ALDH3B1 include a variety of compounds that can enhance the enzyme's activity through different mechanisms. NAD+, a co-substrate, directly facilitates the catalytic function of ALDH3B1 by accepting electrons during the conversion of aldehydes to carboxylic acids. Retinoic acid, by serving as a substrate, enables ALDH3B1 to catalyze its oxidation. In an unorthodox manner, Disulfiram, traditionally an inhibitor, at lower concentrations can bind to ALDH3B1 and induce a conformational change that increases its substrate affinity, thus enhancing enzymatic activity. Similarly, Alda-1, while primarily associated with ALDH2, may activate ALDH3B1 through an analogous binding and stabilization process.
Sulforaphane, known for inducing phase II detoxification enzymes, can foster an environment that upregulates ALDH3B1 activity as part of a cellular response to oxidative stress. Therefore, its role is more indirect but pivotal in boosting ALDH3B1 function. Polydatin and Resveratrol engage in the activation of metabolic pathways that can lead to the upregulation of ALDH3B1. Polydatin does this through the activation of AMP-activated protein kinase, which is known to enhance cellular antioxidant defenses, while Resveratrol activates SIRT1, affecting the cellular stress response mechanisms, thereby enhancing ALDH3B1 activity. Furthermore, 4-Hydroxynonenal, a specific substrate of ALDH3B1 produced during lipid peroxidation, increases the enzyme's activity by providing a substrate for detoxification. Similarly, Acetaldehyde and Benzaldehyde, also substrates for ALDH3B1, promote its activity by being readily available for enzymatic conversion to less reactive molecules. Additionally, cellular metabolites like Fumarate and Malonate, although not substrates, can modulate the activity of dehydrogenases, including ALDH3B1, by affecting the intracellular redox state and NAD+/NADH ratio.
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| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
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 | |
NAD+ serves as a co-substrate for ALDH3B1, which is an aldehyde dehydrogenase. By providing the necessary electron acceptor for the enzymatic reaction where ALDH3B1 converts aldehydes to carboxylic acids, NAD+ directly enhances the catalytic activity of ALDH3B1. | ||||||
Retinoic Acid, all trans | 302-79-4 | sc-200898 sc-200898A sc-200898B sc-200898C | 500 mg 5 g 10 g 100 g | $65.00 $319.00 $575.00 $998.00 | 28 | |
Retinoic acid interacts with aldehyde dehydrogenase enzymes as a substrate. Although primarily associated with ALDH1, retinoic acid could enhance the activity of ALDH3B1 by serving as a substrate, thus promoting the oxidation process that ALDH3B1 facilitates. | ||||||
Disulfiram | 97-77-8 | sc-205654 sc-205654A | 50 g 100 g | $52.00 $87.00 | 7 | |
Disulfiram is an ALDH inhibitor, but at sub-inhibitory concentrations, it could paradoxically increase ALDH3B1 activity by binding to regulatory sites, causing a conformational change that enhances the enzyme's affinity for its substrates without completely inhibiting it. | ||||||
D,L-Sulforaphane | 4478-93-7 | sc-207495A sc-207495B sc-207495C sc-207495 sc-207495E sc-207495D | 5 mg 10 mg 25 mg 1 g 10 g 250 mg | $150.00 $286.00 $479.00 $1299.00 $8299.00 $915.00 | 22 | |
Sulforaphane is known to induce phase II detoxification enzymes and could potentially increase the catalytic efficiency of ALDH3B1 by inducing a cellular environment that favors the oxidative stress response, where ALDH3B1 plays a role. | ||||||
Alda 1 | 349438-38-6 | sc-479867 | 50 mg | $300.00 | ||
Alda-1 enhances the activity of aldehyde dehydrogenases by binding to and stabilizing their active form. Although it is specific to ALDH2, similar aldehyde dehydrogenases like ALDH3B1 could also be activated through a similar mechanism of action. | ||||||
Polydatin | 65914-17-2 | sc-203203 | 10 mg | $92.00 | 5 | |
Polydatin is a stilbenoid that has been shown to activate AMP-activated protein kinase (AMPK), which in turn can enhance cellular antioxidant defenses. This activation could lead to an increased activity of ALDH3B1 as part of the cellular response to oxidative stress. | ||||||
Resveratrol | 501-36-0 | sc-200808 sc-200808A sc-200808B | 100 mg 500 mg 5 g | $60.00 $185.00 $365.00 | 64 | |
Resveratrol activates SIRT1, which is involved in the deacetylation of proteins and impacts cellular stress responses. Through the activation of SIRT1, resveratrol could enhance the activity of ALDH3B1 as part of the cellular protective mechanisms against oxidative damage. | ||||||
4-Hydroxynonenal | 75899-68-2 | sc-202019 sc-202019A sc-202019B | 1 mg 10 mg 50 mg | $116.00 $642.00 $2720.00 | 25 | |
4-Hydroxynonenal is a product of lipid peroxidation and a substrate for ALDH3B1. The presence of 4-Hydroxynonenal could increase the catalytic activity of ALDH3B1 by being a specific substrate that the enzyme acts upon to protect cells from oxidative stress. | ||||||
Fumaric acid | 110-17-8 | sc-250031 sc-250031A sc-250031B sc-250031C | 25 g 100 g 500 g 2.5 kg | $42.00 $56.00 $112.00 $224.00 | ||
Fumarate is a Krebs cycle intermediate that can stimulate the activity of various dehydrogenases. While not a direct substrate of ALDH3B1, the presence of fumarate could promote the dehydrogenase activity, including that of ALDH3B1, within the cellular environment. | ||||||