Switch in Cofactor Specificity of a Baeyer–Villiger Monooxygenase

ChemBioChem

Volumn 17, Issue 24, 2016, Pages 2312-2315

  Beier, Andy ^a   Bordewick, Sven ^a   Genz, Maika ^a   Schmidt, Sandy ^a   van den Bergh, Tom ^b   Peters, Christin ^a   Joosten, Henk Jan ^b   Bornscheuer, Uwe T ^a  

^a UNIVERSITY OF GREIFSWALD   (Germany)

^b Bio Prodict   (Netherlands)

Author keywords

Baeyer Villiger monooxygenases; cofactor specificity; enzyme catalysis; protein engineering; rational design

Indexed keywords

BACTERIAL ENZYME; CYCLOHEXANONE MONOOXYGENASE; HYDROXYL GROUP; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; UNCLASSIFIED DRUG; UNSPECIFIC MONOOXYGENASE; WATER; CYCLOHEXANONE OXYGENASE; MIXED FUNCTION OXIDASE; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; OXYGENASE; RECOMBINANT PROTEIN;

ARTICLE; BAEYER VILLIGER REACTION; ENZYME SPECIFICITY; ENZYME STRUCTURE; HYDROGEN BOND; MUTAGENESIS; NONHUMAN; PRIORITY JOURNAL; RHODOCOCCUS; SEQUENCE ALIGNMENT; STRUCTURE ANALYSIS; ACINETOBACTER; BINDING SITE; BIOCATALYSIS; BIOSYNTHESIS; CHEMISTRY; ENZYMOLOGY; GENETICS; ISOLATION AND PURIFICATION; KINETICS; METABOLISM; MOLECULAR DYNAMICS; PROTEIN ENGINEERING; PROTEIN TERTIARY STRUCTURE; SITE DIRECTED MUTAGENESIS;

ACINETOBACTER; BINDING SITES; BIOCATALYSIS; KINETICS; MIXED FUNCTION OXYGENASES; MOLECULAR DYNAMICS SIMULATION; MUTAGENESIS, SITE-DIRECTED; NADP; OXYGENASES; PROTEIN ENGINEERING; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT PROTEINS; SUBSTRATE SPECIFICITY;

EID: 85000613413     PISSN: 14394227     EISSN: 14397633     Source Type: Journal    
DOI: 10.1002/cbic.201600484     Document Type: Article

References (37)

