L-Glutamine 7-amido-4-methylcoumarin hydrobromide is a fluorogenic amino acid derivative designed for monitoring enzymatic cleavage. The coumarin tag enables sensitive detection of reaction progression and substrate turnover. Researchers use it for analyzing catalytic specificity and mechanistic pathways. Its hydrobromide form enhances aqueous handling.
CAT No: R2199
CAS No:201851-47-0
Synonyms/Alias:201851-47-0;L-Glutamine 7-amido-4-methylcoumarin hydrobromide;(2S)-2-amino-N-(4-methyl-2-oxochromen-7-yl)pentanediamide;hydrobromide;MFCD00237868;H-Gln-AMC hydrobromide;L-Glutamine7-amido-4-methylcoumarinhydrobromide;
L-Glutamine 7-amido-4-methylcoumarin hydrobromide is a specialized biochemical substrate that combines the amino acid L-glutamine with the fluorogenic moiety 7-amido-4-methylcoumarin (AMC) in a hydrobromide salt form. This compound is widely recognized for its utility in enzymology and biochemical assay development, particularly as a sensitive probe for the detection and quantification of enzymatic activity involving glutaminase and related hydrolases. The molecular design enables the release of a fluorescent signal upon enzymatic cleavage, providing researchers with a powerful tool for real-time monitoring of specific enzymatic reactions in complex biological samples. Its robust fluorescence properties, combined with the biological relevance of the glutamine residue, make it a valuable reagent for a variety of investigative and analytical contexts in biochemistry and molecular biology.
Enzyme activity assays: As a fluorogenic substrate, L-Glutamine 7-amido-4-methylcoumarin hydrobromide is extensively employed in the measurement of glutaminase activity. Upon enzymatic hydrolysis, the AMC group is liberated, producing a highly fluorescent compound that can be quantified using standard fluorescence detection methods. This enables sensitive and specific monitoring of glutaminase kinetics in vitro, facilitating the characterization of enzyme inhibitors, activators, or mutant variants. The substrate's selectivity and signal-to-noise ratio are particularly advantageous for high-throughput screening applications in drug discovery and enzymology research.
Biochemical pathway analysis: The compound plays a critical role in dissecting metabolic pathways involving glutamine metabolism. By serving as a reporter substrate, it allows for the investigation of glutaminase function and regulation under various physiological and experimental conditions. Researchers can utilize this substrate to study alterations in glutamine utilization, such as those occurring in cancer cell metabolism or during cellular adaptation to nutrient stress, thereby gaining insight into metabolic flux and regulatory mechanisms at the molecular level.
Cellular and subcellular localization studies: The fluorescent properties of the AMC moiety enable visualization and quantification of enzymatic activity within cellular or subcellular compartments. By applying the substrate to intact cells, tissue lysates, or organelle preparations, scientists can spatially resolve glutaminase activity, supporting studies on enzyme compartmentalization, trafficking, and functional dynamics. This approach underpins research into the localization-dependent regulation of glutamine metabolism and its implications for cellular physiology.
Inhibitor screening and drug discovery: The sensitive fluorescence-based readout provided by this substrate is ideally suited for the identification and characterization of small-molecule modulators of glutaminase and related enzymes. The robust assay format allows for rapid and reproducible evaluation of compound libraries, supporting the development of novel enzyme inhibitors or activators. Such applications are integral to early-stage drug discovery programs targeting metabolic enzymes implicated in disease-relevant pathways.
Analytical method development: L-Glutamine 7-amido-4-methylcoumarin hydrobromide is also utilized in the development and optimization of quantitative analytical methods for enzymatic activity. Its well-characterized fluorescence properties facilitate calibration, validation, and standardization of assay protocols. Laboratories engaged in routine enzyme analytics or in the establishment of reference methods for biochemical quality control frequently rely on this substrate to ensure accuracy, reproducibility, and sensitivity in their measurements.
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