Directed evolution of an enantioselective lipase with broad substrate scope for hydrolysis of α-substituted esters

Journal of the American Chemical Society

Volumn 132, Issue 20, 2010, Pages 7038-7042

  Engström, Karin ^a   Nyhlén, Jonas ^a   Sandström, Anders G ^a   Bäckvall, Jan E ^a  

^a STOCKHOLM UNIVERSITY   (Sweden)

Author keywords

[No Author keywords available]

Indexed keywords

CANDIDA ANTARCTICA LIPASE A; DIRECTED EVOLUTION; ENANTIOMERIC EXCESS; ENANTIOSELECTIVE LIPASE; WILD TYPES;

ENZYMES; ESTERIFICATION; ESTERS; HYDROLYSIS;

SUBSTRATES;

ENZYME VARIANT; TRIACYLGLYCEROL LIPASE;

ARTICLE; CANDIDA ANTARCTICA; CONTROLLED STUDY; ENANTIOMER; ENANTIOSELECTIVITY; ENZYME SUBSTRATE; HYDROLYSIS; NONHUMAN; WILD TYPE;

CANDIDA; CATALYTIC DOMAIN; DIRECTED MOLECULAR EVOLUTION; ESTERS; HYDROLYSIS; KINETICS; LIPASE; MODELS, MOLECULAR; PHENYLPROPIONATES; STEREOISOMERISM; SUBSTRATE SPECIFICITY;

EID: 77952562463     PISSN: 00027863     EISSN: 15205126     Source Type: Journal    
DOI: 10.1021/ja100593j     Document Type: Article

References (36)

1. Evans, A. M. Eur. J. Clin. Pharmacol. 1992, 42, 237-256
2. Davies, N. M. and Anderson, K. E. Clin. Pharmacokinet. 1997, 32, 268-293
3. Davies, N. M. Clin. Pharmacokinet. 1995, 28, 100-114
4. Davies, N. M. Clin. Pharmacokinet. 1998, 34, 101-154
5. Beck, G. Synlett 2002, 6, 837-850
6. Chen, K. and Arnold, F. H. Proc. Natl. Acad. Sci. U.S.A. 1993, 90, 5618-5622
7. Reetz, M. T., Zonta, A., Schimossek, K., Jaeger, K.-E., and Liebeton, K. Angew. Chem., Int. Ed. 1997, 36, 2830-2832
8. Arnold, F. H. Acc. Chem. Res. 1998, 31, 125-131
9. Zhang, J.-H., Dawes, G., and Stemmer, W. P. C. Proc. Natl. Acad. Sci. U.S.A. 1997, 94, 4504-4509
10. Arnold, F. H. and Georgiou, G. Directed Enzyme Evolution: Screening and Selection Methods; Humana Press: Totowa, NJ, 2003; Vol. 230.
11. Otten, L. G. and Quax, L. G. Biomol. Eng. 2005, 22, 1-9
12. Turner, N. J. Nat. Chem. Biol. 2009, 5, 567-573
13. Lutz, S. and Bornscheuer, U. T. Protein Engineering Handbook; Wiley-VCH: Weinheim, Germany, 2009; Vols. 1 and 2.
14. Reetz, M. T. Proc. Natl. Acad. Sci. U.S.A. 2004, 101, 5716-5722
15. Reetz, M. T. and Wu, S. J. Am. Chem. Soc. 2009, 131, 15424-15432
16. Lewis, J. C., Bastian, S., Bennett, C. S., Fu, Y., Mitsuda, Y., Chen, M. M., Greenberg, W. A., Wong, C.-H., and Arnold, F. H. Proc. Natl. Acad. Sci. U.S.A. 2009, 106, 16550-16555
17. DeSantis, G., Wong, K., Farwell, B., Chatman, K., Zhu, Z., Tomlinson, G., Huang, H., Tan, X., Bibbs, L., Chen, P., Kretz, K., and Burk, M. J. J. Am. Chem. Soc. 2003, 125, 11476-11477
18. Landwehr, M., Hochrein, L., Otey, C. R., Kasrayan, A., Bäckvall, J.-E., and Arnold, F. H. J. Am. Chem. Soc. 2006, 128, 6058-6059
19. Lee, C. C., Williams, T. G., Wong, D. W., and Robertson, G. H. Plasmid 2005, 54, 80-85
20. Sandström, A. G., Engström, K., Nyhlén, J., Kasrayan, A., and Bäckvall, J.-E. Protein Eng., Des. Sel. 2009, 22, 413-420
21. For previous examples of extended substrate scope, see
22. Wada, M., Hsu, C.-C., Franke, D., Mitchell, M., Heine, A., Wilson, I., and Wong, C.-H. Bioorg. Med. Chem. 2003, 11, 2091-2098
23. Mihovilovic, M. D., Rudroff, F., Winninger, A., Schneider, T., Schulz, F., and Reetz, M. T. Org. Lett. 2006, 8, 1221-1224
24. Reetz, M. T., Bocola, M., Wang, L.-W., Sanchis, J., Cronin, A., Arand, M., Zou, J., Archelas, A., Bottala, A.-L., Navoryta, A., and Mowbray, S. L. J. Am. Chem. Soc. 2009, 131, 7334-7343
25. Reetz, M. T., Bocola, M., Carballeira, J. D., Zha, D., and Vogel, A. Angew. Chem., Int. Ed. 2005, 44, 4192-4196
26. Reetz, M. T., Carballeira, J. D., Peyralans, J., Höbenreich, H., Maichele, A., and Vogel, A. Chem. - Eur. J. 2006, 12, 6031-6038
27. Reetz, M. T. and Sanchis, J. ChemBioChem 2008, 9, 2260-2267
28. See also ref 9 and ref 10c.
29. Bartsch, S., Kourist, R., and Bornscheuer, U. T. Angew. Chem., Int. Ed. 2008, 47, 1508-1511
30. Liang, L., Zhang, J., and Lin, Z. Microb. Cell Fact. 2007, 6, 36
31. Ericsson, D. J., Kasrayan, A., Johansson, P., Bergfors, T., Sandström, A. G., Bäckvall, J.-E., and Mowbray, S. L. J. Mol. Biol. 2008, 376, 109-119
32. Gerber, P. R. J. Comput.-Aided Mol. Des. 1998, 12, 37-51
33. Janes, E. and Kazlauskas, R. J. J. Org. Chem. 1997, 62, 4560-4561
34. Barbayianni, E., Fotakopoulou, I., Schmidt, M., Constantinou-Kokotou, V., Bornscheuer, U. T., and Kokotos, G. J. Org. Chem. 2005, 70, 8730-8733
35. The hydrolysis of related alkyl esters catalyzed by CalA in ref 18 employed a much higher concentration of enzyme (50 - ) and a higher concentration of substrate (10 - ), and still the reactions typically took 24-48 h.
36. Schulz, N., Hobley, T. J., and Syldatk, C. Biotechnol. Lett. 2007, 29, 365-371