메뉴 건너뛰기




Volumn 5, Issue FEB, 2014, Pages

Flavoprotein monooxygenases for oxidative biocatalysis: Recombinant expression in microbial hosts and applications

Author keywords

Baeyer Villiger oxidation; Biocatalysis; Biooxidations; Epoxidation; Flavoprotein monooxygenase; Hydroxylation; Recombinant biocatalyst; Sulfoxidation

Indexed keywords

3,6 DIKETOCAMPHANE 1,6 MONOOXYGENASE; 4 SULFOPHENYL ACETATE MONOOXYGENASE; BAEYER VILLIGER MONOOXYGENASE; CAMPHOR 1,2 MONOOXYGENASE; CYCLOHEXANONE MONOOXYGENASE; CYCLOPENTADECANONE MONOOXYGENASE; CYCLOPENTANONE MONOOXYGENASE; EPOXIDE; PHENYLACETONE MONOOXYGENASE; RECOMBINANT ENZYME; STEROID MONOOXYGENASE; STYRENE OXYGENASE; TRIMETHYLAMINE OXYGENASE; UNCLASSIFIED DRUG; UNSPECIFIC MONOOXYGENASE;

EID: 84897627714     PISSN: None     EISSN: 1664302X     Source Type: Journal    
DOI: 10.3389/fmicb.2014.00025     Document Type: Review
Times cited : (41)

References (127)
  • 1
    • 84859736232 scopus 로고    scopus 로고
    • Enantioselective oxidation by a cyclohexanone monooxygenase from the xenobiotic-degrading Polaromonas sp. strain JS666
    • doi: 10.1016/j.molcatb.2012.03.002
    • Alexander, A. K., Biedermann, D., Fink, M. J., Mihovilovic, M. D., and Mattes, T. E. (2012). Enantioselective oxidation by a cyclohexanone monooxygenase from the xenobiotic-degrading Polaromonas sp. strain JS666. J. Mol. Catal. B Enzym. 78, 105-110. doi: 10.1016/j.molcatb.2012.03.002
    • (2012) J. Mol. Catal. B Enzym. , vol.78 , pp. 105-110
    • Alexander, A.K.1    Biedermann, D.2    Fink, M.J.3    Mihovilovic, M.D.4    Mattes, T.E.5
  • 2
    • 44349089600 scopus 로고    scopus 로고
    • Revealing the moonlighting role of NADP in the structure of a flavin-containing monooxygenase
    • doi: 10.1073/pnas.0800859105
    • Alfieri, A., Malito, E., Orru, R., Fraaije, M. W., and Mattevi, A. (2008). Revealing the moonlighting role of NADP in the structure of a flavin-containing monooxygenase. Proc. Natl. Acad. Sci. U.S.A. 105, 6572-6577. doi: 10.1073/pnas.0800859105
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 6572-6577
    • Alfieri, A.1    Malito, E.2    Orru, R.3    Fraaije, M.W.4    Mattevi, A.5
  • 3
    • 80052969471 scopus 로고    scopus 로고
    • Oxidation of organoselenium compounds. A study of chemoselectivity of phenylacetone monooxygenase
    • doi: 10.1016/j.molcatb.2011.07.018
    • Andrade, L. H., Pedrozo, E. C., Leite, H. G., and Brondani, P. B. (2011). Oxidation of organoselenium compounds. A study of chemoselectivity of phenylacetone monooxygenase. J. Mol. Catal. B Enzym. 73, 63-66. doi: 10.1016/j.molcatb.2011.07.018
    • (2011) J. Mol. Catal. B Enzym. , vol.73 , pp. 63-66
    • Andrade, L.H.1    Pedrozo, E.C.2    Leite, H.G.3    Brondani, P.B.4
  • 4
    • 84981760110 scopus 로고
    • Einwirkung des Caro'schen Reagens auf Ketone
    • doi: 10.1002/cber.189903203151
    • Baeyer, A., and Villiger, V. (1899). Einwirkung des Caro'schen Reagens auf Ketone. Ber. Dtsch. Chem. Ges. 32, 3625-3633. doi: 10.1002/cber.189903203151
    • (1899) Ber. Dtsch. Chem. Ges. , vol.32 , pp. 3625-3633
    • Baeyer, A.1    Villiger, V.2
  • 5
    • 53549086464 scopus 로고    scopus 로고
    • The first 200-L scale asymmetric Baeyer-Villiger oxidation using a whole-cell biocatalyst
    • doi: 10.1021/op800046t
    • Baldwin, C. V. F., Wohlgemuth, R., and Woodley, J. M. (2008). The first 200-L scale asymmetric Baeyer-Villiger oxidation using a whole-cell biocatalyst. Org. Process Res. Dev. 12, 660-665. doi: 10.1021/op800046t
    • (2008) Org. Process Res. Dev. , vol.12 , pp. 660-665
    • Baldwin, C.V.F.1    Wohlgemuth, R.2    Woodley, J.M.3
  • 6
    • 84863953159 scopus 로고    scopus 로고
    • Discovery, application and protein engineering of Baeyer-Villiger monooxygenases for organic synthesis
    • doi: 10.1039/c2ob25704a
    • Balke, K., Kadow, M., Mallin, H., Sass, S., and Bornscheuer, U. T. (2012). Discovery, application and protein engineering of Baeyer-Villiger monooxygenases for organic synthesis. Org. Biomol. Chem. 10, 6249-6265. doi: 10.1039/c2ob25704a
    • (2012) Org. Biomol. Chem. , vol.10 , pp. 6249-6265
    • Balke, K.1    Kadow, M.2    Mallin, H.3    Sass, S.4    Bornscheuer, U.T.5
  • 7
    • 84887067918 scopus 로고    scopus 로고
    • Discovery of Baeyer-Villiger monooxygenases from photosynthetic eukaryotes
    • doi: 10.1016/j.molcatb.2013.10.006
    • Beneventi, E., Niero, M., Motterle, R., Fraaije, M. W., and Bergantino, E. (2013). Discovery of Baeyer-Villiger monooxygenases from photosynthetic eukaryotes. J. Mol. Catal. B Enzym. 98, 145-154. doi: 10.1016/j.molcatb.2013.10.006
    • (2013) J. Mol. Catal. B Enzym. , vol.98 , pp. 145-154
    • Beneventi, E.1    Niero, M.2    Motterle, R.3    Fraaije, M.W.4    Bergantino, E.5
  • 8
    • 63249107451 scopus 로고    scopus 로고
    • Enzymatic Baeyer-Villiger oxidation of steroids with cyclopentadecanone monooxygenase
    • doi: 10.1016/j.molcatb.2008.12.009
    • Beneventi, E., Ottolina, G., Carrea, G., Panzeri, W., Fronza, G., and Lau, P. C. K. (2009). Enzymatic Baeyer-Villiger oxidation of steroids with cyclopentadecanone monooxygenase. J. Mol. Catal. B Enzym. 58, 164-168. doi: 10.1016/j.molcatb.2008.12.009
    • (2009) J. Mol. Catal. B Enzym. , vol.58 , pp. 164-168
    • Beneventi, E.1    Ottolina, G.2    Carrea, G.3    Panzeri, W.4    Fronza, G.5    Lau, P.C.K.6
  • 9
    • 84876117899 scopus 로고    scopus 로고
    • Enantiocomplementary access to carba-analogs of C-nucleoside derivatives by recombinant Baeyer-Villiger monooxygenases
    • doi: 10.1016/j.bmcl.2013.02.085
    • Bianchi, D. A., Moran-Ramallal, R., Iqbal, N., Rudroff, F., and Mihovilovic, M. D. (2013). Enantiocomplementary access to carba-analogs of C-nucleoside derivatives by recombinant Baeyer-Villiger monooxygenases. Bioorg. Med. Chem. Lett. 23, 2718-2720. doi: 10.1016/j.bmcl.2013.02.085
    • (2013) Bioorg. Med. Chem. Lett. , vol.23 , pp. 2718-2720
    • Bianchi, D.A.1    Moran-Ramallal, R.2    Iqbal, N.3    Rudroff, F.4    Mihovilovic, M.D.5
  • 10
    • 20544433645 scopus 로고    scopus 로고
    • Converting phenylacetone monooxygenase into phenylcyclohexanone monooxygenase by rational design: towards practical Baeyer-Villiger monooxygenases
    • doi: 10.1002/adsc.200505069
    • Bocola, M., Schulz, F., Leca, F., Vogel, A., Fraaije, M. W., and Reetz, M. T. (2005). Converting phenylacetone monooxygenase into phenylcyclohexanone monooxygenase by rational design: towards practical Baeyer-Villiger monooxygenases. Adv. Synth. Catal. 347, 979-986. doi: 10.1002/adsc.200505069
    • (2005) Adv. Synth. Catal. , vol.347 , pp. 979-986
    • Bocola, M.1    Schulz, F.2    Leca, F.3    Vogel, A.4    Fraaije, M.W.5    Reetz, M.T.6
  • 11
    • 84859567304 scopus 로고    scopus 로고
    • An enzymatic pathway for the biosynthesis of the formylhydroxyornithine required for rhodochelin iron coordination
    • doi: 10.1021/bi201837f
    • Bosello, M., Mielcarek, A., Giessen, T. W., and Marahiel, M. A. (2012). An enzymatic pathway for the biosynthesis of the formylhydroxyornithine required for rhodochelin iron coordination. Biochemistry 51, 3059-3066. doi: 10.1021/bi201837f
    • (2012) Biochemistry , vol.51 , pp. 3059-3066
    • Bosello, M.1    Mielcarek, A.2    Giessen, T.W.3    Marahiel, M.A.4
  • 12
    • 84555178925 scopus 로고    scopus 로고
    • Bacterial dioxygenase-and monooxygenase-catalysed sulfoxidation of benzo[b]thiophenes
    • doi: 10.1039/c1ob06678a
    • Boyd, D. R., Sharma, N. D., Mcmurray, B., Haughey, S. A., Allen, C. C., Hamilton, J. T., et al. (2012). Bacterial dioxygenase-and monooxygenase-catalysed sulfoxidation of benzo[b]thiophenes. Org. Biomol. Chem. 10, 782-790. doi: 10.1039/c1ob06678a
    • (2012) Org. Biomol. Chem. , vol.10 , pp. 782-790
