Suc-Ala-Ala-Pro-Phe-AMC

Description:

The peptidylprolyl isomerase substrate Suc-AAPF-AMC is also hydrolyzed by carboxypeptidase Y, cathepsin G, and chymotrypsin. Suc-AAPF-AMC has also been used to analyze the chymotrypsin-like activity of trypsins.

Sequence:

Succinylation-AAPF-AMC

General

References

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Name	Suc-Ala-Ala-Pro-Phe-AMC
Category	Enzyme Substrates and Inhibitors
One Letter Code	Succinylation-AAPF-AMC
Three Letter Code	Succinylation-{Ala}{Ala}{Pro}{Phe}-AMC
Molecular Weight	661.710
Application	Gastrointestinal Research

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Li, Zhenwei, et al. "Insights on activity and stability of subtilisin E towards guanidinium chloride and sodium dodecylsulfate." Journal of biotechnology 169 (2014): 87-94.

Waern, Ida, et al. "Mast cell chymase modulates IL-33 levels and controls allergic sensitization in dust-mite induced airway inflammation." Mucosal immunology 6.5 (2013): 911-920.

O'Meara, Jeff A., et al. "Molecular mechanism by which a potent hepatitis C virus NS3-NS4A protease inhibitor overcomes emergence of resistance." Journal of Biological Chemistry 288.8 (2013): 5673-5681.

Lapsongphon, Nawaporn, and Jirawat Yongsawatdigul. "Production and purification of antioxidant peptides from a mungbean meal hydrolysate by Virgibacillus sp. SK37 proteinase." Food chemistry 141.2 (2013): 992-999.