Suc-Ala-Phe-Pro-Phe-pNA
| Name | Suc-Ala-Phe-Pro-Phe-pNA |
| Category | Enzyme Substrates and Inhibitors |
| One Letter Code | Succinylation-AFPF-p-Nitroanilide |
| Three Letter Code | Succinylation-{Ala}{Phe}{Pro}{Phe}-p-Nitroanilide |
| Molecular Weight | 700.750 |
| Application |
| Norville, Isobel H., et al. "The structure of a Burkholderia pseudomallei immunophilin–inhibitor complex reveals new approaches to antimicrobial development." Biochemical Journal 437.3 (2011): 413-422. |
| 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. |
| Kervinen, Jukka, et al. "Potency variation of small-molecule chymase inhibitors across species." Biochemical pharmacology 80.7 (2010): 1033-1041. |
| Aumüller, Tobias, et al. "Role of prolyl cis/trans isomers in cyclophilin-assisted Pseudomonas syringae AvrRpt2 protease activation." Biochemistry 49.5 (2010): 1042-1052. |
| Davis, Tara L., et al. "Structural and biochemical characterization of the human cyclophilin family of peptidyl-prolyl isomerases." PLoS biology 8.7 (2010). |