamily proteins in the biosynthesis of nucleotide sugars. By increasing the availability of UTP, the activity of these enzymes could be enhanced, as they catalyze the transfer of sugar moieties from nucleotide sugars to acceptor molecules. | ||||||
Nickel Sulfate | 7786-81-4 | sc-507407 | 5 g | $63.00 | ||
Nickel(II) sulfate can supply nickel ions, which can act as a cofactor for certain enzymes. In the context of Nucleotide-diphospho-sugar transferases superfamily proteins, nickel ions could potentially increase enzymatic activity by facilitating substrate binding or by stabilizing the active site conformation. | ||||||
Copper(II) sulfate | 7758-98-7 | sc-211133 sc-211133A sc-211133B | 100 g 500 g 1 kg | $45.00 $120.00 $185.00 | 3 | |
Copper(II) sulfate can provide copper ions, which may serve as cofactors for various enzymes. The activity of Nucleotide-diphospho-sugar transferases superfamily proteins could be increased by the presence of copper ions as they might enhance the structural stability of the enzyme or aid in the catalytic process through proper orientation of the substrate. | ||||||