GLYATL1 Inhibitors
GLYATL1 inhibitors comprise a diverse set of compounds that can interfere with various biochemical and cellular pathways to reduce the enzyme's functional activity. Glyoxylate, the enzyme's substrate, when in excess, can lead to substrate inhibition of GLYATL1. The overabundance of glyoxylate hinders the enzyme's ability to process other substrates by occupying the active site without undergoing conversion. Pyruvate, a central metabolite, when diverted towards alanine formation, minimizes available amino groups for conjugation reactions carried out by GLYATL1. This results in a decreased enzyme activity due to limited substrate availability. Acetyl-CoA, in surplus, can lead to non-specific acetylation of lysine residues, which might alter GLYATL1's activity if such modifications occur on the enzyme itself. α-Ketoglutarate, another cellular metabolite, when excessively aminated to glutamate, competes with glycine, thus reducing GLYATL1's capacity to conjugate its natural substrate.
Hydroxypyruvate, a structural analog of glyoxylate, competes with the natural substrate for GLYATL1's active site, leading to competitive inhibition. Malonate, through its inhibition of the Krebs cycle, can cause an accumulation of succinate, which might suppress α-ketoglutarate-dependent dioxygenases, indirectly affecting GLYATL1's function. Oxamate and its sodium salt, by inhibiting lactate dehydrogenase, shunt pyruvate away from transamination reactions, thereby indirectly limiting GLYATL1 activity. Dichloroacetate, by shifting the balance towards pyruvate dehydrogenase, might limit GLYATL1 function indirectly through reduced pyruvate availability. Methotrexate, by reducing tetrahydrofolate production, indirectly diminishes glycine synthesis, thus inhibiting GLYATL1. Arsenic trioxide, through the oxidation of protein thiols, can inactivate GLYATL1 if critical cysteine residues are modified. Lastly, dimethyl fumarate might inhibit GLYATL1 by modifying cysteine residues, affecting the enzyme's structure and charge, leading to decreased activity.
SEE ALSO...
| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
Glyoxylic acid solution | 298-12-4 | sc-255190 | 250 g | $40.00 | ||
Glyoxylate acts as a substrate for GLYATL1, and its overabundance can lead to substrate inhibition. When present in excess, glyoxylate can bind to the active site of GLYATL1 without being converted efficiently, thereby reducing the enzyme's ability to process other substrates. | ||||||
Pyruvic acid | 127-17-3 | sc-208191 sc-208191A | 25 g 100 g | $41.00 $96.00 | ||
Pyruvate, a key intermediate in glycolysis, can be transaminated to form alanine, decreasing the availability of amino groups for conjugation reactions that GLYATL1 mediates. This indirect effect can reduce the functional activity of GLYATL1 by limiting its substrate availability. | ||||||
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-Coenzyme A, when in surplus, can lead to the acetylation of lysine residues on enzymes, potentially modifying the activity of GLYATL1. If acetylated on critical lysine residues, the function of GLYATL1 could be inhibited due to a conformational change or altered charge state that reduces its enzymatic activity. | ||||||
Sodium dichloroacetate | 2156-56-1 | sc-203275 sc-203275A | 10 g 50 g | $55.00 $209.00 | 6 | |
Dichloroacetate stimulates pyruvate dehydrogenase activity, which can decrease the availability of pyruvate for transamination reactions. Reduced transamination can increase the availability of amino groups for GLYATL1's conjugation reactions. However, excessive stimulation of pyruvate dehydrogenase can lead to a significant reduction in pyruvate levels, indirectly inhibiting GLYATL1 function. | ||||||
Methotrexate | 59-05-2 | sc-3507 sc-3507A | 100 mg 500 mg | $94.00 $213.00 | 33 | |
Methotrexate inhibits dihydrofolate reductase, leading to reduced production of tetrahydrofolate and its derivatives. These derivatives are required for one-carbon metabolism, which is crucial for the synthesis of glycine, a substrate for GLYATL1. Reduced availability of glycine indirectly inhibits the activity of GLYATL1. | ||||||
Arsenic(III) oxide | 1327-53-3 | sc-210837 sc-210837A | 250 g 1 kg | $89.00 $228.00 | ||
Arsenic trioxide can lead to the oxidation of protein thiols and the formation of mixed disulfides between protein thiol groups and low-molecular-weight thiols. If critical cysteine residues in GLYATL1 undergo oxidation, this can inhibit its activity through the modification of its active site, leading to functional inhibition. | ||||||
Dimethyl fumarate | 624-49-7 | sc-239774 | 25 g | $28.00 | 6 | |
Dimethyl fumarate modifies cysteine residues on Keap1, leading to the activation of Nrf2 and the expression of detoxification enzymes. If cysteine residues essential to the catalytic function of GLYATL1 are similarly modified, this could inhibit GLYATL1 activity by altering its structural conformation or charge state. | ||||||
Sodium oxamate | 565-73-1 | sc-215880 sc-215880B sc-215880C sc-215880D sc-215880A | 5 g 100 g 250 g 1 kg 25 g | $77.00 $469.00 $1106.00 $4111.00 $152.00 | 14 | |
Sodium oxamate is the sodium salt of oxamate | ||||||