H-Ala-Ala-Phe-pNA

Description:

Substrate for chymotrypsin and tripeptidyl peptidases I and II.

Sequence:

AAF-p-Nitroanilide
  • General
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  • Name H-Ala-Ala-Phe-pNA
    Category Enzyme Substrates and Inhibitors
    One Letter Code AAF-p-Nitroanilide
    Three Letter Code {Ala}{Ala}{Phe}-p-Nitroanilide
    Molecular Weight 427.460
    Application
    Reichard, Utz, et al. "Sedolisins, a new class of secreted proteases from Aspergillus fumigatus with endoprotease or tripeptidyl-peptidase activity at acidic pHs." Appl. Environ. Microbiol. 72.3 (2006): 1739-1748.
    Tomkinson, Birgitta, Bairbre Ní Laoi, and Kimberly Wellington. "The insert within the catalytic domain of tripeptidyl‐peptidase II is important for the formation of the active complex." European journal of biochemistry 269.5 (2002): 1438-1443.
    Hortin, Glen L., and Jay Murthy. "Substrate size selectivity of 20S proteasomes: analysis with variable-sized synthetic substrates." Journal of protein chemistry 21.5 (2002): 333-337.
    Abbott, Catherine A., et al. "Cloning, expression and chromosomal localization of a novel human dipeptidyl peptidase (DPP) IV homolog, DPP8." European Journal of Biochemistry 267.20 (2000): 6140-6150.
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