Arylsulfatase J Inhibitors
Arylsulfatase J Inhibitors are a diverse set of chemical compounds that impede the enzyme's ability to hydrolyze sulfate esters, which is a critical function in various biological processes. Oxidizing agents like Sodium Chlorate can inactivate the enzyme by modifying the critical cysteine residue in its active site, while compounds such as Heparin and Suramin directly bind to Arylsulfatase J, obstructing substrate access and inducing conformational changes that decrease enzymatic activity. Phenylmethylsulfonyl Fluoride and 1,8-Dihydroxyanthraquinone inhibit the enzyme by covalently modifying or intercalating in its active site, respectively, which prevents substrate binding and diminishes Arylsulfatase J's catalytic function.
Further disrupting Arylsulfatase J's activity are compounds that affect the enzyme indirectly; for example, Warfarin, by inhibiting vitamin K epoxide reductase, could lead to the accumulation of sulfatase substrates, thereby reducing Arylsulfatase J's efficiency. Copper Sulfate and Lead Acetate interfere with the enzyme's structure and metal cofactor binding, causing denaturation and loss of activity. Molybdate competes with the enzyme's natural substrates as a sulfate analog, while Disulfiram modifies the cysteine residues essential for its activity. Chloroquine alters the lysosomal pH, impairing the acidic environment required for Arylsulfatase J, and Methotrexate leads to a decrease in macromolecule synthesis, which could impact enzyme stability and function. Collectively, these inhibitors utilize a range of mechanisms to effectively diminish the functional activity of Arylsulfatase J.
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Items 1 to 10 of 11 total
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| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
Sodium chlorate | 7775-09-9 | sc-212938 | 100 g | $58.00 | 1 | |
Sodium chlorate is an oxidizing agent that leads to the oxidation of the critical cysteine residue in the active site of sulfatases, such as Arylsulfatase J, resulting in enzyme inactivation. | ||||||
Heparin | 9005-49-6 | sc-507344 | 25 mg | $117.00 | 1 | |
Heparin binds to Arylsulfatase J and diminishes its activity by inducing conformational changes that disrupt the enzyme's active site availability, hindering its ability to hydrolyze sulfate esters. | ||||||
Suramin sodium | 129-46-4 | sc-507209 sc-507209F sc-507209A sc-507209B sc-507209C sc-507209D sc-507209E | 50 mg 100 mg 250 mg 1 g 10 g 25 g 50 g | $149.00 $210.00 $714.00 $2550.00 $10750.00 $21410.00 $40290.00 | 5 | |
Suramin acts as an inhibitor by binding to the active site of Arylsulfatase J, blocking substrate access and therefore diminishing the enzyme's sulfatase function. | ||||||
Phenylmethylsulfonyl Fluoride | 329-98-6 | sc-3597 sc-3597A | 1 g 100 g | $50.00 $683.00 | 92 | |
Phenylmethylsulfonyl Fluoride is a serine protease inhibitor that can irreversibly bind to the serine residue within the active site of certain hydrolases. For Arylsulfatase J, it would diminish activity through covalent modification of the active site. | ||||||
Warfarin | 81-81-2 | sc-205888 sc-205888A | 1 g 10 g | $72.00 $162.00 | 7 | |
Warfarin competitively inhibits vitamin K epoxide reductase, which indirectly could lead to the accumulation of sulfatase substrates, potentially overloading and diminishing Arylsulfatase J's catalytic efficiency. | ||||||
Copper(II) sulfate | 7758-98-7 | sc-211133 sc-211133A sc-211133B | 100 g 500 g 1 kg | $45.00 $120.00 $185.00 | 3 | |
Copper ions can bind to and cause the denaturation of proteins like Arylsulfatase J, which would result in a loss of enzymatic activity due to the alteration of tertiary and quaternary structures. | ||||||
Sodium molybdate | 7631-95-0 | sc-236912 sc-236912A sc-236912B | 5 g 100 g 500 g | $55.00 $82.00 $316.00 | 1 | |
Molybdate acts as a sulfate analog and can competitively inhibit sulfatases, including Arylsulfatase J, by mimicking the enzyme's natural substrate, thereby diminishing its activity. | ||||||
Disulfiram | 97-77-8 | sc-205654 sc-205654A | 50 g 100 g | $52.00 $87.00 | 7 | |
Disulfiram can inhibit Arylsulfatase J by modifying the cysteine residues within the enzyme's active site, thus diminishing its ability to cleave sulfate groups from substrates. | ||||||
Chloroquine | 54-05-7 | sc-507304 | 250 mg | $68.00 | 2 | |
Chloroquine accumulates in lysosomes and raises their pH, which can impede the function of lysosomal enzymes like Arylsulfatase J by disrupting the acidic environment required for optimal activity. | ||||||
Methotrexate | 59-05-2 | sc-3507 sc-3507A | 100 mg 500 mg | $92.00 $209.00 | 33 | |
Methotrexate inhibits dihydrofolate reductase, leading to decreased purine synthesis and potentially reduced synthesis of macromolecules necessary for the stability and function of enzymes like Arylsulfatase J. | ||||||