    • Boyd, D.R.1    Sharma, N.D.2    Mcmurray, B.3    Haughey, S.A.4    Allen, C.C.5    Hamilton, J.T.6
  • 13
    • 33845377504 scopus 로고
    • Functional group diversity in enzymic oxygenation reactions catalyzed by bacterial flavin-containing cyclohexanone oxygenase
    • doi: 10.1021/ja00293a054
    • Branchaud, B. P., and Walsh, C. T. (1985). Functional group diversity in enzymic oxygenation reactions catalyzed by bacterial flavin-containing cyclohexanone oxygenase. J. Am. Chem. Soc. 107, 2153-2161. doi: 10.1021/ja00293a054
    • (1985) J. Am. Chem. Soc. , vol.107 , pp. 2153-2161
    • Branchaud, B.P.1    Walsh, C.T.2
  • 14
    • 80052014695 scopus 로고    scopus 로고
    • Selective oxidations of organoboron compounds catalyzed by Baeyer-Villiger monooxygenases
    • doi: 10.1002/adsc.201100029
    • Brondani, P. B., de Gonzalo, G., Fraaije, M. W., and Andrade, L. H. (2011). Selective oxidations of organoboron compounds catalyzed by Baeyer-Villiger monooxygenases. Adv. Synth. Catal. 353, 2169-2173. doi: 10.1002/adsc.201100029
    • (2011) Adv. Synth. Catal. , vol.353 , pp. 2169-2173
    • Brondani, P.B.1    de Gonzalo, G.2    Fraaije, M.W.3    Andrade, L.H.4
  • 15
    • 84862691571 scopus 로고    scopus 로고
    • Exploiting the enantioselectivity of Baeyer-Villiger monooxygenases via boron oxidation
    • doi: 10.1016/j.tetasy.2012.05.004
    • Brondani, P. B., Dudek, H., Reis, J. S., Fraaije, M. W., and Andrade, L. H. (2012a). Exploiting the enantioselectivity of Baeyer-Villiger monooxygenases via boron oxidation. Tetrahedron 23, 703-708. doi: 10.1016/j.tetasy.2012.05.004
    • (2012) Tetrahedron , vol.23 , pp. 703-708
    • Brondani, P.B.1    Dudek, H.2    Reis, J.S.3    Fraaije, M.W.4    Andrade, L.H.5
  • 16
    • 84868502808 scopus 로고    scopus 로고
    • Chemoenzymatic approaches to obtain chiral-centered selenium compounds
    • doi: 10.1016/j.tet.2012.09.087
    • Brondani, P. B., Guilmoto, N. M. A. F., Dudek, H. M., Fraaije, M. W., and Andrade, L. H. (2012b). Chemoenzymatic approaches to obtain chiral-centered selenium compounds. Tetrahedron 68, 10431-10436. doi: 10.1016/j.tet.2012.09.087
    • (2012) Tetrahedron , vol.68 , pp. 10431-10436
    • Brondani, P.B.1    Guilmoto, N.M.A.F.2    Dudek, H.M.3    Fraaije, M.W.4    Andrade, L.H.5
  • 17
    • 79960576970 scopus 로고    scopus 로고
    • Continuous testing system for Baeyer-Villiger biooxidation using recombinant Escherichia coli expressing cyclohexanone monooxygenase encapsulated in polyelectrolyte complex capsules
    • doi: 10.1016/j.enzmictec.2011.05.013
    • Bučko, M., Schenkmayerová, A., Gemeiner, P., Vikartovská, A., Mihovilovic, M. D., and Lacík, I. (2011). Continuous testing system for Baeyer-Villiger biooxidation using recombinant Escherichia coli expressing cyclohexanone monooxygenase encapsulated in polyelectrolyte complex capsules. Enzyme Microb. Technol. 49, 284-288. doi: 10.1016/j.enzmictec.2011.05.013
    • (2011) Enzyme Microb. Technol. , vol.49 , pp. 284-288
    • Bučko, M.1    Schenkmayerová, A.2    Gemeiner, P.3    Vikartovská, A.4    Mihovilovic, M.D.5    Lacík, I.6
  • 18
    • 40549093298 scopus 로고    scopus 로고
    • NADH availability limits asymmetric biocatalytic epoxidation in a growing recombinant Escherichia coli strain
    • doi: 10.1128/AEM.02234-07
    • Bühler, B., Park, J. B., Blank, L. M., and Schmid, A. (2008). NADH availability limits asymmetric biocatalytic epoxidation in a growing recombinant Escherichia coli strain. Appl. Environ. Microbiol. 74, 1436-1446. doi: 10.1128/AEM.02234-07
    • (2008) Appl. Environ. Microbiol. , vol.74 , pp. 1436-1446
    • Bühler, B.1    Park, J.B.2    Blank, L.M.3    Schmid, A.4
  • 19
    • 75349094072 scopus 로고    scopus 로고
    • Studies on the mechanism of p-hydroxyphenylacetate 3-hydroxylase from Pseudomonas aeruginosa: a system composed of a small flavin reductase and a large flavin-dependent oxygenase
    • doi: 10.1021/bi901454u
    • Chakraborty, S., Ortiz-Maldonado, M., Entsch, B., and Ballou, D. P. (2010). Studies on the mechanism of p-hydroxyphenylacetate 3-hydroxylase from Pseudomonas aeruginosa: a system composed of a small flavin reductase and a large flavin-dependent oxygenase. Biochemistry 49, 372-385. doi: 10.1021/bi901454u
    • (2010) Biochemistry , vol.49 , pp. 372-385
    • Chakraborty, S.1    Ortiz-Maldonado, M.2    Entsch, B.3    Ballou, D.P.4
  • 20
    • 42749084315 scopus 로고    scopus 로고
    • Examination and expansion of the substrate range of m-hydroxybenzoate hydroxylase
    • doi: 10.1016/j.bbrc.2008.04.032
    • Chang, H. K., and Zylstra, G. J. (2008). Examination and expansion of the substrate range of m-hydroxybenzoate hydroxylase. Biochem. Biophys. Res. Commun. 371, 149-153. doi: 10.1016/j.bbrc.2008.04.032
    • (2008) Biochem. Biophys. Res. Commun. , vol.371 , pp. 149-153
    • Chang, H.K.1    Zylstra, G.J.2
  • 21
    • 80055095638 scopus 로고    scopus 로고
    • Bacterial flavin-containing monooxygenase is trimethylamine monooxygenase
    • doi: 10.1073/pnas.1112928108
    • Chen, Y., Patel, N. A., Crombie, A., Scrivens, J. H., and Murrell, J. C. (2011). Bacterial flavin-containing monooxygenase is trimethylamine monooxygenase. Proc. Natl. Acad. Sci. U.S.A. 108, 17791-17796. doi: 10.1073/pnas.1112928108
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 17791-17796
    • Chen, Y.1    Patel, N.A.2    Crombie, A.3    Scrivens, J.H.4    Murrell, J.C.5
  • 22
    • 0038772084 scopus 로고    scopus 로고
    • A novel flavin-containing monooxygenase from Methylophaga sp strain SK1 and its indigo synthesis in Escherichia coli
    • doi: 10.1016/S0006-291X(03)01087-8
    • Choi, H. S., Kim, J. K., Cho, E. H., Kim, Y. C., Kim, J. I., and Kim, S. W. (2003). A novel flavin-containing monooxygenase from Methylophaga sp strain SK1 and its indigo synthesis in Escherichia coli. Biochem. Biophys. Res. Commun. 306, 930-936. doi: 10.1016/S0006-291X(03)01087-8
    • (2003) Biochem. Biophys. Res. Commun. , vol.306 , pp. 930-936
    • Choi, H.S.1    Kim, J.K.2    Cho, E.H.3    Kim, Y.C.4    Kim, J.I.5    Kim, S.W.6
  • 23
    • 79952575497 scopus 로고    scopus 로고
    • Biotransformation of 4-halophenols to 4-halocatechols using Escherichia coli expressing 4-hydroxyphenylacetate 3-hydroxylase
    • doi: 10.1007/s00253-010-2969-5
    • Coulombel, L., Nolan, L. C., Nikodinovic, J., Doyle, E. M., and O'connor, K. E. (2011). Biotransformation of 4-halophenols to 4-halocatechols using Escherichia coli expressing 4-hydroxyphenylacetate 3-hydroxylase. Appl. Microbiol. Biotechnol. 89, 1867-1875. doi: 10.1007/s00253-010-2969-5
    • (2011) Appl. Microbiol. Biotechnol. , vol.89 , pp. 1867-1875
    • Coulombel, L.1    Nolan, L.C.2    Nikodinovic, J.3    Doyle, E.M.4    O'connor, K.E.5
  • 24
    • 84873152061 scopus 로고    scopus 로고
    • Recent developments in flavin-based catalysis
    • doi: 10.1002/cctc.201200466
    • de Gonzalo, G., and Fraaije, M. W. (2013). Recent developments in flavin-based catalysis. ChemCatChem 5, 403-415. doi: 10.1002/cctc.201200466
    • (2013) ChemCatChem , vol.5 , pp. 403-415
    • de Gonzalo, G.1    Fraaije, M.W.2
  • 25
    • 78049304724 scopus 로고    scopus 로고
    • Recent developments in the application of Baeyer-Villiger monooxygenases as biocatalysts
    • doi: 10.1002/cbic.201000395
    • de Gonzalo, G., Mihovilovic, M. D., and Fraaije, M. W. (2010). Recent developments in the application of Baeyer-Villiger monooxygenases as biocatalysts. ChemBioChem 11, 2208-2231. doi: 10.1002/cbic.201000395
    • (2010) ChemBioChem , vol.11 , pp. 2208-2231
    • de Gonzalo, G.1    Mihovilovic, M.D.2    Fraaije, M.W.3
  • 26
    • 23644435915 scopus 로고    scopus 로고
    • 2O)]2+ as a coenzyme substitute in enzymatic oxidations catalyzed by Baeyer-Villiger monooxygenases
    • doi: 10.1039/b504921k.
