GFAT2 inhibitors belong to a specific chemical class of compounds that target the enzyme Glutamine Fructose-6-Phosphate Amidotransferase 2 (GFAT2). This enzyme plays a critical role in the hexosamine biosynthetic pathway, which is responsible for generating UDP-N-acetylglucosamine (UDP-GlcNAc). UDP-GlcNAc serves as a crucial substrate for protein glycosylation, a post-translational modification process that affects the structure and function of numerous cellular proteins. By inhibiting GFAT2, these compounds disrupt the production of UDP-GlcNAc, thereby affecting protein glycosylation pathways.
GFAT2 inhibitors work by competitively binding to the active site of the GFAT2 enzyme, preventing its normal catalytic activity. This leads to a decrease in the overall availability of UDP-GlcNAc within cells, potentially altering the glycosylation patterns of proteins involved in various cellular processes. Consequently, these inhibitors have the potential to influence cellular signaling pathways, gene expression, protein trafficking, and other critical biological functions. The development and study of GFAT2 inhibitors are essential for understanding the underlying mechanisms of protein glycosylation and its implications for cellular physiology. Researchers and scientists explore the pharmacological effects of these inhibitors on different cellular models to uncover the roles of glycosylation in various cellular pathways. By elucidating the specific effects of GFAT2 inhibitors on protein glycosylation, these compounds can offer valuable insights into cellular regulation and may hold promise for future applications in various fields of research and potentially other contexts where glycosylation modulation is of interest.
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| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
Azaserine | 115-02-6 | sc-29063 sc-29063A | 50 mg 250 mg | $312.00 $924.00 | 15 | |
Azaserine functions as a glutamine analog, which inhibits GFAT2 by competing with glutamine for the enzyme's active site. This competitive inhibition disrupts the normal function of GFAT2, which is crucial for the hexosamine biosynthetic pathway, leading to decreased production of uridine diphosphate N-acetylglucosamine (UDP-GlcNAc). | ||||||
6-Diazo-5-oxo-L-norleucine | 157-03-9 | sc-227078 sc-227078A sc-227078B sc-227078C | 5 mg 25 mg 100 mg 250 mg | $88.00 $291.00 $926.00 $2195.00 | ||
DON acts as a glutamine antimetabolite that directly inhibits GFAT2 by mimicking glutamine, its natural substrate. This inhibition blocks the enzyme's ability to catalyze the formation of glucosamine-6-phosphate, effectively hindering the hexosamine biosynthesis pathway and the subsequent glycosylation processes. | ||||||
Acivicin | 42228-92-2 | sc-200498B sc-200498C sc-200498 sc-200498D | 1 mg 5 mg 10 mg 25 mg | $104.00 $416.00 $655.00 $1301.00 | 10 | |
Acivicin inhibits GFAT2 through its interaction with the enzyme's active site, where it forms a covalent bond with the catalytic cysteine residue. This binding prevents GFAT2 from converting fructose-6-phosphate and glutamine into glucosamine-6-phosphate, thereby disrupting the hexosamine biosynthesis pathway. | ||||||
BMS-754807 | 1001350-96-4 | sc-507396 | 5 mg | $304.00 | ||
BMS-754807 inhibits GFAT2 by binding to the ATP-binding site of the enzyme, preventing its kinase activity. This inhibition reduces the enzyme's ability to phosphorylate substrates involved in the hexosamine biosynthesis pathway, thereby decreasing the production of critical metabolites for glycosylation. | ||||||
Compound 48/80 trihydrochloride | 94724-12-6 | sc-200736 sc-200736A sc-200736B sc-200736C | 100 mg 250 mg 1 g 5 g | $104.00 $218.00 $843.00 $3756.00 | ||
Compound 48/80 trihydrochloride inhibits GFAT2 by disrupting the enzyme's structural integrity, leading to a loss of enzymatic activity. This inhibition affects the enzyme's capacity to catalyze the conversion of fructose-6-phosphate and glutamine to glucosamine-6-phosphate, crucial for the synthesis of UDP-GlcNAc and glycosylated proteins. | ||||||