IMPA1 Inhibitors
Chemical inhibitors of IMPA1 can directly compete with the enzyme's natural substrate or indirectly affect its activity through alterations in cellular ATP levels. Lithium chloride inhibits IMPA1 by competing with magnesium ions, which are crucial cofactors for the enzyme's function. Without magnesium, IMPA1 cannot catalyze the conversion of myo-inositol-1-phosphate to myo-inositol. Similarly, L-690,330 and L-690,488 are competitive inhibitors that resemble the structure of IMPA1's substrate, thereby preventing the actual substrate from binding to the active site and halting myo-inositol production. These inhibitors exploit the precise substrate recognition capability of IMPA1 to achieve inhibition.
In contrast, other chemicals such as Carbonyl cyanide m-chlorophenyl hydrazone (CCCP), 3,3-Diindolylmethane (DIM), and 2,3-Dichloro-1,4-naphthoquinone (DCNQ) indirectly inhibit IMPA1 by disrupting cellular processes that result in reduced ATP synthesis, a molecule required for IMPA1's enzymatic action. CCCP disrupts mitochondrial membrane potential, impairing ATP production and thereby reducing IMPA1 activity. DIM modulates the PI3K/Akt signaling pathway, which is involved in ATP generation, while DCNQ interferes with redox reactions, potentially diminishing ATP levels. Furthermore, Ebselen alters the intracellular redox state, and 5-Iodoindole interferes with tryptophan metabolism, both leading to a potential decrease in cellular ATP and inhibiting IMPA1. Genistein affects ATP production by inhibiting tyrosine kinase activity within the PI3K/Akt pathway. Sodium orthovanadate inhibits phosphatases that regulate ATP production pathways, while Oligomycin A directly inhibits mitochondrial ATP synthase, both leading to a decrease in ATP available for IMPA1. Lastly, Bithionol disrupts energy metabolism, culminating in reduced ATP synthesis and consequential inhibition of IMPA1. These inhibitors showcase a variety of mechanisms to decrease the functional activity of IMPA1 by targeting the enzyme's reliance on ATP for catalysis.
SEE ALSO...
| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
Lithium | 7439-93-2 | sc-252954 | 50 g | $214.00 | ||
Lithium chloride can inhibit IMPA1 by competing with magnesium ions, which are cofactors necessary for IMPA1's catalytic activity. Without magnesium, IMPA1 cannot properly catalyze the conversion of myo-inositol-1-phosphate to myo-inositol, thus effectively inhibiting the enzyme's function. | ||||||
Carbonyl Cyanide m-Chlorophenylhydrazone | 555-60-2 | sc-202984A sc-202984 sc-202984B | 100 mg 250 mg 500 mg | $77.00 $153.00 $240.00 | 8 | |
CCCP can indirectly inhibit IMPA1 by disrupting mitochondrial membrane potential, which is essential for ATP production. Since IMPA1 requires ATP to function, the reduction in ATP levels due to CCCP's action would result in a functional inhibition of IMPA1 activity. | ||||||
3,3′-Diindolylmethane | 1968-05-4 | sc-204624 sc-204624A sc-204624B sc-204624C sc-204624D sc-204624E | 100 mg 500 mg 5 g 10 g 50 g 1 g | $37.00 $65.00 $89.00 $421.00 $681.00 $66.00 | 8 | |
DIM can exert an indirect inhibitory effect on IMPA1 by modulating the PI3K/Akt signaling pathway, which is involved in cellular survival and metabolism, potentially altering the energy dynamics and indirectly inhibiting enzymes like IMPA1 that depend on ATP. | ||||||
2,3-Dichloro-1,4-naphthoquinone | 117-80-6 | sc-254313 | 5 g | $24.00 | ||
DCNQ can indirectly inhibit IMPA1 by interfering with cellular redox reactions and quinone-dependent enzymes, leading to a potential reduction in ATP synthesis. A decrease in ATP availability can inhibit IMPA1 function, as the enzyme requires ATP to convert myo-inositol-1-phosphate into myo-inositol. | ||||||
Ebselen | 60940-34-3 | sc-200740B sc-200740 sc-200740A | 1 mg 25 mg 100 mg | $33.00 $136.00 $458.00 | 5 | |
Ebselen can indirectly inhibit IMPA1 by mimicking glutathione peroxidase activity, thus altering the intracellular redox state which could affect the metabolic pathways and energy balance within the cell, potentially leading to a decrease in ATP levels and subsequent inhibition of ATP-dependent enzymes like IMPA1. | ||||||
5-Iodoindole | 16066-91-4 | sc-254836 | 5 g | $89.00 | ||
5-Iodoindole can interfere with tryptophan metabolism, which may indirectly affect the biosynthesis of NAD, a cofactor that participates in ATP production. Reduced NAD and ATP levels may lead to functional inhibition of IMPA1 due to insufficient cofactor availability for its enzymatic action. | ||||||
Genistein | 446-72-0 | sc-3515 sc-3515A sc-3515B sc-3515C sc-3515D sc-3515E sc-3515F | 100 mg 500 mg 1 g 5 g 10 g 25 g 100 g | $45.00 $164.00 $200.00 $402.00 $575.00 $981.00 $2031.00 | 46 | |
Genistein, a tyrosine kinase inhibitor, can indirectly inhibit IMPA1 by impacting the PI3K/Akt signaling pathway, which in turn could affect ATP production and availability. Since IMPA1 requires ATP for its enzymatic activity, disruption of ATP synthesis would inhibit the function of IMPA1. | ||||||
Sodium Orthovanadate | 13721-39-6 | sc-3540 sc-3540B sc-3540A | 5 g 10 g 50 g | $49.00 $57.00 $187.00 | 142 | |
Sodium orthovanadate is a phosphatase inhibitor that can indirectly affect IMPA1 function by inhibiting the dephosphorylation of signaling molecules involved in pathways that regulate ATP production, potentially leading to reduced ATP levels and consequent inhibition of ATP-dependent enzymes like IMPA1. | ||||||
Oligomycin A | 579-13-5 | sc-201551 sc-201551A sc-201551B sc-201551C sc-201551D | 5 mg 25 mg 100 mg 500 mg 1 g | $179.00 $612.00 $1203.00 $5202.00 $9364.00 | 26 | |
Oligomycin A inhibits mitochondrial ATP synthase, leading to a decrease in ATP production. Since IMPA1 is an ATP-dependent enzyme, the reduction in ATP synthesis indirectly inhibits IMPA1 activity by reducing the enzyme's access to the necessary ATP for its catalytic function. | ||||||
Bithionol | 97-18-7 | sc-239383 | 25 g | $79.00 | ||
Bithionol can indirectly inhibit IMPA1 by altering the energy metabolism and ATP synthesis pathways within the cell. As a result, the availability of ATP for IMPA1's catalytic activity is reduced, leading to functional inhibition of the enzyme. | ||||||