    • 2O)]2+ as a coenzyme substitute in enzymatic oxidations catalyzed by Baeyer-Villiger monooxygenases. Chem. Commun. 3724-3726. doi: 10.1039/b504921k
    • (2005) Chem. Commun. , pp. 3724-3726
    • de Gonzalo, G.1    Ottolina, G.2    Carrea, G.3    Fraaije, M.W.4
  • 27
    • 24944565284 scopus 로고    scopus 로고
    • Oxidations catalyzed by phenylacetone monooxygenase from Thermobifida fusca
    • doi: 10.1016/j.tetasy.2005.08.004
    • de Gonzalo, G., Torres Pazmiño, D. E., Ottolina, G., Fraaije, M. W., and Carrea, G. (2005b). Oxidations catalyzed by phenylacetone monooxygenase from Thermobifida fusca. Tetrahedron 16, 3077-3083. doi: 10.1016/j.tetasy.2005.08.004
    • (2005) Tetrahedron , vol.16 , pp. 3077-3083
    • de Gonzalo, G.1    Torres Pazmiño, D.E.2    Ottolina, G.3    Fraaije, M.W.4    Carrea, G.5
  • 28
    • 33645991489 scopus 로고    scopus 로고
    • Biocatalytic properties of Baeyer-Villiger monooxygenases in aqueous-organic media
    • doi: 10.1016/j.molcatb.2006.01.010
    • de Gonzalo, G., Ottolina, G., Zambianchi, F., Fraaije, M. W., and Carrea, G. (2006a). Biocatalytic properties of Baeyer-Villiger monooxygenases in aqueous-organic media. J. Mol. Catal. B Enzym. 39, 91-97. doi: 10.1016/j.molcatb.2006.01.010
    • (2006) J. Mol. Catal. B Enzym. , vol.39 , pp. 91-97
    • de Gonzalo, G.1    Ottolina, G.2    Zambianchi, F.3    Fraaije, M.W.4    Carrea, G.5
  • 29
    • 30944441847 scopus 로고    scopus 로고
    • 4-Hydroxyacetophenone monooxygenase from Pseudomonas fluorescens ACB as an oxidative biocatalyst in the synthesis of optically active sulfoxides
    • doi: 10.1016/j.tetasy.2005.11.024
    • de Gonzalo, G., Torres Pazmiño, D. E., Ottolina, G., Fraaije, M. W., and Carrea, G. (2006b). 4-Hydroxyacetophenone monooxygenase from Pseudomonas fluorescens ACB as an oxidative biocatalyst in the synthesis of optically active sulfoxides. Tetrahedron 17, 130-135. doi: 10.1016/j.tetasy.2005.11.024
    • (2006) Tetrahedron , vol.17 , pp. 130-135
    • de Gonzalo, G.1    Torres Pazmiño, D.E.2    Ottolina, G.3    Fraaije, M.W.4    Carrea, G.5
  • 30
    • 82455192255 scopus 로고    scopus 로고
    • Improvement of the biocatalytic properties of one phenylacetone monooxygenase mutant in hydrophilic organic solvents
    • doi: 10.1016/j.enzmictec.2011.09.006
    • de Gonzalo, G., Rodríguez, C., Rioz-Martínez, A., and Gotor, V. (2012). Improvement of the biocatalytic properties of one phenylacetone monooxygenase mutant in hydrophilic organic solvents. Enzyme Microb. Technol. 50, 43-49. doi: 10.1016/j.enzmictec.2011.09.006
    • (2012) Enzyme Microb. Technol. , vol.50 , pp. 43-49
    • de Gonzalo, G.1    Rodríguez, C.2    Rioz-Martínez, A.3    Gotor, V.4
  • 31
    • 80053333905 scopus 로고    scopus 로고
    • Turning a riboflavin-binding protein into a self-sufficient monooxygenase by cofactor redesign
    • doi: 10.1039/c1cc14039f
    • de Gonzalo, G., Smit, C., Jin, J., Minnaard, A. J., and Fraaije, M. W. (2011). Turning a riboflavin-binding protein into a self-sufficient monooxygenase by cofactor redesign. Chem. Commun. 47, 11050-11052. doi: 10.1039/c1cc14039f
    • (2011) Chem. Commun. , vol.47 , pp. 11050-11052
    • de Gonzalo, G.1    Smit, C.2    Jin, J.3    Minnaard, A.J.4    Fraaije, M.W.5
  • 32
    • 0037293124 scopus 로고    scopus 로고
    • Indigo production by Escherichia coli carrying the phenol hydroxylase gene from Acinetobacter sp strain ST-550 in a water-organic solvent two-phase system
    • doi: 10.1007/s00253-002-1187-1
    • Doukyu, N., Toyoda, K., and Aono, R. (2003). Indigo production by Escherichia coli carrying the phenol hydroxylase gene from Acinetobacter sp strain ST-550 in a water-organic solvent two-phase system. Appl. Microbiol. Biotechnol. 60, 720-725. doi: 10.1007/s00253-002-1187-1
    • (2003) Appl. Microbiol. Biotechnol. , vol.60 , pp. 720-725
    • Doukyu, N.1    Toyoda, K.2    Aono, R.3
  • 33
    • 80052619580 scopus 로고    scopus 로고
    • Mapping the substrate binding site of phenylacetone monooxygenase from Thermobifida fusca by mutational analysis
    • doi: 10.1128/AEM.00687-11
    • Dudek, H. M., de Gonzalo, G., Torres Pazmiño, D. E., Stepniak, P., Wyrwicz, L. S., Rychlewski, L., et al. (2011). Mapping the substrate binding site of phenylacetone monooxygenase from Thermobifida fusca by mutational analysis. Appl. Environ. Microbiol. 77, 5730-5738. doi: 10.1128/AEM.00687-11
    • (2011) Appl. Environ. Microbiol. , vol.77 , pp. 5730-5738
    • Dudek, H.M.1    de Gonzalo, G.2    Torres Pazmiño, D.E.3    Stepniak, P.4    Wyrwicz, L.S.5    Rychlewski, L.6
  • 35
    • 84879473655 scopus 로고    scopus 로고
    • A generic, whole-cell-based screening method for Baeyer-Villiger monooxygenases
    • doi: 10.1177/1087057113480390
    • Dudek, H. M., Popken, P., van Bloois, E., Duetz, W. A., and Fraaije, M. W. (2013b). A generic, whole-cell-based screening method for Baeyer-Villiger monooxygenases. J. Biomol. Screen. 18, 678-687. doi: 10.1177/1087057113480390
    • (2013) J. Biomol. Screen. , vol.18 , pp. 678-687
    • Dudek, H.M.1    Popken, P.2    van Bloois, E.3    Duetz, W.A.4    Fraaije, M.W.5
  • 36
    • 0020612907 scopus 로고
    • Expression of the naphthalene oxidation genes in Escherichia coli results in the biosynthesis of indigo
    • doi: 10.1126/science.6353574
    • Ensley, B. D., Ratzkin, B. J., Osslund, T. D., Simpson, M. J., Wackett, L. P., and Gibson, D. T. (1983). Expression of the naphthalene oxidation genes in Escherichia coli results in the biosynthesis of indigo. Science 222, 167-169. doi: 10.1126/science.6353574
    • (1983) Science , vol.222 , pp. 167-169
    • Ensley, B.D.1    Ratzkin, B.J.2    Osslund, T.D.3    Simpson, M.J.4    Wackett, L.P.5    Gibson, D.T.6
  • 37
    • 0024261763 scopus 로고
    • Sequence and organization of pobA, the gene coding for p-hydroxybenzoate hydroxylase, an inducible enzyme from Pseudomonas aeruginosa
    • doi: 10.1016/0378-1119(88)90044-3
    • Entsch, B., Nan, Y., Weaich, K., and Scott, K. F. (1988). Sequence and organization of pobA, the gene coding for p-hydroxybenzoate hydroxylase, an inducible enzyme from Pseudomonas aeruginosa. Gene 71, 279-291. doi: 10.1016/0378-1119(88)90044-3
    • (1988) Gene , vol.71 , pp. 279-291
    • Entsch, B.1    Nan, Y.2    Weaich, K.3    Scott, K.F.4
  • 38
    • 80052967347 scopus 로고    scopus 로고
    • Extensive substrate profiling of cyclopentadecanone monooxygenase as Baeyer-Villiger biocatalyst reveals novel regiodivergent oxidations
    • doi: 10.1016/j.molcatb.2011.07.003
    • Fink, M. J., Fischer, T. C., Rudroff, F., Dudek, H., Fraaije, M. W., and Mihovilovic, M. D. (2011). Extensive substrate profiling of cyclopentadecanone monooxygenase as Baeyer-Villiger biocatalyst reveals novel regiodivergent oxidations. J. Mol. Catal. B Enzym. 73, 9-16. doi: 10.1016/j.molcatb.2011.07.003
    • (2011) J. Mol. Catal. B Enzym. , vol.73 , pp. 9-16
    • Fink, M.J.1    Fischer, T.C.2    Rudroff, F.3    Dudek, H.4    Fraaije, M.W.5    Mihovilovic, M.D.6
  • 39
    • 84871090417 scopus 로고    scopus 로고
    • Quantitative comparison of chiral catalysts selectivity and performance: a generic concept illustrated with cyclododecanone monooxygenase as Baeyer-Villiger biocatalyst
    • doi: 10.1002/adsc.201200453
    • Fink, M. J., Rial, D. V., Kapita, P., Lengar, A., Rehdorf, J., Cheng, Q., et al. (2012). Quantitative comparison of chiral catalysts selectivity and performance: a generic concept illustrated with cyclododecanone monooxygenase as Baeyer-Villiger biocatalyst. Adv. Synth. Catal. 354, 3491-3500. doi: 10.1002/adsc.201200453
    • (2012) Adv. Synth. Catal. , vol.354 , pp. 3491-3500
    • Fink, M.J.1    Rial, D.V.2    Kapita, P.3    Lengar, A.4    Rehdorf, J.5    Cheng, Q.6
  • 40
    • 0037042197 scopus 로고    scopus 로고
    • Identification of a Baeyer-Villiger monooxygenase sequence motif
    • doi: 10.1016/S0014-5793(02)02623-6
    • Fraaije, M. W., Kamerbeek, N. M., van Berkel, W. J., and Janssen, D. B. (2002). Identification of a Baeyer-Villiger monooxygenase sequence motif. FEBS Lett. 518, 43-47. doi: 10.1016/S0014-5793(02)02623-6
    • (2002) FEBS Lett. , vol.518 , pp. 43-47
    • Fraaije, M.W.1    Kamerbeek, N.M.2    van Berkel, W.J.3    Janssen, D.B.4
  • 42
    • 84863313527 scopus 로고    scopus 로고
    • Exploring the structural basis of substrate preferences in Baeyer-Villiger monooxygenases: insight from steroid monooxygenase
    • doi: 10.1074/jbc.M112.372177
    • Franceschini, S., van Beek, H. L., Pennetta, A., Martinoli, C., Fraaije, M. W., and Mattevi, A. (2012). Exploring the structural basis of substrate preferences in Baeyer-Villiger monooxygenases: insight from steroid monooxygenase. J. Biol. Chem. 287, 22626-22634. doi: 10.1074/jbc.M112.372177
    • (2012) J. Biol. Chem. , vol.287 , pp. 22626-22634
    • Franceschini, S.1    van Beek, H.L.2    Pennetta, A.3    Martinoli, C.4    Fraaije, M.W.5    Mattevi, A.6
  • 43
    • 84895567367 scopus 로고    scopus 로고
    • Catalytic activity of the two-component flavin-dependent monooxygenase from Pseudomonas aeruginosa toward cinnamic acid derivatives
    • doi: 10.1007/s00253-013-4958-y.
