Ac-Lys-AMC contains an N-acetylated lysine residue linked to 7-amino-4-methylcoumarin (AMC) through an amide at the carboxamide side, forming a lysine-based peptide substrate mimic with a free ε-amino group masked as part of the linkage to the AMC fluorophore. The molecule bears an N-acetyl group on the α-amino position and an AMC moiety that provides a fluorescence-reporting chromophore, while the remaining functional groups include the lysine-derived amide connectivity and the coumarin amino functionality. Ac-Lys-AMC is used in fluorescence-based substrate and enzyme-assay workflows and analytical method development where monitoring AMC release or fluorescence changes supports studies of proteolytic processing and structure-activity relationships in peptide recognition.
CAT No: CP26426
CAS No:156661-42-6
Synonyms/Alias:Ac-Lys-AMC(Acetatesalt);156661-42-6;CTK8E9583;ZINC2517157;RT-011162
Ac-Lys-AMC is an acetylated lysine-AMC conjugate used as a fluorogenic substrate in enzyme activity assays and mechanistic studies of proteases that recognize lysine-containing sequences. The lysine side chain is linked to the AMC (7-amino-4-methylcoumarin) reporter, so enzymatic cleavage releases a fluorescent moiety suitable for sensitive, real-time readouts in solution-phase formats. This reagent is commonly employed in biochemical screening workflows where consistent substrate structure and a direct fluorescence signal simplify kinetic measurements.
1. Protease Activity Assays
Ac-Lys-AMC is widely used by enzymology and biochemical assay developers to quantify protease activity that can cleave at or near lysine motifs, with fluorescence arising from AMC release after substrate hydrolysis. Researchers use it in microplate-based kinetic assays to compare relative enzyme activity across conditions such as buffer composition, pH, ionic strength, and inhibitor presence, enabling straightforward dose-response or time-course studies. The acetylated lysine context helps standardize substrate presentation so that observed fluorescence changes can be attributed to enzymatic processing rather than variable reporter accessibility.
2. Enzyme Inhibitor Screening
Ac-Lys-AMC supports medicinal chemistry and chemical biology programs that evaluate small-molecule or peptide-like inhibitors targeting lysine-recognizing proteases. In these workflows, the reagent provides a convenient fluorescence endpoint for throughput screening, where inhibitor effects translate into reduced AMC signal over defined incubation windows. Because the readout is directly coupled to cleavage of a defined substrate, it is frequently selected for comparative studies of inhibitor potency and selectivity across panels of protease enzymes under matched assay conditions.
3. Protease Mechanism Studies
Ac-Lys-AMC is used in mechanistic investigations to map how protease activity depends on substrate structure and reaction conditions, including studies of kinetic parameters and cleavage efficiency. Biochemistry groups employ it to examine how changes in experimental variables influence the rate of AMC generation, supporting interpretation of catalytic behavior and substrate recognition patterns. The lysine-AMC architecture also makes it useful for experiments where researchers need a consistent fluorescent reporter to follow cleavage progress without requiring chromatographic separation for every time point.
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