Suc-Ala-Ala-Pro-Lys-pNA

Description:

a substrate for wild-type and K188D/D189K trypsins

Sequence:

Succinylation-AAPK-p-Nitroanilide
  • General
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  • Name Suc-Ala-Ala-Pro-Lys-pNA
    Category Enzyme Substrates and Inhibitors
    One Letter Code Succinylation-AAPK-p-Nitroanilide
    Three Letter Code Succinylation-{Ala}{Ala}{Pro}{Lys}-p-Nitroanilide
    Molecular Weight 605.650
    Application
    Gamble, Michael, et al. "The role of substrate specificity and metal binding in defining the activity and structure of an intracellular subtilisin." FEBS open bio 2 (2012): 209-215.
    Qasim, Mohammad A., et al. "Cleavage of peptide bonds bearing ionizable amino acids at P1 by serine proteases with hydrophobic S1 pocket." Biochemical and biophysical research communications 400.4 (2010): 507-510.
    Halabi, Najeeb, et al. "Protein sectors: evolutionary units of three-dimensional structure." Cell 138.4 (2009): 774-786.
    Mikhailova, A. G., et al. "Psychrophilic trypsin-type protease from Serratia proteamaculans." Biochemistry (Moscow) 71.5 (2006): 563-570.
    Mahrus, Sami, Walter Kisiel, and Charles S. Craik. "Granzyme M is a regulatory protease that inactivates proteinase inhibitor 9, an endogenous inhibitor of granzyme B." Journal of Biological Chemistry 279.52 (2004): 54275-54282.
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