Molecular modeling of the enantioselectivity in lipase-catalyzed transesterification reactions

Biophysical Journal

Volumn 74, Issue 3, 1998, Pages 1251-1262

  Hæffner, Fredrik ^a   Norin, Torbjörn ^a   Hult, Karl ^a  

^a ROYAL INSTITUTE OF TECHNOLOGY   (Sweden)

Author keywords

[No Author keywords available]

Indexed keywords

TRIACYLGLYCEROL LIPASE;

ARTICLE; CANDIDA; CHIRALITY; ENANTIOMER; ENZYME MECHANISM; ENZYME SUBSTRATE COMPLEX; ESTERIFICATION; MOLECULAR DYNAMICS; MOLECULAR MODEL; NONHUMAN;

EID: 0031887073     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(98)77839-7     Document Type: Article

References (41)

1. Ahmed, S. N., R. J. Kazlauskas, A. H. Morinville, P. Grochulski, J. D. Schrag, and M. Cygler. 1994. Enantioselectivity of Candida rugosa lipase toward carboxylic acids: a predictive rule from substrate mapping and x-ray crystallography. Bioacatalysis. 9:209-225.
2. Åqvist, J., and A. Warshel. 1993. Chem. Rev. 93:2523.
3. Bemis, G. W., G. Carlson-Golab, and J. A. Katzenellenbogen. 1992. A molecular dynamics study of the stability of chymotrypsin acyl enzymes. J. Am. Chem. Soc. 114:570-578.
4. Bernstein, F. C., T. F. Koetzle, G. J. B. Williams, E. F. J. Meyer, M. D. Brice, J. R. Rodgers, O. Kennard, T. Shimanouchi, and M. Tasumi. 1977. The protein data bank: a computer-based archival file for macromolecular structures. J. Mol. Biol. 112:535-542.
5. Black, D. R., C. G. Parker, S. S. Zimmerman, and M. L. Lee. 1996. Enantioselective binding of α-pinene and of some cyclohexanetriol derivatives by cyclodextrin hosts: a molecular modeling study. J. Comp. Chem. 17:931-939.
6. Brady, L., A. M. Brzozowski, Z. S. Derewenda, E. Dodson, G. G. Dodson, S. Tolley, J. P. Turkenburg, L. Christiansen, B. Huge-Jensen, L. Norskov, L. Thim, and U. Menge. 1990. A serine protease forms the catalytic center of a triacylglycerol lipase. Nature. 346:767-770.
7. Breneman, C. M., and K. B. Wiberg. 1990. J. Comp. Chem. 11:361.
8. Brooks, C. R., R. E. Bruccoleri, B. D. Olafson, D. J. States, S. Swaminathan, and M. Karplus. 1983. CHARMM: a program for macromolecular energy, minimization, and dynamics calculations. J. Comput. Chem. 4:187-217.
9. Burkert, U., and N. L. Allinger. ACS Monograph 177, ACS: Washington, DC, 1982.
10. DeTar, D. F. 1981. Computation of enzyme-substrate specificity. Biochemistry. 20:1730-1743.
11. Ewig, C. S., and J. R. Van Wazer. 1986. Ab initio studies of molecular structures and energetics. 1. Base-catalyzed hydrolysis of simple formates and structurally related reactions. J. Am. Chem. Soc. 108: 4774-4783.
12. Faber, K., H. Griengl, H. Hönig, and J. Zuegg. 1994. On the prediction of the enantioselectivity of Candida rugosa lipase by comparative molecular field analysis. Biocatalysis. 9:227-239.
13. Fischer, E. 1894. Ber. Dt. Chem. Ges. 27:2985.
14. Frisch, M. J., G. W. Trucks, H. B. Schlegel, P. M. W. Gill, B. G. Johnson, J. R. Cheeseman, T. A. Keith, J. A. Petersson, K. Montgomery, K. Raghavachari, M. A. Al-Laham, J. V. Zakrzewski, J. V. Ortis, J. B. Foresman, J. Cioslowski, B. Stefanov, A. Nanayakkara, M. Challacombe, C. Y. Peng, A. P. Y., W. Chen, M. W. Wong, J. L. Andres, E. S. Replogle, R. Gomperts, R. L. Martin, D. J. Fox, J. S. Binkley, D. J. Defrees, J. Baker, J. J. P. Stewart, M. Head-Gordon, C. Gonzalez, and J. A. Pople. 1995. In Gaussian 94, Gaussian Inc., Pittsburgh PA.
15. Grochulski, P., F. Bouthillier, R. J. Kazlauskas, A. N. Serreqi, J. D. Schrag, E. Ziomek, and M. Cygler. 1994. Analogs of reaction intermediates identify a unique substrate binding site in Candida rugosa lipase. Biochemistry. 33:3494-3500.
16. Grochulski, P., Y. Li, J. D. Schrag, F. Bouthillier, P. Smith, D. Harrison, B. Rubin, and M. Cygler. 1993. Insights into interfacial activation from an open structure of Candida rugosa lipase. J. Biol. Chem. 268: 12843-12847.
17. Haldane, J. B. S. 1965. Enzymes. Longmans, Green, and Co., M.I.T. Press, Cambridge. 1930.
18. Hermoso, J., D. Pignol, B. Kerfelec, I. Crenon, C. Chapus, and J. C. Fontecilla-Camps. 1996. Lipase activation by nonionic detergents. The crystal structure of porcine lipase-colipase-tetraethylene glycol monooctyl ether complex. J. Biol. Chem. 271:18007-18016.
