Date published: 2025-9-13

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GFRP Inhibitors

GFRP inhibitors constitute a class of chemical compounds that have attracted attention in the fields of molecular biology and pharmacology due to modulating specific cellular processes. GFRP, or Glutamine:Fructose-6-Phosphate Amidotransferase Regulatory Protein, is a protein that plays a pivotal role in regulating the activity of the enzyme Glutamine:Fructose-6-Phosphate Amidotransferase (GFAT). This enzyme is a key player in the hexosamine biosynthetic pathway, a metabolic pathway that contributes to the synthesis of UDP-N-acetylglucosamine (UDP-GlcNAc). UDP-GlcNAc serves as a critical substrate for post-translational modification of proteins, such as protein glycosylation, and has implications in various cellular processes, including insulin signaling and cellular response to nutrient availability. GFRP inhibitors are designed to interact with the active site or binding domain of the GFRP protein, effectively inhibiting its function and influencing cellular processes dependent on GFAT-mediated hexosamine biosynthesis.

Structurally, GFRP inhibitors are engineered to selectively target the active site of GFRP, ensuring high specificity for this particular regulatory protein. By inhibiting GFRP, these compounds may disrupt its role in regulating GFAT activity, impacting hexosamine biosynthesis and the subsequent protein glycosylation events in cells. The study of GFRP inhibitors is of significant interest to researchers as it provides insights into the regulatory mechanisms governing essential cellular functions related to nutrient sensing, protein modification, and cellular responses to metabolic changes. This knowledge contributes to our understanding of basic cell biology and may have implications in various research areas, including diabetes research, metabolic disorders, and the molecular basis of diseases associated with altered protein glycosylation. However, further research is required to fully explore the extent of their applications and their impact on cellular physiology in the context of GFAT-mediated hexosamine biosynthesis.

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