Probing the substrate specificity for lipases. II. Kinetic and modeling studies on the molecular recognition of 2-arylpropionic esters by Candida rugosa and Rhizomucor miehei lipases

Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology

Volumn 1337, Issue 2, 1997, Pages 302-310

  Botta, Maurizio ^a   Cernia, Enrico ^b   Corelli, Federico ^a   Manetti, Fabrizio ^a   Soro, Simonetta ^b  

^a UNIVERSITY OF SIENA   (Italy)

^b SAPIENZA UNIVERSITY OF ROME   (Italy)

Author keywords

(C. rugosa); (Rh. miehei); 2 Arylpropionic ester; Lipase; Molecular modeling; Non steroidal antiinflammatory drug precursor; Substrate specificity

Indexed keywords

ANTIINFLAMMATORY AGENT; ARYLPROPIONIC ACID DERIVATIVE; FENOPROFEN; KETOPROFEN; NAPROXEN; TRIACYLGLYCEROL LIPASE;

ARTICLE; CANDIDA; COMPUTER SIMULATION; CONFORMATIONAL TRANSITION; ENANTIOMER; ENZYME ACTIVITY; ENZYME KINETICS; ENZYME SPECIFICITY; IN VITRO STUDY; MOLECULAR MODEL; MOLECULAR RECOGNITION; PRIORITY JOURNAL; STEREOCHEMISTRY;

BINDING SITES; CANDIDA; CRYSTALLOGRAPHY, X-RAY; KINETICS; LIPASE; MODELS, MOLECULAR; MOLECULAR STRUCTURE; MUCORALES; PROPIONIC ACIDS; PROTEIN CONFORMATION; SUBSTRATE SPECIFICITY;

CANDIDA; CANDIDA RUGOSA; RHIZOMUCOR MIEHEI;

EID: 0031016559     PISSN: 01674838     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0167-4838(96)00181-1     Document Type: Article

References (38)

