Suc-Phe-Ala-Ala-Phe-pNA, also known as Succinyl-Phenylalanine-Alanine-Alanine-Phenylalanine-p-nitroanilide, is a synthetic peptide substrate commonly used in biochemical research, particularly in studies involving proteolytic enzymes. This compound features a succinyl group at one end, which enhances its solubility and stability, and a p-nitroanilide moiety that serves as a chromogenic indicator for enzyme activity. The peptide sequence includes phenylalanine and alanine residues, which are important for substrate specificity and interaction with various proteases. Upon cleavage by specific enzymes, the release of p-nitroaniline can be quantitatively measured, providing insights into enzyme kinetics and activity. The compound is typically utilized in assays to evaluate the performance of proteases, making it valuable in both research and clinical settings. Its characteristics, such as solubility, stability, and reactivity, are crucial for its application in enzyme assays, contributing to its role as a tool in understanding proteolytic processes.

Suc-Phe-Ala-Ala-Phe-pNA

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This enzyme substrate was used to test the concept of substrate-assisted catalysis with an engineered bacterial serine endopeptidase, subtilisin. Suc-FAAF-pNA has been employed for assaying subtilisins from psychrophilic bacteria and myroilysin, a metalloproteinase from the deep sea bacterium Myroides profundi.

Suc-Phe-Ala-Ala-Phe-pNA is a serine protease with natriuretic properties. It has been shown to have high salt and pH optima and to be reactive at physiological pH. Suc-Phe-Ala-Ala-Phe-pNA has been sequenced and found to have a carboxy terminal reactive site. There are eight cysteine residues in the amino acid sequence of this protease, four of which are in the reactive site. This protease also has vasoactive intestinal peptide (VIP) activity, which is involved in inflammatory diseases.

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CAS 110906-89-3: Suc-Phe-Ala-Ala-Phe-pNA

Suc-Phe-Ala-Ala-Phe-pNA

Ref: 01-4013859

Suc-Phe-Ala-Ala-Phe-pNA

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Suc-Phe-Ala-Ala-Phe-pNA

Ref: 3D-SUB-3007-PI