1. K. Balke, M. Kadow, H. Mallin, S. Saß, U. T. Bornscheuer, Org. Biomol. Chem. 2012, 10, 6249–6265.
2. A. Baeyer, V. Villiger, Ber. Dtsch. Chem. Ges. 1899, 32, 3625–3633.
3. M. Kadow, K. Balke, A. Willetts, U. T. Bornscheuer, J.-E. Bäckvall, Appl. Microbiol. Biotechnol. 2014, 98, 3975–3986.
4. A. Willetts, I. Joint, J. A. Gilbert, W. Trimble, M. Mühling, Microbial Biotechnol. 2012, 5, 549–559.
5. N. A. Donoghue, D. B. Norris, P. W. Trudgill, Eur. J. Biochem. 1976, 63, 175–192.
6. J. D. Stewart, Curr. Org. Chem. 1998, 2, 195–216;
7. M. D. Mihovilovic, B. Müller, P. Stanetty, Eur. J. Org. Chem. 2002, 3711–3730.
8. N. M. Kamerbeek, M. W. Fraaije, D. B. Janssen, Eur. J. Biochem. 2004, 271, 2107–2116.
9. J. T. Wu, L. H. Wu, J. A. Knight, Clin. Chem. 1986, 32, 314–319.
10. A. Weckbecker, H. Gröger, W. Hummel in Advances in Biochemical Engineering/Biotechnology:Biosystems Engineering I (Eds: C. Wittmann, R. Krull), Springer, 2010, pp. 195–242.
11. S. Schmidt, M. Genz, K. Balke, U. T. Bornscheuer, J. Biotechnol. 2015, 214, 199–211.
12. K. Weissermel, H.-J. Arpe, Industrial Organic Chemistry, 4th ed., Wiley-VCH, Weinheim, 2003.
13. S. Schmidt, C. Scherkus, J. Muschiol, U. Menyes, T. Winkler, W. Hummel, H. Gröger, A. Liese, H.-G. Herz, U. T. Bornscheuer, Angew. Chem. Int. Ed. 2015, 54, 2784–2787;
14. Angew. Chem. 2015, 127, 2825–2828;
15. S. Schmidt, H. C. Büchsenschütz, C. Scherkus, A. Liese, H. Gröger, U. T. Bornscheuer, ChemCatChem 2015, 7, 3951–3955.
16. M. H. M. Eppink, K. M. Overkamp, H. A. Schreuder, W. J. H. Van Berkel, J. Mol. Biol. 1999, 292, 87–96;
17. C. Didierjean, S. Rahuel-Clermont, B. Vitoux, O. Dideberg, G. Branlant, A. Aubry, J. Mol. Biol. 1997, 268, 739–759;
18. S. Brinkmann-Chen, T. Flock, J. K. B. Cahn, C. D. Snow, E. M. Brustad, J. A. McIntosh, P. Meinhold, L. Zhang, F. H. Arnold, Proc. Natl. Acad. Sci. USA 2013, 110, 10946–10951;
19. Protein Engineering Handbook, Vol. 2 (Eds.: S. Lutz, U. T. Bornscheuer), Wiley-VCH, Weinheim, Germany, 2009;
20. E. Campbell, I. R. Wheeldon, S. Banta, Biotechnol. Bioeng. 2010, 107, 763–774;
21. E. Campbell, S. Chuang, S. Banta, Protein Eng. Des. Sel. 2013, 26, 181–186;
22. V. I. Tishkov, V. O. Popov, Biomol. Eng. 2006, 23, 89–110;
23. J. K. B. Cahn, S. Brinkmann-Chen, T. Spatzal, J. A. Wiig, A. R. Buller, O. Einsle, Y. Hu, M. W. Ribbe, F. H. Arnold, Biochem. J. 2015, 468, 475–484;
24. J. K. B. Cahn, A. Baumschlager, S. Brinkmann-Chen, F. Arnold, Protein Eng. Des. Sel. 2016, 29, 31–38;
25. N. S. Scrutton, A. Berry, R. N. Perham, Nature 1990, 343, 38–43;
26. R. Chen, A. Greer, A. M. Dean, Proc. Natl. Acad. Sci. USA 1996, 93, 12171–12176;
27. N. Holmberg, U. Ryde, L. Bülow, Protein Eng. 1999, 12, 851–856;
28. A. E. Serov, A. S. Popova, V. V. Fedorchuk, V. I. Tishkov, Biochem. J. 2002, 367, 841–847;
29. S. Banta, B. A. Swanson, S. Wu, A. Jarnagin, S. Anderson, Protein Eng. 2002, 15, 131–140;
30. T. M. Penning, J. M. Jez, Chem. Rev. 2001, 101, 3027–3046;
31. J. H. Hurley, R. Chen, A. M. Dean, Biochemistry 1996, 35, 5670–5678;
32. G. A. Khoury, H. Fazelinia, J. W. Chin, R. J. Pantazes, P. C. Cirino, C. D. Maranas, Protein Sci. 2009, 18, 2125–2138;
33. S. Reiße, D. Garbe, T. Brück, Biochimie 2015, 108, 76–84.
34. A. Völker, A. Kirschner, U. T. Bornscheuer, J. Altenbuchner, Appl. Microbiol. Biotechnol. 2008, 77, 1251–1260.
35. H. M. Dudek, D. E. T. Pazmiño, C. Rodríguez, G. de Gonzalo, V. Gotor, M. W. Fraaije, Appl. Microbiol. Biotechnol. 2010, 88, 1135–1143.
36. A. Riebel, H. M. Dudek, G. de Gonzalo, P. Stepniak, L. Rychlewski, M. W. Fraaije, Appl. Microbiol. Biotechnol. 2012, 95, 1479–1489.
37. A. Kirschner, U. T. Bornscheuer, Appl. Microbiol. Biotechnol. 2008, 81, 465–472.