    • Furuya, T., and Kino, K. (2013). Catalytic activity of the two-component flavin-dependent monooxygenase from Pseudomonas aeruginosa toward cinnamic acid derivatives. Appl. Microbiol. Biotechnol. doi: 10.1007/s00253-013-4958-y
    • (2013) Appl. Microbiol. Biotechnol.
    • Furuya, T.1    Kino, K.2
  • 44
    • 27744568351 scopus 로고    scopus 로고
    • Molecular and biochemical characterization of the xlnD-encoded 3-hydroxybenzoate 6-hydroxylase involved in the degradation of 2,5-xylenol via the gentisate pathway in Pseudomonas alcaligenes NCIMB 9867
    • doi: 10.1128/JB.187.22.7696-7702.2005
    • Gao, X., Tan, C. L., Yeo, C. C., and Poh, C. L. (2005). Molecular and biochemical characterization of the xlnD-encoded 3-hydroxybenzoate 6-hydroxylase involved in the degradation of 2,5-xylenol via the gentisate pathway in Pseudomonas alcaligenes NCIMB 9867. J. Bacteriol. 187, 7696-7702. doi: 10.1128/JB.187.22.7696-7702.2005
    • (2005) J. Bacteriol. , vol.187 , pp. 7696-7702
    • Gao, X.1    Tan, C.L.2    Yeo, C.C.3    Poh, C.L.4
  • 45
    • 33749649804 scopus 로고    scopus 로고
    • Heterologous expression, purification, and characterization of an l-ornithine N(5)-hydroxylase involved in pyoverdine siderophore biosynthesis in Pseudomonas aeruginosa
    • doi: 10.1128/JB.00949-06
    • Ge, L., and Seah, S. Y. (2006). Heterologous expression, purification, and characterization of an l-ornithine N(5)-hydroxylase involved in pyoverdine siderophore biosynthesis in Pseudomonas aeruginosa. J. Bacteriol. 188, 7205-7210. doi: 10.1128/JB.00949-06
    • (2006) J. Bacteriol. , vol.188 , pp. 7205-7210
    • Ge, L.1    Seah, S.Y.2
  • 46
    • 78149414692 scopus 로고    scopus 로고
    • Scale-up of Baeyer-Villiger monooxygenase-catalyzed synthesis of enantiopure compounds
    • doi: 10.1007/s00253-010-2724-y
    • Geitner, K., Rehdorf, J., Snajdrova, R., and Bornscheuer, U. T. (2010). Scale-up of Baeyer-Villiger monooxygenase-catalyzed synthesis of enantiopure compounds. Appl. Microbiol. Biotechnol. 88, 1087-1093. doi: 10.1007/s00253-010-2724-y
    • (2010) Appl. Microbiol. Biotechnol. , vol.88 , pp. 1087-1093
    • Geitner, K.1    Rehdorf, J.2    Snajdrova, R.3    Bornscheuer, U.T.4
  • 47
    • 76649092627 scopus 로고    scopus 로고
    • In vitro evolution of styrene monooxygenase from Pseudomonas putida CA-3 for improved epoxide synthesis
    • doi: 10.1007/s00253-009-2096-3
    • Gursky, L. J., Nikodinovic-Runic, J., Feenstra, K. A., and O'connor, K. E. (2010). In vitro evolution of styrene monooxygenase from Pseudomonas putida CA-3 for improved epoxide synthesis. Appl. Microbiol. Biotechnol. 85, 995-1004. doi: 10.1007/s00253-009-2096-3
    • (2010) Appl. Microbiol. Biotechnol. , vol.85 , pp. 995-1004
    • Gursky, L.J.1    Nikodinovic-Runic, J.2    Feenstra, K.A.3    O'connor, K.E.4
  • 48
    • 79951518313 scopus 로고    scopus 로고
    • Bio-indigo production in two different fermentation systems using recombinant Escherichia coli cells harboring a flavin-containing monooxygenase gene (fmo)
    • doi: 10.1016/j.procbio.2010.10.015
    • Han, G. H., Bang, S. E., Babu, B. K., Chang, M., Shin, H. J., and Kim, S. W. (2011). Bio-indigo production in two different fermentation systems using recombinant Escherichia coli cells harboring a flavin-containing monooxygenase gene (fmo). Proc. Biochem. 46, 788-791. doi: 10.1016/j.procbio.2010.10.015
    • (2011) Proc. Biochem. , vol.46 , pp. 788-791
    • Han, G.H.1    Bang, S.E.2    Babu, B.K.3    Chang, M.4    Shin, H.J.5    Kim, S.W.6
  • 49
    • 43049141442 scopus 로고    scopus 로고
    • Optimization of bio-indigo production by recombinant E. coli harboring fmo gene
    • doi: 10.1016/j.enzmictec.2008.02.004
    • Han, G. H., Shin, H. J., and Kim, S. W. (2008). Optimization of bio-indigo production by recombinant E. coli harboring fmo gene. Enzyme Microb. Technol. 42, 617-623. doi: 10.1016/j.enzmictec.2008.02.004
    • (2008) Enzyme Microb. Technol. , vol.42 , pp. 617-623
    • Han, G.H.1    Shin, H.J.2    Kim, S.W.3
  • 50
    • 34347247296 scopus 로고    scopus 로고
    • A light-driven stereoselective biocatalytic oxidation
    • doi: 10.1002/anie.200605169
    • Hollmann, F., Taglieber, A., Schulz, F., and Reetz, M. T. (2007). A light-driven stereoselective biocatalytic oxidation. Angew Chem. Int. Ed. 46, 2903-2906. doi: 10.1002/anie.200605169
    • (2007) Angew Chem. Int. Ed. , vol.46 , pp. 2903-2906
    • Hollmann, F.1    Taglieber, A.2    Schulz, F.3    Reetz, M.T.4
  • 51
    • 84877105687 scopus 로고    scopus 로고
    • Camphor pathway redux: functional recombinant expression of 2,5-and 3,6-diketocamphane monooxygenases of Pseudomonas putida ATCC 17453 with their cognate flavin reductase catalyzing Baeyer-Villiger reactions
    • doi: 10.1128/AEM.03958-12
    • Iwaki, H., Grosse, S., Bergeron, H., Leisch, H., Morley, K., Hasegawa, Y., et al. (2013). Camphor pathway redux: functional recombinant expression of 2,5-and 3,6-diketocamphane monooxygenases of Pseudomonas putida ATCC 17453 with their cognate flavin reductase catalyzing Baeyer-Villiger reactions. Appl. Environ. Microbiol. 79, 3282-3293. doi: 10.1128/AEM.03958-12
    • (2013) Appl. Environ. Microbiol. , vol.79 , pp. 3282-3293
    • Iwaki, H.1    Grosse, S.2    Bergeron, H.3    Leisch, H.4    Morley, K.5    Hasegawa, Y.6
  • 52
    • 33646140803 scopus 로고    scopus 로고
    • Pseudomonad cyclopentadecanone monooxygenase displaying an uncommon spectrum of Baeyer-Villiger oxidations of cyclic ketones
    • doi: 10.1128/AEM.72.4.2707-2720.2006
    • Iwaki, H., Wang, S., Grosse, S., Bergeron, H., Nagahashi, A., Lertvorachon, J., et al. (2006). Pseudomonad cyclopentadecanone monooxygenase displaying an uncommon spectrum of Baeyer-Villiger oxidations of cyclic ketones. Appl. Environ. Microbiol. 72, 2707-2720. doi: 10.1128/AEM.72.4.2707-2720.2006
    • (2006) Appl. Environ. Microbiol. , vol.72 , pp. 2707-2720
    • Iwaki, H.1    Wang, S.2    Grosse, S.3    Bergeron, H.4    Nagahashi, A.5    Lertvorachon, J.6
  • 53
    • 84859593802 scopus 로고    scopus 로고
    • A flavoprotein monooxygenase that catalyses a Baeyer-Villiger reaction and thioether oxidation using NADH as the nicotinamide cofactor
    • doi: 10.1002/cbic.201200006
    • Jensen, C. N., Cartwright, J., Ward, J., Hart, S., Turkenburg, J. P., Ali, S. T., et al. (2012). A flavoprotein monooxygenase that catalyses a Baeyer-Villiger reaction and thioether oxidation using NADH as the nicotinamide cofactor. ChemBioChem 13, 872-878. doi: 10.1002/cbic.201200006
    • (2012) ChemBioChem , vol.13 , pp. 872-878
    • Jensen, C.N.1    Cartwright, J.2    Ward, J.3    Hart, S.4    Turkenburg, J.P.5    Ali, S.T.6
  • 54
    • 84899974905 scopus 로고    scopus 로고
    • Functional assembly of camphor converting two-component Baeyer-Villiger monooxygenases with a flavin reductase from E. coli
    • doi: 10.1007/s00253-013-5338-3.
