Chemical activators of S-adenosylmethionine decarboxylase 2 play a pivotal role in modulating the enzyme's activity. Methylthioadenosine, a precursor in polyamine synthesis, acts to enhance the demand for decarboxylated S-adenosylmethionine, upregulating the enzyme's function. Similarly, Putrescine, Spermidine, and Spermine, which are polyamines, activate the enzyme by increasing the intracellular concentration of these molecules, which is essential for cellular functions and stimulates the enzyme's activity as part of their biosynthetic pathway. Ornithine directly serves as a substrate for the synthesis of polyamines, thereby necessitating increased enzymatic activity for conversion into Putrescine. Adenosylmethionine, being a direct substrate for S-adenosylmethionine decarboxylase 2, also activates the enzyme by its conversion into the decarboxylated product, a crucial step in polyamine biosynthesis.
Cofactors such as Magnesium Chloride and Pyridoxal Phosphate are essential for the structural and catalytic functionality of S-adenosylmethionine decarboxylase 2. Magnesium Chloride is necessary for the proper folding of the enzyme, which is directly related to its activation. Pyridoxal Phosphate, on the other hand, facilitates the decarboxylation reaction, thereby enhancing the enzyme's activity. Additionally, Methionine acts as an amino acid precursor to S-adenosylmethionine, elevating the substrate availability for the enzyme, which in turn may increase its activity to fulfill the requirements for polyamine synthesis. Decarboxylated Adenosine, by mimicking the enzyme's product, can induce a positive effect on the enzyme's efficiency. N-Acetylcysteine contributes to the maintenance of cellular redox states, thus indirectly supporting enzymatic activity by preserving the enzyme's integrity. Lastly, Nicotinamide Adenine Dinucleotide (NAD+) participates in redox reactions that sustain the activity of the enzyme by maintaining the cellular energy status necessary for its function.
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| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
Spermidine | 124-20-9 | sc-215900 sc-215900B sc-215900A | 1 g 25 g 5 g | $56.00 $595.00 $173.00 | ||
Spermidine acts to activate S-adenosylmethionine decarboxylase 2 by being a downstream product of the enzyme's reaction, potentially upregulating the enzyme's activity through feedback enhancement mechanisms. | ||||||
Spermine | 71-44-3 | sc-212953A sc-212953 sc-212953B sc-212953C | 1 g 5 g 25 g 100 g | $60.00 $192.00 $272.00 $883.00 | 1 | |
Spermine can activate S-adenosylmethionine decarboxylase 2 by interacting with the enzyme as part of the polyamine biosynthesis pathway, which may lead to an increase in the enzyme's catalytic activity due to higher substrate availability. | ||||||
Ornithine | 70-26-8 | sc-507552 | 100 mg | $75.00 | ||
Ornithine directly activates S-adenosylmethionine decarboxylase 2 by serving as a substrate for the synthesis of polyamines, necessitating greater enzymatic activity for conversion into putrescine, which is a precursor in the polyamine biosynthesis pathway. | ||||||
Ademetionine | 29908-03-0 | sc-278677 sc-278677A | 100 mg 1 g | $180.00 $655.00 | 2 | |
Adenosylmethionine activates S-adenosylmethionine decarboxylase 2 by acting as a direct substrate for the enzyme, leading to its conversion into decarboxylated S-adenosylmethionine, which is a key step in polyamine biosynthesis. | ||||||
L-Methionine | 63-68-3 | sc-394076 sc-394076A sc-394076B sc-394076C sc-394076D sc-394076E | 25 g 100 g 250 g 1 kg 5 kg 10 kg | $33.00 $36.00 $56.00 $148.00 $566.00 $1081.00 | ||
Methionine activates S-adenosylmethionine decarboxylase 2 by being the amino acid precursor to S-adenosylmethionine, thus increasing the substrate pool for the enzyme and potentially enhancing its activity to meet the demand for polyamine synthesis. | ||||||
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 Chloride activates S-adenosylmethionine decarboxylase 2 by acting as a cofactor that is essential for the proper folding and catalytic function of the enzyme, thus directly contributing to its activation. | ||||||
Pyridoxal-5-phosphate | 54-47-7 | sc-205825 | 5 g | $102.00 | ||
Pyridoxal Phosphate activates S-adenosylmethionine decarboxylase 2 by serving as a cofactor that facilitates the decarboxylation reaction catalyzed by the enzyme, enhancing its functional activity. | ||||||
N-Acetyl-L-cysteine | 616-91-1 | sc-202232 sc-202232A sc-202232C sc-202232B | 5 g 25 g 1 kg 100 g | $33.00 $73.00 $265.00 $112.00 | 34 | |
N-Acetylcysteine can activate S-adenosylmethionine decarboxylase 2 by contributing to the maintenance of cellular redox states, which may indirectly support the enzymatic activity by preserving the integrity of the enzyme under oxidative stress conditions. | ||||||
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 | |
Nicotinamide Adenine Dinucleotide (NAD+) activates S-adenosylmethionine decarboxylase 2 by participating in redox reactions that may indirectly sustain the activity of the enzyme through maintaining the cellular energy status required for its function. | ||||||