19. Holmquist, M., F. Hæffner, T. Norin, and K. Hult. 1996. A structural basis for enantioselective inhibition of Candida rugosa lipase by long-chain aliphatic alcohols. Protein Sci. 5:83-88.
20. Karplus, M., and G. A. Petsko. 1990. Molecular dynamics simulations in biology. Nature. 347:631-639.
21. Kazlauskas, R. J. 1994. Elucidating structure-mechanism relationships in lipases: prospects for predicting and engineering catalytic properties. TIBTECH Nov. 12:
22. Kraut, J. 1977. Serine protease: structure and mechanism of catalysis. Annu. Rev. Biochem. 46:331-358.
23. Lang, D., B. Hofmann, L. Haalck, H. J. Hecht, F. Spener, R. D. Schmid, and D. Schoburg. 1996. Crystal structure of a bacterial lipase from Chromobacterium viscosum ATCC 6918 refined at 1.6 Å resolution. J. Mol. Biol. 259:704-717.
24. Lee, T., R. Sakowicz, V. Martichonok, J. K. Hogan, M. Gold, and J. B. Jones. 1996. Probing enzyme specificity. Acta Chem. Scand. 50: 697-706.
25. Martinez, C., P. De Geus, M. Lauwereys, G. Matthyssens, and C. Cambillau. 1992. Fusarium solani cutinase is a lipolytic enzyme with a catalytic serine accessible to the solvent. Nature. 356:615-618.
26. Martinez, C., P. De Geus, P. Stanssens, M. Lauwereys, and C. Cambillau. 1993. Engineering cysteine mutants to obtain crystallography phases with a cutinase from Fusarium solani pisi. Protein Eng. 6:157-165.
27. Nicolas, A., M. Egmond, C. T. Verrips, S. Longhi, C. Cambillau, and C. Martinez. 1996. Contribution of cutinase serine 42 side chain to the stabilization of the oxyanion transition state. Biochemistry. 35: 398-410.
28. Norin, M., F. Hæffner, A. Achour, T. Norin, and K. Hult. 1994. Computer modeling of substrate binding to lipases from Rhizomucor miehei, Humicola lanuginosa, and Candida rugosa. Protein Sci. 3:1493-1503.
29. Norin, M., K. Hult, A. Mattson, and T. Norin. 1993. Molecular modelling of chymotrypsin-substrate interactions: calculation of enantioselectivity. Biocatalysis. 7:131-147.
30. Öhrner, N., C. Orrenius, A. Mattson, E. Dahlén, T. Norin, and K. Hult. 1996. Kinetic resolution of amine and thiol analogues of secondary alcohols catalyzed by the Candida antarctica lipase B. Enzyme. Microb. Technol. 19:328-331.
31. Orrenius, C., F. Hæffner, D. Rotticci, N. Öhrner, T. Norin, and K. Hult. 1998. Chiral recognition of sec-alcohol enantiomers in acyl transfer reactions catalyzed by Candida antarctica lipase B. Biocatalysis and Biotransformation. In press.
32. Ryckaert, J.-P., G. Ciccotti, and H. J. C. Berendsen. 1977. Numerical integration of the cartesian equations of motion of a system with constraints: molecular dynamics of n-alkanes. J. Comp. Phys. 23: 327-341.
33. Schrag, J. D., and M. Cygler. 1993. 1.8 Å refined structure of the lipase from Geotrichum candidum. J. Mol. Biol. 230:575-591.
34. Schrag, J. D., Y. Li, S. Wu, and M. Cygler. 1991. Ser-His-Glu triad forms the catalytic site of the lipase from Geotrichum candidum. Nature. 351:761-764.
35. Stites, W. E., and J. Pranata. 1995. Empirical evaluation of the influence of side chains on the conformational entropy of the polypeptide backbone. Proteins Struct. Funct. Genet. 22:132-140.
36. Uppenberg, J., M. T. Hansen, S. Patkar, and T. A. Jones. 1994. The sequence, crystal structure determination and refinement of two crystal forms of lipase B from Candida antarctica. Structure. 2:293.
37. Uppenberg, J., N. Öhrner, M. Norin, K. Hult, G. J. Kleywegt, S. Patkar, V. Waagen, T. Anthonsen, and T. A. Jones. 1995. Crystallography and molecular modeling studies of lipase B from Candida antarctica reveal a stereospecificity pocket for secondary alcohols. Biochemistry. 34: 16838-16851.
38. van Tilbeurgh, H., M. P. Egloff, C. Martinez, N. Rugani, R. Verger, and C. Cambillau. 1993. Interfacial activation of the lipase-procolipase complex by mixed micelles revealed by X-ray crystallography. Nature. 362:814-820.
39. van Tilbeurgh, H., L. Sarda, R. Verger, and C. Cambillau. 1992. Structure of the pancreatic lipase-procolipase complex. Nature. 359:159-162.
40. Warshel, A., G. Naray-Szabo, F. Sussman, and J.-K. Hwang. 1989. How do serine proteases really work? Biochemistry. 28:3629-3637.
41. Winkler, F. K., A. D'Arcy, and W. Hunziker. 1990. Structure of human pancreatic lipase. Nature. 343:771-774.