4933437F05Rik Activators
Chemical activators of NADP+ dependent oxidoreductase domain containing 1 play crucial roles in the modulation of its function. NADPH, as a reducing equivalent provider, plays a pivotal role in enhancing the reductase activity of the protein by donating the necessary electrons for reduction reactions. Similarly, FAD and FMN, both found in riboflavin, are integral to the protein's activity, as they participate in the electron transfer processes during substrate oxidation. This facilitates the catalytic cycle of the protein, thereby promoting its activation. Glutathione, in its reduced form, further contributes by donating electrons in the detoxification of hydrogen peroxide, which is catalyzed by NADP+ dependent oxidoreductase domain containing 1. This interaction enables the protein to carry out its antioxidative function more efficiently.
The presence of heme enhances the electron transfer capabilities of NADP+ dependent oxidoreductase domain containing 1, which is crucial for its enzymatic activity. The heme group, by facilitating electron transfers within the protein's active site, helps in optimizing its function. Selenium dioxide, while less commonly recognized as a cofactor, can aid in the proper folding of the protein, which is important for its redox reaction catalysis. Additionally, alpha-ketoglutarate supplies substrates that are necessary for the protein's reductase activity. Nicotinamide, a component of NADPH, ensures a steady supply of necessary cofactors for the reducing reactions mediated by the protein. Isoalloxazine, the active portion of FAD and FMN, is essential for these redox reactions, reinforcing the protein's ability to facilitate electron transfer. Zinc sulfate can induce conformational changes in NADP+ dependent oxidoreductase domain containing 1, which can lead to enhanced catalytic efficiency. Ascorbic acid donates electrons, further facilitating the reductase reactions of the protein. Lastly, copper(II) sulfate may interact with the protein to improve substrate orientation and cofactor alignment within the active site, thus augmenting the protein's overall activity.
SEE ALSO...
| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
NADPH tetrasodium salt | 2646-71-1 | sc-202725 sc-202725A sc-202725B sc-202725C | 25 mg 50 mg 250 mg 1 g | $47.00 $84.00 $286.00 $754.00 | 11 | |
NADPH provides the reducing equivalents for antioxidant function and is utilized by NADP+ dependent oxidoreductase domain containing 1 for its reductase activity. The presence of NADPH directly enhances the catalytic activity of the protein by providing the necessary electrons for the reduction reactions it catalyzes. | ||||||
Glutathione, reduced | 70-18-8 | sc-29094 sc-29094A | 10 g 1 kg | $82.00 $2091.00 | 8 | |
Glutathione in its reduced form (GSH) serves as an electron donor in the detoxification of hydrogen peroxide, a process that NADP+ dependent oxidoreductase domain containing 1 can catalyze. The interaction with GSH activates the protein by enabling it to perform its antioxidative role more efficiently. | ||||||
Riboflavin | 83-88-5 | sc-205906 sc-205906A sc-205906B | 25 g 100 g 1 kg | $41.00 $112.00 $525.00 | 3 | |
Riboflavin, or vitamin B2, can be phosphorylated intracellularly to form flavin mononucleotide (FMN), a cofactor used by NADP+ dependent oxidoreductase domain containing 1. FMN is essential for the protein's activity as it participates in the redox reactions that the protein mediates. | ||||||
Selenium | 7782-49-2 | sc-250973 | 50 g | $62.00 | 1 | |
Selenium dioxide can act as a cofactor for certain redox enzymes and may assist in the proper folding and function of NADP+ dependent oxidoreductase domain containing 1. It can enhance the protein's ability to catalyze redox reactions, directly increasing its functional activation. | ||||||
α-Ketoglutaric Acid | 328-50-7 | sc-208504 sc-208504A sc-208504B sc-208504C sc-208504D sc-208504E sc-208504F | 25 g 100 g 250 g 500 g 1 kg 5 kg 16 kg | $33.00 $43.00 $63.00 $110.00 $188.00 $738.00 $2091.00 | 2 | |
Alpha-ketoglutarate participates in the tricarboxylic acid cycle and is also involved in redox homeostasis. It may directly supply the necessary substrates for NADP+ dependent oxidoreductase domain containing 1, which in turn could activate the protein's oxidoreductase activity by providing substrates for reduction. | ||||||
Nicotinamide | 98-92-0 | sc-208096 sc-208096A sc-208096B sc-208096C | 100 g 250 g 1 kg 5 kg | $44.00 $66.00 $204.00 $831.00 | 6 | |
Nicotinamide can be incorporated into NADPH molecules, which are used by NADP+ dependent oxidoreductase domain containing 1 as a cofactor. This directly increases the enzymatic activity of the protein by ensuring a sufficient supply of NADPH for its reducing reactions. | ||||||
Zinc | 7440-66-6 | sc-213177 | 100 g | $48.00 | ||
Zinc ions can serve as structural or catalytic cofactors for many enzymes. They may bind to NADP+ dependent oxidoreductase domain containing 1 and induce a conformational change that increases the protein's catalytic efficiency, thereby activating its reductase function. | ||||||
L-Ascorbic acid, free acid | 50-81-7 | sc-202686 | 100 g | $46.00 | 5 | |
Ascorbic acid, or vitamin C, can act as a reducing agent and thereby donate electrons to NADP+ dependent oxidoreductase domain containing 1. This electron donation can activate the protein by allowing it to carry out its reductase reactions more effectively. | ||||||
Copper(II) sulfate | 7758-98-7 | sc-211133 sc-211133A sc-211133B | 100 g 500 g 1 kg | $46.00 $122.00 $189.00 | 3 | |
Copper ions can interact with proteins that have oxidoreductase functions, potentially altering their structure and enhancing their enzymatic activity. In the case of NADP+ dependent oxidoreductase domain containing 1, copper(II) sulfate may bind and facilitate the proper orientation of substrates and cofactors within the active site, directly contributing to an increase in the protein's activity. | ||||||