H-Ala-Pro-pNA

Description:

Substrate for the assay of dipeptidyl aminopeptidase IV (DPP IV).

Sequence:

AP-p-Nitroanilide

General

References

Comments (0)

Name	H-Ala-Pro-pNA
Category	Enzyme Substrates and Inhibitors
One Letter Code	AP-p-Nitroanilide
Three Letter Code	{Ala}{Pro}-p-Nitroanilide
Molecular Weight	306.320
Application

Merz, Michael, et al. "Flavourzyme, an enzyme preparation with industrial relevance: automated nine-step purification and partial characterization of eight enzymes." Journal of agricultural and food chemistry 63.23 (2015): 5682-5693.

Wang, J., et al. "Prolylcarboxypeptidase independently activates plasma prekallikrein (fletcher factor)." Current molecular medicine 14.9 (2014): 1173-1185.

Juárez-Montiel, Margarita, et al. "Molecular cloning and heterologous expression in Pichia pastoris of X-prolyl-dipeptidyl aminopeptidase from basidiomycete Ustilago maydis." Applied biochemistry and biotechnology 172.5 (2014): 2530-2539.

Hatanaka, Tadashi, Kayoko Kawakami, and Misugi Uraji. "Inhibitory effect of collagen-derived tripeptides on dipeptidylpeptidase-IV activity." Journal of enzyme inhibition and medicinal chemistry 29.6 (2014): 823-828.

Wilson, Claire H., et al. "Identifying natural substrates for dipeptidyl peptidases 8 and 9 using terminal amine isotopic labeling of substrates (TAILS) reveals in vivo roles in cellular homeostasis and energy metabolism." Journal of Biological Chemistry 288.20 (2013): 13936-13949.

Stressler, Timo, et al. "Characterization of the recombinant exopeptidases PepX and PepN from Lactobacillus helveticus ATCC 12046 important for food protein hydrolysis." PloS one 8.7 (2013).