Bulletin of the Korean Chemical Society

  • 제19권6호
  • /
  • Pages.689-695
  • /
  • 1998
  • /
  • 0253-2964(pISSN)
  • /
  • 1229-5949(eISSN)
대한화학회 (Korean Chemical Society)
권호 표지
DOI QR코드

DOI QR Code

Synthesis of Carbobenzoxy-alanyl-thiaarginine (thialysine) benzyl ester and kinetic Studies with Trypsin

  • 발행 : 1998.06.20
PDF 다운로드
⟨ 이전 논문 다음 논문 ⟩

초록

Carbobenzoxy-alanyl-thiaarginine benzyl ester and carbobenzoxy-alanyl-thialysine benzyl ester were synthesized in solution. Kinetic studies were carried out using three different analytical methods, semi-classical method, progress curve analysis and competitive spectrophotometry. In competitive spectrophotometry, carbobenzoxy-valyl-glycyl-arginyl-p-nitroaniline was used as a detector. Kinetic constants such as $K_m$ and $V_{max}$ measured by competitive spectrophotometry are almost the same as those values measured by semi-classical method. Colorimetric Ellman's assays showed the thio-peptido mimetics to be a suitable substrates for trypsin. Kinetic studies with trypsin gave $K_m$ of 2.33 mM and $k_{cat}$ of $1.50{\times}10^5\;min^{-1}$ for carboxy-alanyl-thiaarginine benzyl ester and $K_m$ of $3.41{\times}10^{-3}\; Mm\; and\; k_{cat}\; of\; 520{\times}102\; min^{-1}$ for carbobenzoxy-alanyl-thialysine benzyl ester, respectively. Kinetic constants $(K_m=2.04{\times}10^{-2}\; mM, K_{cat}=4.42{\times}10^3 \;min^{-1})$ for natural substrate, carbobenzoxy-alanyl-lysine benzyl ester, were also evaluated by competitive spectrophotometry in order to compare the mode of binding on trypsin.

키워드

참고문헌

  1. Bull. Korean Chem. Soc. v.19 no.2 Hong, N. J.;Park, Y. A.;Son, K. N.
  2. J. of Resource Development v.16 no.1 Hong, N. J.;Park, Y. A.;
  3. Peptides of Chinese Peptide Symposium v.14 no.1 Hong, N. J.;Choi, C.
  4. J. Med. Chem. v.32 Hwang, S.;Berges, S.;Taggart, J.;Gilverg. C.
  5. Proc. Nat. Aca. Sci. v.81 Kingsburry, W.;Boehm, J.;Givarg, C.
  6. Anal. Biochem. v.154 Hwang, S. Y.;Kingsburry, W. D.;Hall, N. M.;Jakes, D. R.;Dunn, G.;Gilvarg, C.
  7. Anal. Biochem. v.161 Brown, K.;Kingsurry, W.;Hall, N.;Dunn, G.;Gilvarg, C.
  8. J. Bact. v.160 Perry, D.;Gilvarg, C.
  9. J. Med. Chem. v.29 Kingsburry, W.;Boehn, J.;Newman, D.
  10. Bull. Korean Chem. Soc. v.14 no.6 Hong, N. J.;Park, Y. T.
  11. J. Med. Chem. v.23 Stenfeld, A.;Naider, F.;Becker, J.
  12. Biochem v.28 Duncan, K.;Faraci, W.;Walsh, C.
  13. J. Gen. Microbial v.94 Kenig, M.;Bandamme, E.;Abraham, E.
  14. FEMS Microbial Lett. v.37 Shallow, D. A.;Barrett, K. J.;Payne, W.
  15. Int. J. Peptide Protein Res. v.37 Reux, P. L.;Blant, D.;Lecreux, D. M.;Heigenhort, J. V.
  16. Arch. Biochem. Biophy. v.82 Ellman, G. L.
  17. Arch. Biochem. Biophy. v.74 Ellman, G. L.
  18. J. Fed. Eur. Biochem. Soc v.247 Orskov, C.;Buhl, T.;Rabenhoj, L.;Kofod, H.;Holst, J.
  19. J. Biol. Chem. v.246 Kemmlar, W.;Peterson, J. D.;Steiner, D. F.
  20. In Mehods in Enzymology v.11 Ambler, R. P.;Jacoby, C.(ed.)
  21. Proc. Nat. Acad. Sci. v.62 Clark, J. L.;Steiner, D. F.
  22. J. Neurochem v.53 Smith, D. G.;Mauthainar, K.;Darby, N. J.;Fricker, L. D.
  23. Proc. Natl. Acad. Sci. U. S. A. v.81 Hook, V. Y.;Loh, Y. P.
  24. Biochem. J. v.245 Davidson, H. W.;Hutton, J. C.
  25. In the Enzymes v.3 Folk, J. E.;Boyer, P. D.(ed.)
  26. J. Biol. Chem. v.258 Simmon, C. M.;Chan, S. J.;Donald, F.
  27. In Method in Enzymology v.ⅩⅨ Walsh, K. A.;Perlmann, G.(ed.);Lorand, L.(ed.)
  28. Anal. Biochem. v.170 Hwang, S.;Brown, K. S.;Gilvarg, C.
  29. J. Amer. Chem. Soc. v.79 Doherty, D.;Shapira, R.;Burnett, W.
  30. Biochem. Soc. Trans. v.11 Wharten, C.
  31. In The Chemical Kinetics of Enzyme Action Laidler, K. J.;Bunting, P. S.;Laidler, K. J.(ed.)
  32. In Methods in Enzymology v.63 Orsi, B. A.;Tipton, K. F.;Jacody, C.(ed.)
  33. Biochem. J. v.203 Wharton, C. W.;Szawelski, R. J.
  34. J. of Molecular Biology v.46 Steitz, T. A.;Henderson, R.;Blow, D. M.
  35. Structure-Function Relationships of Proteolytic Enzymes Desnuelle, P.;Neurath, H.;Ottesen, M.
  36. J. Phys. Chem. v.68 Bondi, A.
  37. Enzymes Haldane, J. B.
  38. Biochem. Biophys, Res. Com. v.27 Schechter, I.;Berg, A.
  39. Ann. Rev. Biochem. v.46 Kraut, J.