    • Kadow, M., Balke, K., Willetts, A., Bornscheuer, U. T., and Bäckvall, J. E. (2013). Functional assembly of camphor converting two-component Baeyer-Villiger monooxygenases with a flavin reductase from E. coli. Appl. Microbiol. Biotechnol. doi: 10.1007/s00253-013-5338-3
    • (2013) Appl. Microbiol. Biotechnol.
    • Kadow, M.1    Balke, K.2    Willetts, A.3    Bornscheuer, U.T.4    Bäckvall, J.E.5
  • 55
    • 84866485850 scopus 로고    scopus 로고
    • Completing the series of BVMOs involved in camphor metabolism of Pseudomonas putida NCIMB 10007 by identification of the two missing genes, their functional expression in E. coli, and biochemical characterization
    • doi: 10.1007/s00253-011-3859-1
    • Kadow, M., Loschinski, K., Sass, S., Schmidt, M., and Bornscheuer, U. T. (2012). Completing the series of BVMOs involved in camphor metabolism of Pseudomonas putida NCIMB 10007 by identification of the two missing genes, their functional expression in E. coli, and biochemical characterization. Appl. Microbiol. Biotechnol. 96, 419-429. doi: 10.1007/s00253-011-3859-1
    • (2012) Appl. Microbiol. Biotechnol. , vol.96 , pp. 419-429
    • Kadow, M.1    Loschinski, K.2    Sass, S.3    Schmidt, M.4    Bornscheuer, U.T.5
  • 56
    • 84877081893 scopus 로고    scopus 로고
    • Recombinant expression and purification of the 2,5-diketocamphane 1,2-monooxygenase from the camphor metabolizing Pseudomonas putida strain NCIMB 10007
    • doi: 10.1186/2191-0855-1-13
    • Kadow, M., Sass, S., Schmidt, M., and Bornscheuer, U. T. (2011). Recombinant expression and purification of the 2,5-diketocamphane 1,2-monooxygenase from the camphor metabolizing Pseudomonas putida strain NCIMB 10007. AMB Exp. 1, 13. doi: 10.1186/2191-0855-1-13
    • (2011) AMB Exp. , vol.1 , pp. 13
    • Kadow, M.1    Sass, S.2    Schmidt, M.3    Bornscheuer, U.T.4
  • 57
    • 0034857466 scopus 로고    scopus 로고
    • 4-Hydroxyacetophenone monooxygenase from Pseudomonas fluorescens ACB. A novel flavoprotein catalyzing Baeyer-Villiger oxidation of aromatic compounds
    • doi: 10.1046/j.1432-1327.2001.02137.x
    • Kamerbeek, N. M., Moonen, M. J., van der Ven, J. G., van Berkel, W. J., Fraaije, M. W., and Janssen, D. B. (2001). 4-Hydroxyacetophenone monooxygenase from Pseudomonas fluorescens ACB. A novel flavoprotein catalyzing Baeyer-Villiger oxidation of aromatic compounds. Eur. J. Biochem. 268, 2547-2557. doi: 10.1046/j.1432-1327.2001.02137.x
    • (2001) Eur. J. Biochem. , vol.268 , pp. 2547-2557
    • Kamerbeek, N.M.1    Moonen, M.J.2    van der Ven, J.G.3    van Berkel, W.J.4    Fraaije, M.W.5    Janssen, D.B.6
  • 58
    • 39649122805 scopus 로고    scopus 로고
    • Molecular cloning and functional characterization of the genes encoding benzoate and p-hydroxybenzoate degradation by the halophilic Chromohalobacter sp. strain HS-2
    • doi: 10.1111/j.1574-6968.2008.01067.x
    • Kim, D., Kim, S. W., Choi, K. Y., Lee, J. S., and Kim, E. (2008). Molecular cloning and functional characterization of the genes encoding benzoate and p-hydroxybenzoate degradation by the halophilic Chromohalobacter sp. strain HS-2. FEMS Microbiol. Lett. 280, 235-241. doi: 10.1111/j.1574-6968.2008.01067.x
    • (2008) FEMS Microbiol. Lett. , vol.280 , pp. 235-241
    • Kim, D.1    Kim, S.W.2    Choi, K.Y.3    Lee, J.S.4    Kim, E.5
  • 59
    • 84865750538 scopus 로고    scopus 로고
    • Expression and bioconversion of recombinant m-and p-hydroxybenzoate hydroxylases from a novel moderate halophile, Chromohalobacter sp
    • doi: 10.1007/s10529-012-0950-3
    • Kim, W., Park, Y. R., Im, S., Kim, D., and Kim, S. W. (2012). Expression and bioconversion of recombinant m-and p-hydroxybenzoate hydroxylases from a novel moderate halophile, Chromohalobacter sp. Biotechnol. Lett. 34, 1687-1692. doi: 10.1007/s10529-012-0950-3
    • (2012) Biotechnol. Lett. , vol.34 , pp. 1687-1692
    • Kim, W.1    Park, Y.R.2    Im, S.3    Kim, D.4    Kim, S.W.5
  • 60
    • 0031862051 scopus 로고    scopus 로고
    • Novel biological process for L-DOPA production from L-tyrosine by P-hydroxyphenylacetate 3-hydroxylase
    • doi: 10.1023/A:1005440229420
    • Lee, J. Y., and Xun, L. (1998). Novel biological process for L-DOPA production from L-tyrosine by P-hydroxyphenylacetate 3-hydroxylase. Biotechnol. Lett. 20, 479-482. doi: 10.1023/A:1005440229420
    • (1998) Biotechnol. Lett. , vol.20 , pp. 479-482
    • Lee, J.Y.1    Xun, L.2
  • 61
    • 84874378034 scopus 로고    scopus 로고
    • Effects of NADH kinase on NADPH-dependent biotransformation processes in Escherichia coli
    • doi: 10.1007/s00253-012-4431-3
    • Lee, W.-H., Kim, J.-W., Park, E.-H., Han, N. S., Kim, M.-D., and Seo, J.-H. (2013). Effects of NADH kinase on NADPH-dependent biotransformation processes in Escherichia coli. Appl. Microbiol. Biotechnol. 97, 1561-1569. doi: 10.1007/s00253-012-4431-3
    • (2013) Appl. Microbiol. Biotechnol. , vol.97 , pp. 1561-1569
    • Lee, W.-H.1    Kim, J.-W.2    Park, E.-H.3    Han, N.S.4    Kim, M.-D.5    Seo, J.-H.6
  • 62
    • 34547114478 scopus 로고    scopus 로고
    • Enhanced production of epsilon-caprolactone by overexpression of NADPH-regenerating glucose 6-phosphate dehydrogenase in recombinant Escherichia coli harboring cyclohexanone monooxygenase gene
    • doi: 10.1007/s00253-007-1016-7
    • Lee, W. H., Park, J. B., Park, K., Kim, M. D., and Seo, J. H. (2007). Enhanced production of epsilon-caprolactone by overexpression of NADPH-regenerating glucose 6-phosphate dehydrogenase in recombinant Escherichia coli harboring cyclohexanone monooxygenase gene. Appl. Microbiol. Biotechnol. 76, 329-338. doi: 10.1007/s00253-007-1016-7
    • (2007) Appl. Microbiol. Biotechnol. , vol.76 , pp. 329-338
    • Lee, W.H.1    Park, J.B.2    Park, K.3    Kim, M.D.4    Seo, J.H.5
  • 63
    • 84890012234 scopus 로고    scopus 로고
    • The steroid monooxygenase from Rhodococcus rhodochrous; a versatile biocatalyst
    • doi: 10.1016/j.tetasy.2013.11.003
    • Leipold, F., Rudroff, F., Mihovilovic, M. D., and Bornscheuer, U. T. (2013). The steroid monooxygenase from Rhodococcus rhodochrous; a versatile biocatalyst. Tetrahedron 24, 1620-1624. doi: 10.1016/j.tetasy.2013.11.003
    • (2013) Tetrahedron , vol.24 , pp. 1620-1624
    • Leipold, F.1    Rudroff, F.2    Mihovilovic, M.D.3    Bornscheuer, U.T.4
