Suc-Ala-Glu-Pro-Phe-pNA

Description:

chromogenic substrate for the peptidylprolyl isomerase Pin1.

Sequence:

Succinylation-AEPF-p-Nitroanilide

General

References

Comments (0)

Name	Suc-Ala-Glu-Pro-Phe-pNA
Category	Enzyme Substrates and Inhibitors
One Letter Code	Succinylation-AEPF-p-Nitroanilide
Three Letter Code	Succinylation-{Ala}{Glu}{Pro}{Phe}-p-Nitroanilide
Molecular Weight	682.690
Application

Duncan, Kelly E., et al. "Discovery and characterization of a nonphosphorylated cyclic peptide inhibitor of the peptidylprolyl isomerase, Pin1." (2011).

Erben, Esteban D., et al. "Identification of an atypical peptidyl-prolyl cis/trans isomerase from trypanosomatids." Biochimica et Biophysica Acta (BBA)-Molecular Cell Research 1803.9 (2010): 1028-1037.

Ohashi, Tsubasa, et al. "Preparation of Protein Transduction Domain-Fused Peptidyl Prolyl cis/trans Isomerase Pin1." Bioscience, biotechnology, and biochemistry 74.10 (2010): 2067-2070.

Zoldak, Gabriel, et al. "A library of fluorescent peptides for exploring the substrate specificities of prolyl isomerases." Biochemistry 48.43 (2009): 10423-10436.

Heikkinen, Outi, et al. "Solution structure of the parvulin-type PPIase domain of Staphylococcus aureus PrsA–implications for the catalytic mechanism of parvulins." BMC structural biology 9.1 (2009): 17.