The role of active-site Phe87 in modulating the organic co-solvent tolerance of cytochrome P450 BM3 monooxygenase

Acta Crystallographica Section F: Structural Biology and Crystallization Communications

Volumn 68, Issue 9, 2012, Pages 1013-1017

  Kuper, Jochen ^a   Tee, Kang Lan ^b   Wilmanns, Matthias ^c   Roccatano, Danilo ^d   Schwaneberg, Ulrich ^e   Wong, Tuck Seng ^f  

^a Rudolf Virchow Centre for Biomedical Research   (Germany)

^b UNIVERSITY OF MANCHESTER   (United Kingdom)

^c DESY   (Germany)

^d JACOBS UNIVERSITY BREMEN   (Germany)

^e RWTH AACHEN UNIVERSITY   (Germany)

^f UNIVERSITY OF SHEFFIELD   (United Kingdom)

Author keywords

CYP102A1; cytochrome P450 BM3; directed evolution; DMSO; organic co solvent tolerance

Indexed keywords

CYTOCHROME P450; DIMETHYL SULFOXIDE;

ARTICLE; CHEMICAL STRUCTURE; CHEMISTRY; ENZYME ACTIVE SITE; ENZYME SPECIFICITY; HUMAN; METABOLISM;

CATALYTIC DOMAIN; CYTOCHROME P-450 ENZYME SYSTEM; DIMETHYL SULFOXIDE; HUMANS; MODELS, MOLECULAR; SUBSTRATE SPECIFICITY;

EID: 84865714068     PISSN: None     EISSN: 17443091     Source Type: Journal    
DOI: 10.1107/S1744309112031570     Document Type: Article

References (21)

1. Brenner, S., Hay, S., Girvan, H. M., Munro, A. W. & Scrutton, N. S. (2007). J. Phys. Chem. B, 111, 7879-7886.
2. Carmichael, A. B. & Wong, L.-L. (2001). Eur. J. Biochem. 268, 3117-3125.
3. Cojocaru, V., Winn, P. J. & Wade, R. C. (2007). Biochim. Biophys. Acta, 1770, 390-401.
4. Emsley, P. & Cowtan, K. (2004). Acta Cryst. D60, 2126-2132.
5. Evans, P. R. (1997). Jnt CCP4/ESF-EACBM Newsl. Protein Crystallogr. 33, 22-24.
6. Feenstra, K. A., Starikov, E. B., Urlacher, V. B., Commandeur, J. N. & Vermeulen, N. P. (2007). Protein Sci. 16, 420-431.
7. Graham-Lorence, S., Truan, G., Peterson, J. A., Falck, J. R., Wei, S., Helvig, C. & Capdevila, J. H. (1997). J. Biol. Chem. 272, 1127-1135.
8. Kuper, J.,Wong, T. S., Roccatano, D.,Wilmanns,M. & Schwaneberg, U. (2007). J. Am. Chem. Soc. 129, 5786-5787.
9. Lentz, O., Li, Q.-S., Schwaneberg,U., Lutz-Wahl, S., Fischer, P. & Schmid, R. D. (2001). J. Mol. Catal. B Enzym. 15, 123-133.
10. Leslie, A. G. W. (2006). Acta Cryst. D62, 48-57.
11. Li, H. & Poulos, T. L. (1997). Nature Struct. Biol. 4, 140-146.
12. Munro, A. W., Leys, D. G., McLean, K. J., Marshall, K. R., Ost, T. W., Daff, S., Miles, C. S., Chapman, S. K., Lysek, D. A., Moser, C. C., Page, C. C. & Dutton, P. L. (2002). Trends Biochem. Sci. 27, 250-257.
13. Murshudov, G. N., Skubák, P., Lebedev, A. A., Pannu, N. S., Steiner, R. A., Nicholls, R. A., Winn, M. D., Long, F. & Vagin, A. A. (2011). Acta Cryst. D67, 355-367.
14. Noble, M. A., Miles, C. S., Chapman, S. K., Lysek, D. A., MacKay, A. C., Reid, G. A., Hanzlik, R. P. & Munro, A. W. (1999). Biochem. J. 339, 371-379.
15. Read, R. J. (2001). Acta Cryst. D57, 1373-1382.
16. Schwaneberg, U., Otey, C., Cirino, P. C., Farinas, E. & Arnold, F. H. (2001). J. Biomol. Screen. 6, 111-117.
17. Schwaneberg, U., Schmidt-Dannert, C., Schmitt, J. & Schmid, R. D. (1999). Anal. Biochem. 269, 359-366.
18. Sevrioukova, I. F., Li, H., Zhang, H., Peterson, J. A. & Poulos, T. L. (1999). Proc. Natl Acad. Sci. USA, 96, 1863-1868.
19. Tee, K. L., Roccatano, D., Stolte, S., Arning, J., Jastorff, B. & Schwaneberg, U. (2008). Green Chem. 10, 117-123.
20. Winn, M. D. et al. (2011). Acta Cryst. D67, 235-242.
21. Wong, T. S., Arnold, F. H. & Schwaneberg, U. (2004). Biotechnol. Bioeng. 85, 351-358.