  • 64
    • 84862692238 scopus 로고    scopus 로고
    • Cloning, expression and characterization of a eukaryotic cycloalkanone monooxygenase from Cylindrocarpon radicicola ATCC 11011
    • doi: 10.1007/s00253-011-3670-z
    • Leipold, F., Wardenga, R., and Bornscheuer, U. T. (2012). Cloning, expression and characterization of a eukaryotic cycloalkanone monooxygenase from Cylindrocarpon radicicola ATCC 11011. Appl. Microbiol. Biotechnol. 94, 705-717. doi: 10.1007/s00253-011-3670-z
    • (2012) Appl. Microbiol. Biotechnol. , vol.94 , pp. 705-717
    • Leipold, F.1    Wardenga, R.2    Bornscheuer, U.T.3
  • 65
    • 79960605776 scopus 로고    scopus 로고
    • Baeyer-Villiger monooxygenases: more than just green chemistry
    • doi: 10.1021/cr1003437
    • Leisch, H., Morley, K., and Lau, P. C. (2011). Baeyer-Villiger monooxygenases: more than just green chemistry. Chem. Rev. 111, 4165-4222. doi: 10.1021/cr1003437
    • (2011) Chem. Rev. , vol.111 , pp. 4165-4222
    • Leisch, H.1    Morley, K.2    Lau, P.C.3
  • 66
    • 84860861683 scopus 로고    scopus 로고
    • Cloning, Baeyer-Villiger biooxidations, and structures of the camphor pathway 2-oxo-Delta(3)-4,5,5-trimethylcyclopentenylacetyl-coenzyme A monooxygenase of Pseudomonas putida ATCC 17453
    • doi: 10.1128/AEM.07694-11
    • Leisch, H., Shi, R., Grosse, S., Morley, K., Bergeron, H., Cygler, M., et al. (2012). Cloning, Baeyer-Villiger biooxidations, and structures of the camphor pathway 2-oxo-Delta(3)-4,5,5-trimethylcyclopentenylacetyl-coenzyme A monooxygenase of Pseudomonas putida ATCC 17453. Appl. Environ. Microbiol. 78, 2200-2212. doi: 10.1128/AEM.07694-11
    • (2012) Appl. Environ. Microbiol. , vol.78 , pp. 2200-2212
    • Leisch, H.1    Shi, R.2    Grosse, S.3    Morley, K.4    Bergeron, H.5    Cygler, M.6
  • 67
    • 79952486403 scopus 로고    scopus 로고
    • Asymmetric epoxidation of styrene derivatives by styrene monooxygenase from Pseudomonas sp. LQ26 effects of α-and β-substituents
    • doi: 10.1016/j.tetasy.2010.12.022
    • Lin, H., Liu, Y., and Wu, Z. L. (2011a). Asymmetric epoxidation of styrene derivatives by styrene monooxygenase from Pseudomonas sp. LQ26 effects of α-and β-substituents. Tetrahedron 22, 134-137. doi: 10.1016/j.tetasy.2010.12.022
    • (2011) Tetrahedron , vol.22 , pp. 134-137
    • Lin, H.1    Liu, Y.2    Wu, Z.L.3
  • 68
    • 79952267013 scopus 로고    scopus 로고
    • Highly diastereo-and enantio-selective epoxidation of secondary allylic alcohols catalyzed by styrene monooxygenase
    • doi: 10.1039/c0cc04360e
    • Lin, H., Liu, Y., and Wu, Z. L. (2011b). Highly diastereo-and enantio-selective epoxidation of secondary allylic alcohols catalyzed by styrene monooxygenase. Chem. Commun. 47, 2610-2612. doi: 10.1039/c0cc04360e
    • (2011) Chem. Commun. , vol.47 , pp. 2610-2612
    • Lin, H.1    Liu, Y.2    Wu, Z.L.3
  • 69
    • 78049314530 scopus 로고    scopus 로고
    • Styrene monooxygenase from Pseudomonas sp. LQ26 catalyzes the asymmetric epoxidation of both conjugated and unconjugated alkenes
    • doi: 10.1016/j.molcatb.2010.08.012
    • Lin, H., Qiao, J., Liu, Y., and Wu, Z. L. (2010). Styrene monooxygenase from Pseudomonas sp. LQ26 catalyzes the asymmetric epoxidation of both conjugated and unconjugated alkenes. J. Mol. Catal. B Enzym. 67, 236-241. doi: 10.1016/j.molcatb.2010.08.012
    • (2010) J. Mol. Catal. B Enzym. , vol.67 , pp. 236-241
    • Lin, H.1    Qiao, J.2    Liu, Y.3    Wu, Z.L.4
  • 70
    • 84864567619 scopus 로고    scopus 로고
    • Mutations at the putative active cavity of styrene monooxygenase: enhanced activity and reversed enantioselectivity
    • doi: 10.1016/j.jbiotec.2012.06.028
    • Lin, H., Tang, D. F., Ahmed, A. A., Liu, Y., and Wu, Z. L. (2012). Mutations at the putative active cavity of styrene monooxygenase: enhanced activity and reversed enantioselectivity. J. Biotechnol. 161, 235-241. doi: 10.1016/j.jbiotec.2012.06.028
    • (2012) J. Biotechnol. , vol.161 , pp. 235-241
    • Lin, H.1    Tang, D.F.2    Ahmed, A.A.3    Liu, Y.4    Wu, Z.L.5
  • 71
    • 4444307667 scopus 로고    scopus 로고
    • Crystal structure of a Baeyer-Villiger monooxygenase
    • doi: 10.1073/pnas.0404538101
    • Malito, E., Alfieri, A., Fraaije, M. W., and Mattevi, A. (2004). Crystal structure of a Baeyer-Villiger monooxygenase. Proc. Natl. Acad. Sci. U.S.A. 101, 13157-13162. doi: 10.1073/pnas.0404538101
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 13157-13162
    • Malito, E.1    Alfieri, A.2    Fraaije, M.W.3    Mattevi, A.4
  • 72
    • 84881227846 scopus 로고    scopus 로고
    • Cloning, overexpression and biocatalytic exploration of a novel Baeyer-Villiger monooxygenase from Aspergillus fumigatus Af293
    • doi: 10.1186/2191-0855-3-33
    • Mascotti, M. L., Juri Ayub, M., Dudek, H., Sanz, M. K., and Fraaije, M. W. (2013). Cloning, overexpression and biocatalytic exploration of a novel Baeyer-Villiger monooxygenase from Aspergillus fumigatus Af293. AMB Exp. 3, 33. doi: 10.1186/2191-0855-3-33
    • (2013) AMB Exp. , vol.3 , pp. 33
    • Mascotti, M.L.1    Juri Ayub, M.2    Dudek, H.3    Sanz, M.K.4    Fraaije, M.W.5
  • 73
    • 35448932511 scopus 로고    scopus 로고
    • Biochemical characterization of a flavin adenine dinucleotide-dependent monooxygenase, ornithine hydroxylase from Pseudomonas aeruginosa, suggests a novel reaction mechanism
    • doi: 10.1021/bi700932q
    • Meneely, K. M., and Lamb, A. L. (2007). Biochemical characterization of a flavin adenine dinucleotide-dependent monooxygenase, ornithine hydroxylase from Pseudomonas aeruginosa, suggests a novel reaction mechanism. Biochemistry 46, 11930-11937. doi: 10.1021/bi700932q
    • (2007) Biochemistry , vol.46 , pp. 11930-11937
    • Meneely, K.M.1    Lamb, A.L.2
  • 74
    • 33745743032 scopus 로고    scopus 로고
    • Enzyme mediated Baeyer-Villiger oxidations
    • doi: 10.2174/138527206777698002
    • Mihovilovic, M. D. (2006). Enzyme mediated Baeyer-Villiger oxidations. Curr. Org. Chem. 10, 1265-1287. doi: 10.2174/138527206777698002
    • (2006) Curr. Org. Chem. , vol.10 , pp. 1265-1287
    • Mihovilovic, M.D.1
  • 75
    • 33746393218 scopus 로고    scopus 로고
    • Accessing tetrahydrofuran-based natural products by microbial Baeyer-Villiger biooxidation
    • doi: 10.1039/b606633j.
