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Chemical Compound Review

Suc-aapf-pna     3-[[(1S)-1-[[(2S)-1-[(2S)-2- [[(1S)-1-[(4...

Synonyms: CHEMBL298712, S7388_SIGMA, CHEBI:175645, AC1NUZ6U, 70967-97-4, ...
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High impact information on Suc-aapf-pna


Biological context of Suc-aapf-pna


Associations of Suc-aapf-pna with other chemical compounds


Gene context of Suc-aapf-pna

  • Based on the chymotrypsin-coupled assay using the tetrapeptide substrate succinyl-Ala-Ala-Pro-Phe-p-nitroanilide, the purified protein has rotamase activity identical to human cyclophilin with a catalytic efficiency close to the upper diffusional limit (kcat/Km approximately 1.0 x 10(7) M-1 x S-1 at 10 degrees C) [10].
  • The proteinase degraded azocoll, type III collagen, type IV procollagen, laminin, fibronectin, and the peptide substrates succinyl-Ala-Ala-Pro-Phe-p-nitroanilide (1,573 M-1 s-1) and t-butyloxy carbonyl-Ala-Ala-Leu-p-nitroanilide (1,614 M-1 s-1) [11].


  1. Yeast NPI46 encodes a novel prolyl cis-trans isomerase that is located in the nucleolus. Shan, X., Xue, Z., Mélèse, T. J. Cell Biol. (1994) [Pubmed]
  2. Neisseria meningitidis encodes an FK506-inhibitable rotamase. Sampson, B.A., Gotschlich, E.C. Proc. Natl. Acad. Sci. U.S.A. (1992) [Pubmed]
  3. The streptococcal lipoprotein rotamase A (SlrA) is a functional peptidyl-prolyl isomerase involved in pneumococcal colonization. Hermans, P.W., Adrian, P.V., Albert, C., Estevão, S., Hoogenboezem, T., Luijendijk, I.H., Kamphausen, T., Hammerschmidt, S. J. Biol. Chem. (2006) [Pubmed]
  4. Clipsin, a chymotrypsin-like protease in rat brain which is irreversibly inhibited by alpha-1-antichymotrypsin. Nelson, R.B., Siman, R. J. Biol. Chem. (1990) [Pubmed]
  5. Crystal structure implies that cyclophilin predominantly catalyzes the trans to cis isomerization. Zhao, Y., Ke, H. Biochemistry (1996) [Pubmed]
  6. NMR analysis of in vitro-synthesized proteins without purification: a high-throughput approach. Guignard, L., Ozawa, K., Pursglove, S.E., Otting, G., Dixon, N.E. FEBS Lett. (2002) [Pubmed]
  7. Directed evolution converts subtilisin E into a functional equivalent of thermitase. Zhao, H., Arnold, F.H. Protein Eng. (1999) [Pubmed]
  8. Probing the importance of hydrogen bonds in the active site of the subtilisin nattokinase by site-directed mutagenesis and molecular dynamics simulation. Zheng, Z.L., Ye, M.Q., Zuo, Z.Y., Liu, Z.G., Tai, K.C., Zou, G.L. Biochem. J. (2006) [Pubmed]
  9. Mechanistic implication of crystal structures of the cyclophilin-dipeptide complexes. Zhao, Y., Ke, H. Biochemistry (1996) [Pubmed]
  10. Peptidyl-prolyl cis-trans-isomerase from Escherichia coli: a periplasmic homolog of cyclophilin that is not inhibited by cyclosporin A. Liu, J., Walsh, C.T. Proc. Natl. Acad. Sci. U.S.A. (1990) [Pubmed]
  11. Purification and characterization of a 27,000-Mr extracellular proteinase from Trichophyton rubrum. Apodaca, G., McKerrow, J.H. Infect. Immun. (1989) [Pubmed]
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