CTU1 Activators
CTU1 serve integral roles in modulating the protein's enzymatic activity, particularly in the post-transcriptional modification of tRNA. S-Adenosylmethionine is indispensable for CTU1, as it donates the methyl groups that CTU1 requires to fulfill its function in tRNA methylation. The availability of this chemical ensures that CTU1 can carry out its methylating actions efficiently. Concurrently, thiamine diphosphate provides structural support for CTU1, enhancing the enzyme's stability and enabling the proper progression of tRNA modification reactions. In harmony, glutathione reduced and nicotinamide adenine dinucleotide (NADH) contribute to maintaining a reduced cellular environment, which is vital for the correct folding and activity of CTU1. This redox balance is crucial, as it influences the structural integrity of CTU1 and the successful execution of its enzymatic tasks.
Further contributing to CTU1's activity are magnesium chloride and zinc acetate, which supply magnesium and zinc ions, respectively. These ions are cofactors that bind to CTU1, facilitating the correct enzyme conformation and catalytic function. Potassium chloride, by modulating the ionic concentration around CTU1, ensures that the protein maintains its proper shape and is poised for activity. Adenosine triphosphate (ATP) is another chemical activator that supplies the energy required for the dynamic structural changes CTU1 undergoes during the catalysis of tRNA modification. Folinic acid and pyridoxal phosphate offer additional coenzyme support, possibly providing formyl groups and participating in the enzymatic reaction as necessary. Trace elements like manganese, via manganese(II) sulfate, and copper, from copper(II) sulfate, are also crucial as they may stabilize enzyme intermediates or enhance structural stability, thereby promoting the catalytic efficiency of CTU1 in its essential role in tRNA modification processes.
Items 1 to 10 of 11 total
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| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
Ademetionine | 29908-03-0 | sc-278677 sc-278677A | 100 mg 1 g | $180.00 $655.00 | 2 | |
S-Adenosylmethionine (SAM) serves as a methyl donor in methylation reactions mediated by methyltransferases, including those that modify tRNA, which is a process CTU1 is involved in. Hence, SAM activates CTU1 by providing the necessary methyl groups for its tRNA modification function. | ||||||
Thiamine pyrophosphate | 154-87-0 | sc-215966 sc-215966A sc-215966B sc-215966C sc-215966D | 1 g 5 g 25 g 100 g 1 kg | $32.00 $95.00 $284.00 $1126.00 $5906.00 | 1 | |
Thiamine diphosphate is a cofactor for enzymes involved in the biosynthesis of amino acids and nucleic acids, which are substrates in reactions that CTU1 catalyzes. This cofactor thereby supports CTU1's role in the modification of tRNA molecules. | ||||||
Glutathione, reduced | 70-18-8 | sc-29094 sc-29094A | 10 g 1 kg | $76.00 $2050.00 | 8 | |
Glutathione reduced (GSH) maintains cellular redox state and provides reducing equivalents. CTU1 activity may be influenced by the redox state of the cell, and GSH could support CTU1 activity by maintaining a reduced environment, which is conducive to its function in tRNA modification. | ||||||
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 | $56.00 $186.00 $296.00 $655.00 $2550.00 $3500.00 $10500.00 | 4 | |
NADH participates in redox reactions, potentially assisting in the restoration of disulfide bonds within the tRNA modification process, thereby promoting the catalytic action of CTU1. | ||||||
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 | |
As a cofactor, magnesium ions are essential for the active conformation of many enzymes, including those involved in phosphorylation. By stabilizing the structure of enzymes, magnesium chloride could enhance the catalytic efficiency of CTU1 in tRNA modification. | ||||||
Zinc | 7440-66-6 | sc-213177 | 100 g | $47.00 | ||
Zinc ions are known to serve as catalytic or structural cofactors for many proteins. By coordinating with residues in the active site, zinc acetate may directly participate in the catalytic mechanism of CTU1, promoting its activity in tRNA modification. | ||||||
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 vital for maintaining osmotic balance and proper enzyme function. Potassium chloride may facilitate CTU1 activity by ensuring optimal ionic strength and enzyme conformation for its role in the tRNA modification process. | ||||||
ATP | 56-65-5 | sc-507511 | 5 g | $17.00 | ||
ATP provides the energy required for many enzymatic reactions. It could activate CTU1 by supplying the necessary energy for conformational changes that enhance CTU1's catalytic activity in modifying tRNA molecules. | ||||||
Folinic Acid | 58-05-9 | sc-337846A sc-337846B sc-337846 | 5 mg 25 mg 100 mg | $110.00 $291.00 $592.00 | ||
Folinic acid acts as a donor of formyl groups in metabolic reactions, which could be utilized in the tRNA modification reactions that CTU1 catalyzes, thus promoting its enzymatic activity. | ||||||
Pyridoxal-5-phosphate | 54-47-7 | sc-205825 | 5 g | $102.00 | ||
Pyridoxal phosphate is a vitamin B6 derivative that acts as a coenzyme in various enzymatic reactions involving amino acids, potentially supporting CTU1's function in tRNA modification by providing necessary coenzyme activity. | ||||||