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References  61

               whole-cell environment, as the majority of successful case studies are based on
               such processes (either in a fully in vivo format or in combination with an in vitro
               biocatalyst). In this context, the enzyme group is a highly compatible ‘‘reagent’’
               for the combination with other biocatalysts. This can be attributed to the high
               functional and/or stereochemical selectivity of such proteins. Consequently, it can
               be expected that monooxygenases will become a versatile tool in the armory of the
               diverse catalytic systems to be utilized for the construction of nonmetabolic reaction
               cascades as well as mini-metabolic pathways en route toward true biocatalytic cell
               factories.


               References
                1. Montersino, S., Tischler, D., Gassner,  biocatalysis for selective and produc-
                  G.T., and van Berkel, W.J.H. (2011)  tive C-O functional group introduction
                  Catalytic and structural features of flavo-  and modification. Chem.Soc.Rev., 42,
                  protein hydroxylases and epoxidases.  6346–6377.
                  Adv.Synth.Catal., 353, 2301–2319.  10. Schrittwieser, J.H., Sattler, J., Resch,
                2. Pazmino, D.E.T., Winkler, M., Glieder,  V., Mutti, F.G., and Kroutil, W. (2011)
                  A., and Fraaije, M.W. (2010) Monooxy-  Recent biocatalytic oxidation-reduction
                  genases as biocatalysts: classification,  cascades. Curr. Opin. Chem. Biol., 15,
                  mechanistic aspects and biotechnological  249–256.
                  applications. J. Biotechnol., 146, 9–24.  11. Hollmann, F., Arends, I.W.C.E.,
                3. van Berkel, W.J.H., Kamerbeek, N.M.,  Buehler, K., Schallmey, A., and Buehler,
                                                  B. (2011) Enzyme-mediated oxida-
                  and Fraaije, M.W. (2006) Flavoprotein
                                                  tions for the chemist. Green Chem., 13,
                  monooxygenases, a diverse class of
                                                  226–265.
                  oxidative biocatalysts. J. Biotechnol., 124,
                                               12. Lopez-Gallego, F. and Schmidt-Dannert,
                  670–689.
                                                  C. (2010) Multi-enzymatic synthesis.
                4. Mayer, S.F., Kroutil, W., and Kurt, F.
                                                  Curr. Opin. Chem. Biol., 14, 174–183.
                  (2001) Enzyme-initiated domino (cas-
                  cade) reactions. Chem.Soc.Rev., 30,  13. Willetts, A.J., Knowles, C.J., Levitt,
                                                  M.S., Roberts, S.M., Sandey, H., and
                  332–339.
                                                  Shipston, N.F. (1991) Biotransformation
                5. Bruggink, A., Schoevaart, R., and  of endo-bicyclo[2.2.1]heptan-2-ols and
                  Kieboom, T. (2003) Concepts of nature
                                                  endo-bicyclo[3.2.0]hept-2-en-6-ol into the
                  in organic synthesis: cascade catalysis
                                                  corresponding lactones. J. Chem. Soc.,
                  and multistep conversions in concert.  Perkin Trans. 1, 1608–1610.
                  Org. Process Res. Dev., 7, 622–640.
                                               14. Stewart, J.D. (1997) A Chemist’s per-
                6. Ricca, E., Brucher, B., and Schrittwieser,
                                                  spective on the use of genetically
                  J.H. (2011) Multi-enzymatic cascade  engineered microbes as reagents for
                  reactions: overview and perspectives.  organic synthesis. Biotechnol. Genet. Eng.
                  Adv.Synth.Catal., 353, 2239–2262.  Rev., 14, 67–143.
                7. Oroz-Guinea, I. and Garcia-Junceda,  15. Peretz, M., Bogin, O., TelOr, S., Cohen,
                  E. (2013) Enzyme catalysed tandem  A., Li, G.S., Chen, J.S., and Burstein,
                  reactions. Curr. Opin. Chem. Biol., 17,  Y. (1997) Molecular cloning, nucleotide
                  236–249.                        sequencing, and expression of genes
                8. Guterl, J.K. and Sieber, V. (2013)  encoding alcohol dehydrogenases from
                  Biosynthesis ‘‘debugged’’: novel bio-  the thermophile Thermoanaerobacter
                  production strategies. Eng. Life Sci., 13,  brockii and the mesophile Clostridium
                  4–18.                           beijerinckii. Anaerobe, 3, 259–270.
                9. Schrewe, M., Julsing, M.K., Buehler,  16. Tishkov, V.I., Galkin, A.G., Fedorchuk,
                  B., and Schmid, A. (2013) Whole-cell  V.V., Savitsky, P.A., Rojkova, A.M.,
   80   81   82   83   84   85   86   87   88   89   90