1. Wong, C.-H. and Whitesides, G.M. (1994) Enzymes in Synthetic Organic Chemistry, Elsevier, Oxford.
2. Schneider, M.P (1986) Enzymes as Catalysts in Organic Synthesis, Reidel, Dordrecht, The Netherlands.
3. Toone, E.J., Werth, M.J. and Jones, J.B. (1990) J. Am. Chem. Soc. 112, 4946-4952 (and references cited therein).
4. Norin, M., Hult, K., Mattson, A. and Norin, T. (1993) Biocatalysis 7, 131-147.
5. Scott, D.L., White, S.P., Otwinowski, Z., Yuan, W., Gelb, M.H. and Sigler, P.B. (1990) Science 250, 1541-1546.
6. Hultin, P.G. and Jones, J.B. (1992) Tetrahedron Lett. 33, 1399-1402.
7. Guanti, G., Banfi, L. and Narisano, E. (1992) J. Org. Chem. 57, 1540-1554.
8. Wimmer, Z. (1992) Tetrahedron 48, 8431-8436.
9. Kim, M.J. and Cho, H. (1992) J. Chem. Soc., Chem. Commun. 1411-1413.
10. Ader, U., Andersch, P., Berger, M., Goergens, U., Seemayer, R. and Schneider, M.P. (1992) Pure Appl. Chem. 64, 1165-1170.
11. Burgess, K. and Jennings, L.D. (1991) J. Am. Chem. Soc. 113, 6129-6139.
12. Johnson, C.R., Golebiowski, A., McGill, T.K. and Steensma, D.H. (1991) Tetrahedron Lett. 32, 2597-2600.
13. Kazlauskas, R.L., Weissfloch, A.N.E., Rappaport, A.T. and Cuccia, L.A. (1991) J. Org. Chem. 56, 2656-2665.
14. Oberhauser, T., Faber, K. and Griengl, H. (1989) Tetrahedron 45, 1679-1682.
15. Roberts, S.M. (1989) Phil. Trans. R. Soc. London B 324, 557-587.
16. Umemura, T. and Hirohara, H. (1989) in Biocatalysis in Agricultural Biotechnology (Whitaker, J.R. and Sonnet, P.E., eds.), Chap. 26, American Chemical Society, Washington, DC.
17. Derewenda, Z.S., Derewenda, U. and Dodson, G.G. (1992) J. Mol. Biol. 227, 818-839.
18. Derewenda, U., Brzozowski, A.M., Lawson, D.M. and Derewenda, Z.S. (1992) Biochemistry 31, 1532-1541.
19. Blow, D. (1991) Nature (London) 351, 444-445.
20. Brzozowski, A.M., Derewenda, U., Derewenda, Z.S., Dodson, G.G., Lawson, D.M., Turkenburg, J.P., Bjorkling, F., Huge-Jensen, B., Patkar, S.A. and Thim, L. (1991) Nature (London) 351, 491-494.
21. Brady, L., Brzozowski, A.M., Derewenda, Z.S., Dodson, E., Dodson, G.G., Tolley, S., Turkenburg, J.P., Christiansen, L., Huge-Jensen, B., Norskov, L., Thim, L. and Menge, U. (1990) Nature (London) 343, 767-770.
22. Grochulski, P., Li, Y., Schrag, J.D., Bouthillier, F., Smith, P., Harrison, D., Rubin, B. and Cygler, M. (1993) J. Biol. Chem. 268, 12843-12847.
23. Van Tilbeurgh, H., Sarda, L., Verger, R. and Cambillau, C. (1992) Nature (London) 359, 159-162.
24. Winkler, F.K., D'Arcy, A. and Hunziker, W. (1990) Nature (London) 343, 771-774.
25. Thunnissen, M.M.G.M., Ab, E., Kalk, K.H., Drenth, J., Dijkstra, B.W., Kuipers, O.P., Dijkman, R., De Haas, G.H. and Verheij, H.M. (1990) Nature (London) 347, 689-691 (and references cited therein).
26. Botta, M., Cernia, E., Corelli, F., Manetti, F. and Soro, S. (1996) Biochim. Biophys. Acta 1296, 121-126.
27. Lombardino, J.G. (1985) Nonsteroidal Antiinflammatory Drugs, Chap. 4, pp. 253-431, Wiley, New York.
28. Brook, M.A. and Chan, T.H. (1983) Synthesis 201-203.
29. Sinibaldi, M., Flieger, M., Cvak, L., Messina, A. and Pichini, A. (1994) J. Chromatogr. 666, 471-478.
30. Gu, Q.-M., Chen, C.-S. and Sih, C.J. (1986) Tetrahedron Lett. 27, 1763-1766.
31. Still, W.C. (1993) Programs MacroModel (version 4.0) and BatchMin (version 4.0), Department of Chemistry, Columbia University, New York, NY.
32. SYBYL version 6.1 (1994) Tripos Associates, St. Louis, MO.
33. Chen, C.S., Fujimoto, Y., Girdaukas, G. and Sih, C.J. (1982) J. Am. Chem. Soc. 104, 7294-7299.
34. Grochulski, P., Li, Y., Schrag, J.D. and Cygler, M. (1994) Protein Sci. 3, 82-91.
35. Schrag, J.D., Li, Y., Wu, S. and Cygler, M. (1991) Nature (London) 351, 761-764.
36. Podlogar, B.L., Farr, R.A., Friedrich, D., Tarnus, C., Huber, E.W., Cregge, R.J. and Schirlin, D. (1994) J. Med. Chem. 37, 3684-3692.
37. Colton, I.J., Ahmed, S.N. and Kazlauskas, R.J. (1995) J. Org. Chem. 60, 212-217.
38. Wu, S.-H., Guo, Z.-W. and Sih, C.J. (1990) J. Am. Chem. Soc. 112, 1990-1995.