GLYATL2 inhibitors encompass a variety of compounds that interfere with the enzyme's ability to conjugate glycine to acyl-CoA substrates, which is a key process in the metabolism and detoxification pathways. Acetyl-CoA, a primary substrate for GLYATL2, can induce substrate inhibition when present in excessive amounts, which could decrease the enzyme's activity. Similarly, malonyl-CoA competes with acetyl-CoA and other acyl-CoA molecules, leading to a reduced enzymatic function of GLYATL2 due to substrate competition. Hydroxylamine and methylglyoxal can deplete or modify GLYATL2's substrates, while high levels of glycine itself can lead to feedback inhibition.
Additionally, certain organic acids like benzoic and salicylic acid, which undergo conjugation with glycine, could serve as competitive inhibitors, further decreasing the functional activity of GLYATL2. Phenylacetate, which conjugates with glutamine, may reduce the availability of acyl-CoA substrates for GLYATL2. Disruption of cellular membranes by bile acids such as deoxycholic acid could affect the stability and localization of GLYATL2, impairing its function.
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| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
Acetyl coenzyme A trisodium salt | 102029-73-2 | sc-210745 sc-210745A sc-210745B | 1 mg 5 mg 1 g | $47.00 $92.00 $5826.00 | 3 | |
Acetyl-CoA is a substrate for GLYATL2 in the conjugation of glycine with acyl-CoA substrates, producing acylglycines. An oversupply of Acetyl-CoA could lead to substrate inhibition of GLYATL2, reducing its activity through mass action. | ||||||
Hydroxylamine solution | 7803-49-8 | sc-250136 | 100 ml | $72.00 | ||
Hydroxylamine can react with acyl-CoA esters, potentially depleting GLYATL2 substrates and reducing its activity indirectly by limiting substrate availability. | ||||||
Glycine | 56-40-6 | sc-29096A sc-29096 sc-29096B sc-29096C | 500 g 1 kg 3 kg 10 kg | $41.00 $71.00 $112.00 $357.00 | 15 | |
As a substrate for GLYATL2, elevated levels of glycine can cause feedback inhibition, potentially reducing the activity of GLYATL2 through substrate excess. | ||||||
Methylglyoxal solution | 78-98-8 | sc-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 | |
Methylglyoxal is a by-product of glycolysis that can adduct to and modify proteins. If it modifies GLYATL2's substrates, it could decrease GLYATL2's activity by reducing the availability of proper substrates. | ||||||
Benzoic acid | 65-85-0 | sc-203317 sc-203317A sc-203317B | 25 g 100 g 500 g | $20.00 $51.00 $61.00 | ||
Benzoic acid is conjugated by glycine in the liver to form hippuric acid and could compete with GLYATL2 substrates, potentially decreasing GLYATL2 activity through competitive inhibition. | ||||||
Salicylic acid | 69-72-7 | sc-203374 sc-203374A sc-203374B | 100 g 500 g 1 kg | $47.00 $94.00 $119.00 | 3 | |
Salicylic acid undergoes glycine conjugation to form salicyluric acid. High concentrations can act as a competitive inhibitor for GLYATL2, reducing its functional activity. | ||||||
Deoxycholic acid | 83-44-3 | sc-214865 sc-214865A sc-214865B | 5 g 25 g 1 kg | $37.00 $67.00 $941.00 | 4 | |
Deoxycholic acid can disrupt cellular membranes, potentially affecting the stability and function of membrane-associated enzymes like GLYATL2. | ||||||
N-Ethylmaleimide | 128-53-0 | sc-202719A sc-202719 sc-202719B sc-202719C sc-202719D | 1 g 5 g 25 g 100 g 250 g | $22.00 $69.00 $214.00 $796.00 $1918.00 | 19 | |
NEM can alkylate the cysteine residues in proteins, potentially modifying GLYATL2 at critical cysteine residues and inhibiting its enzymatic activity. | ||||||
Sodium arsenite, 0.1N Standardized Solution | 7784-46-5 | sc-301816 | 500 ml | $130.00 | 4 | |
Arsenite can bind to vicinal thiols, potentially modifying the active site of GLYATL2 or its substrates, leading to inhibition of its enzymatic activity. | ||||||