Z-Ala-ala-asn-amc couples a protected tripeptide motif with a fluorogenic marker to characterize enzymatic cleavage. The residue combination supports controlled hydrogen bonding and substrate recognition. Researchers track fluorescence changes to analyze catalytic behavior. Uses include protease profiling, assay development, and mechanistic evaluation.
CAT No: R2344
CAS No:149697-16-5
Synonyms/Alias:Z-ALA-ALA-ASN-AMC;149697-16-5;benzyl N-[(2S)-1-[[(2S)-1-[[(2S)-4-amino-1-[(4-methyl-2-oxochromen-7-yl)amino]-1,4-dioxobutan-2-yl]amino]-1-oxopropan-2-yl]amino]-1-oxopropan-2-yl]carbamate;Z-Ala-Ala-Asn-MCA;MFCD02684274;starbld0000904;Cbz-Ala-Ala-Asn-AMC;SCHEMBL17205800;AKOS040756863;DA-68800;FA110589;MS-30244;HY-136626;CS-0132606;G13153;benzyloxycarbonyl-Ala-Ala-Asn-4-methyl-7-coumarylamide;
Z-Ala-ala-asn-amc is a synthetic fluorogenic peptide substrate widely utilized in biochemical research for its ability to facilitate sensitive detection and quantification of enzymatic activity. Composed of a protected tripeptide sequence (Z-Ala-Ala-Asn) conjugated to 7-amino-4-methylcoumarin (AMC), this compound enables real-time monitoring of proteolytic cleavage events. The presence of the AMC moiety allows for the generation of a highly fluorescent signal upon enzymatic hydrolysis, making it an invaluable tool in various investigative and analytical contexts. Its chemical stability, solubility in aqueous and organic solvents, and compatibility with standard fluorescence detection platforms enhance its versatility for laboratory applications. Researchers value this substrate for its specificity and efficiency in studying protease function, substrate specificity, and enzyme kinetics, contributing to advancements in enzymology and peptide chemistry.
Protease Activity Assays: Z-Ala-ala-asn-amc is extensively employed in the assessment of protease activity in vitro. By serving as a substrate for specific proteases, its cleavage releases AMC, which emits a strong fluorescence signal detectable by spectrophotometric or fluorometric methods. This property enables precise quantification of enzymatic rates, facilitating kinetic studies and inhibitor screening. Its use in high-throughput assays accelerates the identification of enzyme modulators, supporting drug discovery and basic research into proteolytic mechanisms.
Enzyme Specificity Profiling: The substrate's defined peptide sequence allows researchers to investigate the substrate preferences of various proteases. By comparing the hydrolysis rates of Z-Ala-ala-asn-amc with those of structurally related substrates, scientists can elucidate the structural determinants that govern enzyme-substrate recognition. This application is crucial for mapping the substrate specificity of newly discovered or engineered proteases, advancing the understanding of enzyme function at a molecular level.
Biochemical Pathway Elucidation: Utilization of this fluorogenic peptide in cell-free extracts or purified enzyme systems aids in dissecting complex proteolytic pathways. By monitoring AMC release, researchers can track the activity of target proteases within multi-enzyme cascades, helping to clarify their roles in physiological and pathological processes. This approach provides insights into regulatory networks and protein turnover, informing the development of targeted biochemical interventions.
High-Throughput Screening: Z-Ala-ala-asn-amc is ideally suited for high-throughput screening formats due to its robust fluorescent readout and compatibility with microplate-based platforms. Laboratories leverage this feature to rapidly evaluate large libraries of chemical compounds for their ability to modulate protease activity. The substrate's sensitivity and reproducibility streamline the identification of potential enzyme inhibitors or activators, expediting the early phases of pharmaceutical and chemical biology research.
Quality Control in Enzyme Production: In industrial and academic settings, the substrate serves as a quality control reagent for the production and purification of proteases. By providing a rapid and quantitative measure of enzyme activity, it ensures consistency and reliability in enzyme preparations used for research or biotechnological applications. Its application in standardizing activity assays supports reproducibility and comparability across batches and laboratories.
Peptidase Mechanism Studies: The use of Z-Ala-ala-asn-amc extends to mechanistic investigations of peptidase catalysis, where it helps delineate the stepwise processes involved in peptide bond hydrolysis. Researchers employ this substrate to probe the effects of mutations, cofactors, or environmental conditions on enzyme action, yielding detailed mechanistic insights. These studies are fundamental for rational enzyme engineering, the development of novel biocatalysts, and the broader field of protein chemistry. Collectively, these applications underscore the central role of Z-Ala-ala-asn-amc in advancing protease research, enzymology, and related scientific disciplines.
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