    • Mihovilovic, M. D., Bianchi, D. A., and Rudroff, F. (2006). Accessing tetrahydrofuran-based natural products by microbial Baeyer-Villiger biooxidation. Chem. Commun. 3214-3216. doi: 10.1039/b606633j
    • (2006) Chem. Commun. , pp. 3214-3216
    • Mihovilovic, M.D.1    Bianchi, D.A.2    Rudroff, F.3
  • 76
    • 84867613558 scopus 로고    scopus 로고
    • Identification of a novel Baeyer-Villiger monooxygenase from Acinetobacter radioresistens: close relationship to the Mycobacterium tuberculosis prodrug activator EtaA
    • doi: 10.1111/j.1751-7915.2012.00356.x
    • Minerdi, D., Zgrablic, I., Sadeghi, S. J., and Gilardi, G. (2012). Identification of a novel Baeyer-Villiger monooxygenase from Acinetobacter radioresistens: close relationship to the Mycobacterium tuberculosis prodrug activator EtaA. Microb. Biotechnol. 5, 700-716. doi: 10.1111/j.1751-7915.2012.00356.x
    • (2012) Microb. Biotechnol. , vol.5 , pp. 700-716
    • Minerdi, D.1    Zgrablic, I.2    Sadeghi, S.J.3    Gilardi, G.4
  • 77
    • 84883693290 scopus 로고    scopus 로고
    • Crystal structure of 3-hydroxybenzoate 6-hydroxylase uncovers lipid-assisted flavoprotein strategy for regioselective aromatic hydroxylation
    • doi: 10.1074/jbc.M113.479303
    • Montersino, S., Orru, R., Barendregt, A., Westphal, A. H., van Duijn, E., Mattevi, A., et al. (2013). Crystal structure of 3-hydroxybenzoate 6-hydroxylase uncovers lipid-assisted flavoprotein strategy for regioselective aromatic hydroxylation. J. Biol. Chem. 288, 26235-26245. doi: 10.1074/jbc.M113.479303
    • (2013) J. Biol. Chem. , vol.288 , pp. 26235-26245
    • Montersino, S.1    Orru, R.2    Barendregt, A.3    Westphal, A.H.4    van Duijn, E.5    Mattevi, A.6
  • 78
    • 84856058506 scopus 로고    scopus 로고
    • Functional annotation and characterization of 3-hydroxybenzoate 6-hydroxylase from Rhodococcus jostii RHA1
    • doi: 10.1016/j.bbapap.2011.12.003
    • Montersino, S., and van Berkel, W. J. (2012). Functional annotation and characterization of 3-hydroxybenzoate 6-hydroxylase from Rhodococcus jostii RHA1. Biochim. Biophys. Acta 1824, 433-442. doi: 10.1016/j.bbapap.2011.12.003
    • (2012) Biochim. Biophys. Acta , vol.1824 , pp. 433-442
    • Montersino, S.1    van Berkel, W.J.2
  • 79
    • 84878016310 scopus 로고    scopus 로고
    • The oxidation of alkylaryl sulfides and benzo[b]thiophenes by Escherichia coli cells expressing wild-type and engineered styrene monooxygenase from Pseudomonas putida CA-3
    • doi: 10.1007/s00253-012-4332-5
    • Nikodinovic-Runic, J., Coulombel, L., Francuski, D., Sharma, N. D., Boyd, D. R., Ferrall, R. M., et al. (2013). The oxidation of alkylaryl sulfides and benzo[b]thiophenes by Escherichia coli cells expressing wild-type and engineered styrene monooxygenase from Pseudomonas putida CA-3. Appl. Microbiol. Biotechnol. 97, 4849-4858. doi: 10.1007/s00253-012-4332-5
    • (2013) Appl. Microbiol. Biotechnol. , vol.97 , pp. 4849-4858
    • Nikodinovic-Runic, J.1    Coulombel, L.2    Francuski, D.3    Sharma, N.D.4    Boyd, D.R.5    Ferrall, R.M.6
  • 80
    • 80052395555 scopus 로고    scopus 로고
    • Two structures of an N-hydroxylating flavoprotein monooxygenase: ornithine hydroxylase from Pseudomonas aeruginosa
    • doi: 10.1074/jbc.M111.265876
    • Olucha, J., Meneely, K. M., Chilton, A. S., and Lamb, A. L. (2011). Two structures of an N-hydroxylating flavoprotein monooxygenase: ornithine hydroxylase from Pseudomonas aeruginosa. J. Biol. Chem. 286, 31789-31798. doi: 10.1074/jbc.M111.265876
    • (2011) J. Biol. Chem. , vol.286 , pp. 31789-31798
    • Olucha, J.1    Meneely, K.M.2    Chilton, A.S.3    Lamb, A.L.4
  • 81
    • 78650008114 scopus 로고    scopus 로고
    • Towards practical Baeyer-Villiger-monooxygenases: design of cyclohexanone monooxygenase mutants with enhanced oxidative stability
    • doi: 10.1002/cbic.201000464
    • Opperman, D. J., and Reetz, M. T. (2010). Towards practical Baeyer-Villiger-monooxygenases: design of cyclohexanone monooxygenase mutants with enhanced oxidative stability. ChemBioChem 11, 2589-2596. doi: 10.1002/cbic.201000464
    • (2010) ChemBioChem , vol.11 , pp. 2589-2596
    • Opperman, D.J.1    Reetz, M.T.2
  • 82
    • 80051703580 scopus 로고    scopus 로고
    • Snapshots of enzymatic Baeyer-Villiger catalysis: oxygen activation and intermediate stabilization
    • doi: 10.1074/jbc.M111.255075
    • Orru, R., Dudek, H. M., Martinoli, C., Torres Pazmiño, D. E., Royant, A., Weik, M., et al. (2011). Snapshots of enzymatic Baeyer-Villiger catalysis: oxygen activation and intermediate stabilization. J. Biol. Chem. 286, 29284-29291. doi: 10.1074/jbc.M111.255075
    • (2011) J. Biol. Chem. , vol.286 , pp. 29284-29291
    • Orru, R.1    Dudek, H.M.2    Martinoli, C.3    Torres Pazmiño, D.E.4    Royant, A.5    Weik, M.6
  • 83
    • 0031745849 scopus 로고    scopus 로고
    • Towards a biocatalyst for (S)-styrene oxide production: characterization of the styrene degradation pathway of Pseudomonas sp. strain VLB120
    • Panke, S., Witholt, B., Schmid, A., and Wubbolts, M. G. (1998). Towards a biocatalyst for (S)-styrene oxide production: characterization of the styrene degradation pathway of Pseudomonas sp. strain VLB120. Appl. Environ. Microbiol. 64, 2032-2043.
    • (1998) Appl. Environ. Microbiol. , vol.64 , pp. 2032-2043
    • Panke, S.1    Witholt, B.2    Schmid, A.3    Wubbolts, M.G.4
  • 84
    • 34548233702 scopus 로고    scopus 로고
    • Molecular and biochemical characterization of 3-hydroxybenzoate 6-hydroxylase from Polaromonas naphthalenivorans CJ2
    • doi: 10.1128/AEM.00782-07
    • Park, M., Jeon, Y., Jang, H. H., Ro, H. S., Park, W., Madsen, E. L., et al. (2007). Molecular and biochemical characterization of 3-hydroxybenzoate 6-hydroxylase from Polaromonas naphthalenivorans CJ2. Appl. Environ. Microbiol. 73, 5146-5152. doi: 10.1128/AEM.00782-07
    • (2007) Appl. Environ. Microbiol. , vol.73 , pp. 5146-5152
    • Park, M.1    Jeon, Y.2    Jang, H.H.3    Ro, H.S.4    Park, W.5    Madsen, E.L.6
  • 85
    • 79951773298 scopus 로고    scopus 로고
    • Rational design of styrene monooxygenase mutants with altered substrate preference
    • doi: 10.1007/s10529-010-0472-9
    • Qaed, A. A., Lin, H., Tang, D. F., and Wu, Z. L. (2011). Rational design of styrene monooxygenase mutants with altered substrate preference. Biotechnol. Lett. 33, 611-616. doi: 10.1007/s10529-010-0472-9
    • (2011) Biotechnol. Lett. , vol.33 , pp. 611-616
    • Qaed, A.A.1    Lin, H.2    Tang, D.F.3    Wu, Z.L.4
  • 86
    • 70350292190 scopus 로고    scopus 로고
    • Laboratory evolution of robust and enantioselective Baeyer-Villiger monooxygenases for asymmetric catalysis
    • doi: 10.1021/ja906212k
    • Reetz, M. T., and Wu, S. (2009). Laboratory evolution of robust and enantioselective Baeyer-Villiger monooxygenases for asymmetric catalysis. J. Am. Chem. Soc. 131, 15424-15432. doi: 10.1021/ja906212k
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 15424-15432
    • Reetz, M.T.1    Wu, S.2
  • 87
    • 66249142686 scopus 로고    scopus 로고
    • Cloning, expression, characterization, and biocatalytic investigation of the 4-hydroxyacetophenone monooxygenase from Pseudomonas putida JD1
    • doi: 10.1128/AEM.02707-08
    • Rehdorf, J., Zimmer, C. L., and Bornscheuer, U. T. (2009). Cloning, expression, characterization, and biocatalytic investigation of the 4-hydroxyacetophenone monooxygenase from Pseudomonas putida JD1. Appl. Environ. Microbiol. 75, 3106-3114. doi: 10.1128/AEM.02707-08
    • (2009) Appl. Environ. Microbiol. , vol.75 , pp. 3106-3114
    • Rehdorf, J.1    Zimmer, C.L.2    Bornscheuer, U.T.3
  • 88
    • 53849090276 scopus 로고    scopus 로고
    • Stereoselective desymmetrizations by recombinant whole cells expressing the Baeyer-Villiger monooxygenase from Xanthobacter sp. ZL5: a new biocatalyst accepting structurally demanding substrates
    • doi: 10.1002/ejoc.200700872
    • Rial, D. V., Bianchi, D. A., Kapitanova, P., Lengar, A., van Beilen, J. B., and Mihovilovic, M. D. (2008a). Stereoselective desymmetrizations by recombinant whole cells expressing the Baeyer-Villiger monooxygenase from Xanthobacter sp. ZL5: a new biocatalyst accepting structurally demanding substrates. Eur. J. Org. Chem. 2008, 1203-1213. doi: 10.1002/ejoc.200700872
    • (2008) Eur. J. Org. Chem. , vol.2008 , pp. 1203-1213
    • Rial, D.V.1    Bianchi, D.A.2    Kapitanova, P.3    Lengar, A.4    van Beilen, J.B.5    Mihovilovic, M.D.6
  • 89
    • 36849043080 scopus 로고    scopus 로고
    • Biocatalyst assessment of recombinant whole-cells expressing the Baeyer-Villiger monooxygenase from Xanthobacter sp. ZL5
    • doi: 10.1016/j.molcatb.2007.09.001
    • Rial, D. V., Cernuchova, P., van Beilen, J. B., and Mihovilovic, M. D. (2008b). Biocatalyst assessment of recombinant whole-cells expressing the Baeyer-Villiger monooxygenase from Xanthobacter sp. ZL5. J. Mol. Catal. B Enzym. 50, 61-68. doi: 10.1016/j.molcatb.2007.09.001
    • (2008) J. Mol. Catal. B Enzym. , vol.50 , pp. 61-68
    • Rial, D.V.1    Cernuchova, P.2    van Beilen, J.B.3    Mihovilovic, M.D.4
  • 90
    • 84871026016 scopus 로고    scopus 로고
    • Expanding the biocatalytic toolbox of flavoprotein monooxygenases from Rhodococcus jostii RHA1
    • doi: 10.1016/j.molcatb.2012.11.009
    • Riebel, A., de Gonzalo, G., and Fraaije, M. W. (2013a). Expanding the biocatalytic toolbox of flavoprotein monooxygenases from Rhodococcus jostii RHA1. J. Mol. Catal. B Enzym. 88, 20-25. doi: 10.1016/j.molcatb.2012.11.009
    • (2013) J. Mol. Catal. B Enzym. , vol.88 , pp. 20-25
    • Riebel, A.1    de Gonzalo, G.2    Fraaije, M.W.3
  • 91
    • 84897654772 scopus 로고    scopus 로고
    • Type II flavin-containing monooxygenases: a new class of biocatalysts that harbors Baeyer-Villiger monooxygenases with a relaxed coenzyme specificity
    • doi: 10.1002/cctc.201300550.
