HGD Inhibitors
Chemical inhibitors of Homogentisate 1,2-dioxygenase (HGD) can be diverse in their structure and mode of action. Methimazole is a thiourea derivative that, due to its structural resemblance to tyrosine, can competitively inhibit HGD. It can achieve this by inserting itself into the active site of HGD, thus preventing the enzyme from metabolizing homogentisic acid, its natural substrate. Similarly, allopurinol has a molecular structure that allows it to bind to the active site of HGD. This binding can prevent homogentisic acid from being metabolized by HGD. Phenylbutazone, another inhibitor, has structural similarities to phenolic compounds that are substrates of dioxygenases. Because HGD falls into this enzyme category, phenylbutazone can block the enzyme's active site, inhibiting the breakdown of homogentisic acid.
Other compounds, such as nitisinone, act upstream of HGD in the tyrosine degradation pathway. By inhibiting 4-hydroxyphenylpyruvate dioxygenase, nitisinone can cause an increase in tyrosine levels, which in turn can lead to a decrease in HGD activity through feedback inhibition mechanisms. Febuxostat and sulfinpyrazone, both xanthine oxidase inhibitors, possess structures that enable them to interact with the HGD active site. Their binding can obstruct the access of homogentisic acid to the active site, thereby inhibiting the activity of HGD. Tungsten (VI) oxide and molybdenum (VI) oxide can influence HGD by potentially altering the metal environment within the active site of this metalloenzyme, which can inhibit its activity. Quercetin can bind to enzymes requiring specific organic molecules for their activity and can inhibit HGD by blocking its active site. Theophylline can bind to the active site of HGD and inhibit its function. Folic acid, in elevated concentrations, can interfere with the cofactors needed for HGD activity, while pyrazinamide can inhibit HGD by occupying its active site and preventing the natural substrate metabolism. Each of these chemicals can affect HGD's ability to catalyze the oxidation of homogentisic acid, a critical step in the catabolic pathway of tyrosine.
| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
Methimazole | 60-56-0 | sc-205747 sc-205747A | 10 g 25 g | $70.00 $112.00 | 4 | |
Methimazole is a thiourea derivative that acts as an inhibitor of the enzyme thyroid peroxidase. Homogentisate 1,2-dioxygenase (HGD), the protein in question, is involved in the catabolism of tyrosine. Methimazole's structural similarity to the amino acid tyrosine could allow it to interact with the active site of HGD, competitively inhibiting its function in breaking down tyrosine. | ||||||
Allopurinol | 315-30-0 | sc-207272 | 25 g | $131.00 | ||
Allopurinol is primarily known to inhibit xanthine oxidase, an enzyme involved in purine metabolism. HGD also operates in a metabolic pathway, specifically the degradation of tyrosine. Allopurinol could theoretically inhibit HGD by binding to its active site due to structural similarities to substrates of HGD, thereby preventing the breakdown of homogentisic acid by HGD. | ||||||
Phenylbutazone | 50-33-9 | sc-204843 | 5 g | $32.00 | 1 | |
Phenylbutazone, an anti-inflammatory drug, has structural similarities to phenolic compounds that are substrates or inhibitors of dioxygenases. Since HGD is a dioxygenase, phenylbutazone could bind to the active site of HGD, inhibiting its ability to metabolize homogentisic acid. | ||||||
Febuxostat | 144060-53-7 | sc-207680 | 10 mg | $168.00 | 3 | |
Febuxostat, a selective xanthine oxidase inhibitor, has a molecular structure that could theoretically allow it to bind to the active site of HGD. This binding could inhibit the normal function of HGD by competitively blocking the access of its natural substrate. | ||||||
(±)-Sulfinpyrazone | 57-96-5 | sc-202822 sc-202822A | 1 g 5 g | $42.00 $94.00 | 2 | |
Sulfinpyrazone is an inhibitor of xanthine oxidase and has structural features that could enable it to interact with dioxygenases like HGD. Sulfinpyrazone could inhibit HGD by mimicking its natural substrates, leading to a decrease in its enzymatic activity. | ||||||
Quercetin | 117-39-5 | sc-206089 sc-206089A sc-206089E sc-206089C sc-206089D sc-206089B | 100 mg 500 mg 100 g 250 g 1 kg 25 g | $11.00 $17.00 $110.00 $250.00 $936.00 $50.00 | 33 | |
Quercetin is a flavonoid known to inhibit a wide range of enzymes. Due to its structure, it could bind to the active sites of enzymes like HGD, which may require specific organic molecules for activity, leading to inhibition of HGD function. | ||||||
Theophylline | 58-55-9 | sc-202835 sc-202835A sc-202835B | 5 g 25 g 100 g | $20.00 $32.00 $85.00 | 6 | |
Theophylline, similar to other xanthine derivatives, has the potential to inhibit various enzymes. Due to its structural properties, it could bind to the active site of HGD, potentially inhibiting its activity in metabolizing homogentisic acid. | ||||||
Folic Acid | 59-30-3 | sc-204758 | 10 g | $73.00 | 2 | |
Folic acid, a B vitamin, is essential for various metabolic processes, including amino acid metabolism. While not a direct inhibitor, folic acid in high concentrations could compete with the cofactors required by HGD for its activity, thereby reducing its function. | ||||||
Pyrazinamide | 98-96-4 | sc-205824 sc-205824A sc-205824B sc-205824C sc-205824D sc-205824E | 10 g 25 g 100 g 250 g 1 kg 5 kg | $49.00 $67.00 $89.00 $151.00 $483.00 $2276.00 | ||
Pyrazinamide is an antimycobacterial agent that has been shown to inhibit various enzymes. It could theoretically inhibit HGD by binding to its active site, thereby preventing HGD from metabolizing its natural substrates. | ||||||