Date published: 2026-5-18

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Aasdh Inhibitors

Aasdh Inhibitors are a specific class of chemical compounds that target the Aasdh (Aminoadipate-semialdehyde dehydrogenase) enzyme, a key player in the metabolic pathways involved in the breakdown of lysine and other amino acids. These inhibitors function by binding to the active site or other crucial regions of the Aasdh enzyme, thereby blocking its catalytic activity. The inhibition occurs when the inhibitor molecule interacts with the enzyme in a way that either mimics the natural substrate or occupies the active site, preventing the enzyme from processing its normal substrates. This interaction often results in a conformational change in the enzyme, which can significantly reduce or completely halt its activity, disrupting the associated metabolic pathways. The specificity of Aasdh Inhibitors is typically achieved through the careful design of their molecular structures, which are tailored to fit precisely within the unique active sites of the Aasdh enzyme.

The chemical properties of Aasdh Inhibitors, such as molecular weight, solubility, and stability, are essential factors that influence their effectiveness in interacting with the Aasdh enzyme. These inhibitors are often designed with a combination of hydrophobic and hydrophilic regions, allowing them to form strong interactions with both the non-polar and polar amino acid residues within the enzyme's active site. Additionally, the inhibitors may include specific functional groups, such as carbonyl or hydroxyl groups, that facilitate binding through hydrogen bonding or other non-covalent interactions. The binding kinetics of these inhibitors, including the rates of association and dissociation, are critical in determining how effectively they can modulate the activity of Aasdh. By studying these interactions, researchers can gain valuable insights into the enzyme's role in amino acid metabolism and the broader implications of its inhibition on metabolic processes. Understanding the detailed molecular interactions between Aasdh Inhibitors and the enzyme helps elucidate the complex biochemical pathways that are essential for maintaining cellular and organismal homeostasis.

SEE ALSO...

Product NameCAS #Catalog #QUANTITYPriceCitationsRATING

Disulfiram

97-77-8sc-205654
sc-205654A
50 g
100 g
$53.00
$89.00
7
(1)

Disulfiram can inhibit aminoadipate-semialdehyde dehydrogenase by chelating with metal ions that are essential for the catalytic activity of the enzyme.

Fomepizole

7554-65-6sc-252838
1 g
$75.00
1
(1)

Fomepizole can inhibit aminoadipate-semialdehyde dehydrogenase by acting as an alternative substrate, binding to the active site and preventing the enzyme from processing its natural substrate.

Methylglyoxal solution

78-98-8sc-250394
sc-250394A
sc-250394B
sc-250394C
sc-250394D
25 ml
100 ml
250 ml
500 ml
1 L
$146.00
$437.00
$478.00
$754.00
$1446.00
3
(3)

Methylglyoxal can inhibit aminoadipate-semialdehyde dehydrogenase by modifying the enzyme's active site, leading to enzyme inactivation.

Sulfasalazine

599-79-1sc-204312
sc-204312A
sc-204312B
sc-204312C
1 g
2.5 g
5 g
10 g
$61.00
$77.00
$128.00
$209.00
8
(1)

Sulfasalazine can inhibit aminoadipate-semialdehyde dehydrogenase by interfering with the enzyme's redox status, which is crucial for its catalytic cycle.

Oltipraz

64224-21-1sc-205777
sc-205777A
500 mg
1 g
$286.00
$622.00
(1)

Oltipraz can inhibit aminoadipate-semialdehyde dehydrogenase by conjugation with the enzyme's thiol groups, which are essential for the catalytic mechanism.

Vitamin K3

58-27-5sc-205990B
sc-205990
sc-205990A
sc-205990C
sc-205990D
5 g
10 g
25 g
100 g
500 g
$26.00
$36.00
$47.00
$136.00
$455.00
3
(1)

Menadione can inhibit aminoadipate-semialdehyde dehydrogenase by redox cycling, depleting essential cofactors required for the enzyme's activity.

Chlorpromazine

50-53-3sc-357313
sc-357313A
5 g
25 g
$61.00
$110.00
21
(1)

Chlorpromazine can inhibit aminoadipate-semialdehyde dehydrogenase by intercalating in the enzyme's structure, which disturbs the conformation necessary for its activity.