Suc-Ala-Ala-Pro-Lys-pNA is a chromogenic substrate containing a lysine-p-nitroanilide reporter that enables measurement of trypsin-like protease activity. The succinyl cap regulates charge and substrate orientation. Researchers quantify p-nitroaniline release to determine catalytic constants. Applications include enzyme-screening assays, mechanistic studies, and protease-specificity analysis.
CAT No: R2375
CAS No:108929-39-1
Synonyms/Alias:Suc-Ala-Ala-Pro-Lys-pNA;108929-39-1;Suc-AAPK-pNA;4-[[(2S)-1-[[(2S)-1-[(2S)-2-[[(2S)-6-amino-1-(4-nitroanilino)-1-oxohexan-2-yl]carbamoyl]pyrrolidin-1-yl]-1-oxopropan-2-yl]amino]-1-oxopropan-2-yl]amino]-4-oxobutanoic acid;MFCD00238358;HY-P4484;4-((S)-1-((S)-1-((S)-2-((S)-6-amino-1-(4-nitrophenylamino)-1-oxohexan-2-ylcarbamoyl)pyrrolidin-1-yl)-1-oxopropan-2-ylamino)-1-oxopropan-2-ylamino)-4-oxobutanoic acid;DA-58147;FS110776;CS-0654443;
Suc-Ala-Ala-Pro-Lys-pNA is a synthetic peptide substrate widely utilized in enzymology and biochemical research, characterized by its sequence of alanine, proline, and lysine residues capped with a succinyl group at the N-terminus and a para-nitroanilide (pNA) chromogenic group at the C-terminus. As a chromogenic peptide, it is specifically designed to serve as a substrate for serine proteases, particularly those with trypsin-like specificity. The release of the pNA moiety upon enzymatic cleavage enables precise spectrophotometric quantification of protease activity, making this compound an important analytical tool for investigating enzyme kinetics, substrate specificity, and inhibitor screening in both academic and industrial laboratories.
Enzyme Activity Assays: Suc-Ala-Ala-Pro-Lys-pNA is extensively employed in the quantitative measurement of serine protease activity, especially for enzymes such as trypsin, kallikrein, and related proteases that recognize lysine at the P1 position. The peptide's chromogenic pNA group is liberated upon enzymatic hydrolysis, producing a yellow color that can be monitored at 405 nm. This property allows researchers to perform continuous or endpoint assays to determine enzyme activity, monitor reaction rates, and compare the catalytic efficiency of different protease preparations under various experimental conditions.
Substrate Specificity Studies: The defined sequence of Suc-Ala-Ala-Pro-Lys-pNA enables detailed analysis of protease substrate preferences and cleavage site selectivity. By utilizing this substrate in comparative assays, researchers can dissect the influence of amino acid residues surrounding the scissile bond on enzyme recognition and catalysis. Such studies are valuable for elucidating the molecular determinants of substrate specificity, guiding the design of new protease substrates, and informing the development of selective enzyme inhibitors.
Inhibitor Screening: The chromogenic nature of Suc-Ala-Ala-Pro-Lys-pNA makes it an ideal substrate for high-throughput screening of protease inhibitors. By measuring the inhibition of pNA release in the presence of candidate compounds, scientists can rapidly evaluate inhibitor potency and selectivity. This application is particularly relevant in pharmaceutical and biotechnology research, where the identification of novel protease inhibitors is essential for drug discovery and the development of biochemical probes.
Kinetic Characterization: The substrate's well-defined chemical structure and reliable chromogenic response support detailed kinetic studies of serine proteases. Researchers can use Suc-Ala-Ala-Pro-Lys-pNA to determine key enzymatic parameters such as Km, Vmax, and kcat, providing quantitative insights into enzyme mechanisms and catalytic efficiency. Such kinetic analyses are fundamental for comparing enzyme variants, assessing the effects of mutations, and optimizing assay conditions in both basic and applied research settings.
Quality Control in Protease Production: In industrial and bioprocessing environments, Suc-Ala-Ala-Pro-Lys-pNA serves as a standard substrate for quality control and activity testing of protease preparations. Its consistent performance in chromogenic assays allows manufacturers and quality assurance teams to verify batch-to-batch consistency, monitor enzyme stability during storage, and ensure that protease products meet required specifications for downstream applications. This role supports reliable biomanufacturing processes and the development of high-quality enzyme reagents for research and industrial use.
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