Biotransformations with engineered E. coli cells expressing wild-type and mutant Baeyer-Villiger monooxygenases under non-growing conditions

Journal of Molecular Catalysis B: Enzymatic

Volumn 46, Issue 1-4, 2007, Pages 32-36

  Clouthier, Christopher M ^a   Kayser, Margaret M ^a  

^a UNIVERSITY OF NEW BRUNSWICK   (Canada)

Author keywords

CHMO mutants; CPMO mutants; Enantiopure lactones; Monooxygenases; Non growing conditions; Oxidations

Indexed keywords

BIOTRANSFORMATIONS; CYCLOHEXANONE MONOOXYGENASE (CHMO); CYCLOPENTANONE MONOOXYGENASE (CPMO); ESCHERICHIA COLI (E. COLI) OVEREXPRESSION SYSTEMS;

ENZYMES; ESCHERICHIA COLI; FERMENTATION; OXIDATION;

CELL CULTURE;

BACTERIAL ENZYME; BAEYER VILLIGER MONOOXYGENASE; CYCLOHEXANONE MONOOXYGENASE; CYCLOPENTANONE MONOOXYGENASE; UNCLASSIFIED DRUG; UNSPECIFIC MONOOXYGENASE;

ARTICLE; BACTERIAL CELL; BAEYER VILLIGER REACTION; BIOTRANSFORMATION; CATALYST; CELL SCREENING; CELL TRANSFORMATION; ENANTIOSELECTIVITY; ESCHERICHIA COLI; FERMENTATION; OXIDATION; SCALE UP; WILD TYPE;

ESCHERICHIA COLI;

EID: 34047169797     PISSN: 13811177     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molcatb.2007.02.001     Document Type: Article

References (34)

1. Krow G.R. In: Paquette L.A. (Ed). In Organic Reactions 43 (1993), John Wiley and Sons, New York 251-296
2. ten Brink G.-J., Arends I.W.C.E., and Sheldon R.A. Chem. Rev. 104 (2004) 4105-4123
3. Corma A., Nemeth L.T., Renz M., and Valencia S. Nature 412 (2001) 423-425
4. Bolm C., Luong T.K.K., and Beckmann O. In: Katsuki T. (Ed). Asymmetric Oxidation Reactions (2001), Oxford University Press 147
5. Bolm C., Luong T.K.K., and Schlingloff G. Synlett (1997) 1151-1152
6. Stewart J.D. Curr. Org. Chem. 2 (1998) 195-216
7. Flitsch S., and Grogan G. In: Drauz K., and Waldman H. (Eds). Enzyme Catalysis in Organic Synthesis (2002), Wiley-VCH, Weinheim 1202
8. Kamberbeek N.M., Janssen D.B., van Berkel W.J.H., and Fraaije M.W. Adv. Synth. Catal. 345 (2003) 667-678
9. Mihovilovic M.D., Müller B., and Stanetty P. Eur. J. Org. Chem. (2002) 3711-3730
10. Donoghue N.A., Norris D.B., and Trudgill P.W. Eur. J. Biochem. 63 (1976) 175-192
11. Iwaki H., Hasegawa Y., Wang S., Kayser M.M., and Lau P.C.K. Appl. Environ. Microbiol. 68 (2002) 5671-5684
12. Griffin M., and Trudgill P.W. Biochem. J. 129 (1972) 595-603
13. Griffin M., and Trudgill P.W. Eur. J. Biochem. 63 (1976) 199-209
14. Wang S., Kayser M.M., Iwaki H., and Lau P.C.K. J. Mol. Catal. B: Enzymatic 22 (2003) 211-218
15. Wang S., Chen G., Kayser M.M., Iwaki H., Lau P.C.K., and Hasegawa Y. Can. J. Chem. 80 (2002) 613-621
16. Mihovilovic M.D., Müller B., Schulze A., Stanetty P., and Kayser M.M. Eur. J. Org. Chem. (2003) 2243-2249
17. Reetz M.T., Brunner B., Schneider T., Schulz F., Clouthier C.M., and Kayser M.M. Angew. Chem. Int. Ed. 43 (2004) 4075-4078
18. Clouthier C.M., Kayser M.M., and Reetz M.T. J. Org. Chem. 71 (2006) 8431-8437.
19. Kayser M.M., and Clouthier C.M. J. Org. Chem. 71 (2006) 8424-8430
20. Mihovilovic M.D., Rudroff F., Winninger A., Schneider T., Schulz F., and Reetz M.T. Org. Lett. 8 (2006) 1221-1224
21. Hilker I., Alphand V., Wohlgemuth R., and Furstoss R. Adv. Synth. Catal. 346 (2004) 203-214
22. Simpson H.D., Alphand V., and Furstoss R. J. Mol. Catal. B: Enzym. 16 (2001) 101-108
23. Stewart J.D., Reed K.W., Martinez C.A., Zhu J., Chen G., and Kayser M.M. J. Amer. Chem. Soc. 120 (1998) 3541-3548
24. Stewart J.D., Reed K.W., and Kayser M.M. J. Chem. Soc., Perkin Trans. 1 (1996) 755-757
25. Doig S.D., O'Sullivan L.M., Patel S., Ward J.M., and Woodley J.M. Enzyme Microb. Technol. 28 (2001) 265-274
26. Doig S.D., Avenell P.J., Bird P.A., Gallati P., Lander K.S., Lye G.J., Wohlgemuth R., and Woodley J.M. Biotechnol. Progr. 18 (2002) 1039-1046
27. Walton A.Z., and Stewart J.D. Biotechnol. Progr. 20 (2004) 403-411
28. Walton A.Z., and Stewart J.D. Biotechnol. Progr. 18 (2002) 262-268
29. Schulz F., Leca F., Hollmann F., and Reetz M.T. Beil. J. Org. Chem. 1 (2005) 10
30. Rudroff F., Alphand V., Furstoss R., and Mihovilovic M.D. Proc. Res. Develop. 10 (2006) 599-604
31. Yang Y., Drolet M., and Kayser M.M. Tetrahedron Asymmetr. 16 (2005) 2748-2753
32. Kayser M.M., Drolet M., and Stewart J.D. Tetrahedron Asymmetr. 16 (2005) 4004-4009
33. Taschner M.J., Black D.J., and Chen Q. Tetrahedron Asymmetr. 4 (1993) 1387-1390
34. This is in agreement with Walton and Stewart's conclusions that cyclohexanone transport, 2001 is the rate-limiting step during the initial reaction period [18] and that the decrease in the cofactor level after 24 h is most likely due to increased membrane permeability. An increased membrane permeability may contribute to the loss of the cofactor, but at the same time may allow a substrate better access into the cell.