    • Riebel, A., Fink, M. J., Mihovilovic, M. D., and Fraaije, M. W. (2013b). Type II flavin-containing monooxygenases: a new class of biocatalysts that harbors Baeyer-Villiger monooxygenases with a relaxed coenzyme specificity. ChemCatChem. doi: 10.1002/cctc.201300550
    • (2013) ChemCatChem
    • Riebel, A.1    Fink, M.J.2    Mihovilovic, M.D.3    Fraaije, M.W.4
  • 92
    • 84872036176 scopus 로고    scopus 로고
    • Expanding the set of rhodococcal Baeyer-Villiger monooxygenases by high-throughput cloning, expression and substrate screening
    • doi: 10.1007/s00253-011-3823-0
    • Riebel, A., Dudek, H. M., de Gonzalo, G., Stepniak, P., Rychlewski, L., and Fraaije, M. W. (2012). Expanding the set of rhodococcal Baeyer-Villiger monooxygenases by high-throughput cloning, expression and substrate screening. Appl. Microbiol. Biotechnol. 95, 1479-1489. doi: 10.1007/s00253-011-3823-0
    • (2012) Appl. Microbiol. Biotechnol. , vol.95 , pp. 1479-1489
    • Riebel, A.1    Dudek, H.M.2    de Gonzalo, G.3    Stepniak, P.4    Rychlewski, L.5    Fraaije, M.W.6
  • 93
    • 66149089180 scopus 로고    scopus 로고
    • Enzymatic Baeyer-Villiger oxidation of benzo-fused ketones: formation of regiocomplementary lactones
    • doi: 10.1002/ejoc.200900084
    • Rioz-Martínez, A., de Gonzalo, G., Torres Pazmiño, D. E., Fraaije, M. W., and Gotor, V. (2009). Enzymatic Baeyer-Villiger oxidation of benzo-fused ketones: formation of regiocomplementary lactones. Eur. J. Org. Chem. 2009, 2526-2532. doi: 10.1002/ejoc.200900084
    • (2009) Eur. J. Org. Chem. , vol.2009 , pp. 2526-2532
    • Rioz-Martínez, A.1    de Gonzalo, G.2    Torres Pazmiño, D.E.3    Fraaije, M.W.4    Gotor, V.5
  • 94
    • 78649284752 scopus 로고    scopus 로고
    • Enzymatic synthesis of novel chiral sulfoxides employing Baeyer-Villiger monooxygenases
    • doi: 10.1002/ejoc.201000890
    • Rioz-Martínez, A., de Gonzalo, G., Torres Pazmiño, D. E., Fraaije, M. W., and Gotor, V. (2010a). Enzymatic synthesis of novel chiral sulfoxides employing Baeyer-Villiger monooxygenases. Eur. J. Org. Chem. 2010, 6409-6416. doi: 10.1002/ejoc.201000890
    • (2010) Eur. J. Org. Chem. , vol.2010 , pp. 6409-6416
    • Rioz-Martínez, A.1    de Gonzalo, G.2    Torres Pazmiño, D.E.3    Fraaije, M.W.4    Gotor, V.5
  • 95
    • 77949806555 scopus 로고    scopus 로고
    • Synthesis of chiral 3-alkyl-3,4-dihydroisocoumarins by dynamic kinetic resolutions catalyzed by a Baeyer-Villiger monooxygenase
    • doi: 10.1021/jo902519j
    • Rioz-Martínez, A., de Gonzalo, G., Torres Pazmiño, D. E., Fraaije, M. W., and Gotor, V. (2010b). Synthesis of chiral 3-alkyl-3,4-dihydroisocoumarins by dynamic kinetic resolutions catalyzed by a Baeyer-Villiger monooxygenase. J. Org. Chem. 75, 2073-2076. doi: 10.1021/jo902519j
    • (2010) J. Org. Chem. , vol.75 , pp. 2073-2076
    • Rioz-Martínez, A.1    de Gonzalo, G.2    Torres Pazmiño, D.E.3    Fraaije, M.W.4    Gotor, V.5
  • 97
    • 34447092984 scopus 로고    scopus 로고
    • Enzymatic kinetic resolution of racemic ketones catalyzed by Baeyer-Villiger monooxygenases
    • doi: 10.1016/j.tetasy.2007.05.033
    • Rodríguez, C., de Gonzalo, G., Fraaije, M. W., and Gotor, V. (2007). Enzymatic kinetic resolution of racemic ketones catalyzed by Baeyer-Villiger monooxygenases. Tetrahedron 18, 1338-1344. doi: 10.1016/j.tetasy.2007.05.033
    • (2007) Tetrahedron , vol.18 , pp. 1338-1344
    • Rodríguez, C.1    de Gonzalo, G.2    Fraaije, M.W.3    Gotor, V.4
  • 98
    • 80054905200 scopus 로고    scopus 로고
    • Optimization of oxidative bioconversions catalyzed by phenylacetone monooxygenase from Thermobifida fusca
    • doi: 10.1016/j.molcatb.2011.09.010
    • Rodríguez, C., de Gonzalo, G., and Gotor, V. (2012). Optimization of oxidative bioconversions catalyzed by phenylacetone monooxygenase from Thermobifida fusca. J. Mol. Catal. B Enzym. 74, 138-143. doi: 10.1016/j.molcatb.2011.09.010
    • (2012) J. Mol. Catal. B Enzym. , vol.74 , pp. 138-143
    • Rodríguez, C.1    de Gonzalo, G.2    Gotor, V.3
  • 99
    • 38749106942 scopus 로고    scopus 로고
    • Selective Baeyer-Villiger oxidation of racemic ketones in aqueous-organic media catalyzed by phenylacetone monooxygenase
    • doi: 10.1016/j.tetasy.2007.12.008
    • Rodríguez, C., de Gonzalo, G., Torres Pazmiño, D. E., Fraaije, M. W., and Gotor, V. (2008). Selective Baeyer-Villiger oxidation of racemic ketones in aqueous-organic media catalyzed by phenylacetone monooxygenase. Tetrahedron 19, 197-203. doi: 10.1016/j.tetasy.2007.12.008
    • (2008) Tetrahedron , vol.19 , pp. 197-203
    • Rodríguez, C.1    de Gonzalo, G.2    Torres Pazmiño, D.E.3    Fraaije, M.W.4    Gotor, V.5
  • 100
    • 84880244734 scopus 로고    scopus 로고
    • Conserved and non-conserved residues and their role in the structure and function of p-hydroxybenzoate hydroxylase
    • doi: 10.1093/protein/gzt026
    • Suemori, A. (2013). Conserved and non-conserved residues and their role in the structure and function of p-hydroxybenzoate hydroxylase. Protein Eng. Des. Sel. 26, 479-488. doi: 10.1093/protein/gzt026
    • (2013) Protein Eng. Des. Sel. , vol.26 , pp. 479-488
    • Suemori, A.1
  • 101
    • 34547118607 scopus 로고    scopus 로고
    • A systematic and comprehensive combinatorial approach to simultaneously improve the activity, reaction specificity, and thermal stability of p-hydroxybenzoate hydroxylase
    • doi: 10.1074/jbc.M610320200
    • Suemori, A., and Iwakura, M. (2007). A systematic and comprehensive combinatorial approach to simultaneously improve the activity, reaction specificity, and thermal stability of p-hydroxybenzoate hydroxylase. J. Biol. Chem. 282, 19969-19978. doi: 10.1074/jbc.M610320200
    • (2007) J. Biol. Chem. , vol.282 , pp. 19969-19978
    • Suemori, A.1    Iwakura, M.2
  • 102
    • 67650498684 scopus 로고    scopus 로고
    • Insights into sequence-activity relationships amongst Baeyer-Villiger monooxygenases as revealed by the intragenomic complement of enzymes from Rhodococcus jostii RHA1
    • doi: 10.1002/cbic.200900011
    • Szolkowy, C., Eltis, L. D., Bruce, N. C., and Grogan, G. (2009). Insights into sequence-activity relationships amongst Baeyer-Villiger monooxygenases as revealed by the intragenomic complement of enzymes from Rhodococcus jostii RHA1. ChemBioChem 10, 1208-1217. doi: 10.1002/cbic.200900011
    • (2009) ChemBioChem , vol.10 , pp. 1208-1217
    • Szolkowy, C.1    Eltis, L.D.2    Bruce, N.C.3    Grogan, G.4
  • 103
    • 4644255461 scopus 로고    scopus 로고
    • Cloning and expression of p-hydroxyphenylacetate 3-hydroxylase from Acinetobacter baumannii: evidence of the divergence of enzymes in the class of two-protein component aromatic hydroxylases
    • doi: 10.1016/j.bbaexp.2004.08.003
    • Thotsaporn, K., Sucharitakul, J., Wongratana, J., Suadee, C., and Chaiyen, P. (2004). Cloning and expression of p-hydroxyphenylacetate 3-hydroxylase from Acinetobacter baumannii: evidence of the divergence of enzymes in the class of two-protein component aromatic hydroxylases. Biochim. Biophys. Acta 1680, 60-66. doi: 10.1016/j.bbaexp.2004.08.003
    • (2004) Biochim. Biophys. Acta , vol.1680 , pp. 60-66
    • Thotsaporn, K.1    Sucharitakul, J.2    Wongratana, J.3    Suadee, C.4    Chaiyen, P.5
  • 104
    • 67749139572 scopus 로고    scopus 로고
    • Identification of a novel self-sufficient styrene monooxygenase from Rhodococcus opacus 1CP
    • doi: 10.1128/JB.00307-09
    • Tischler, D., Eulberg, D., Lakner, S., Kaschabek, S. R., van Berkel, W. J., and Schlomann, M. (2009). Identification of a novel self-sufficient styrene monooxygenase from Rhodococcus opacus 1CP. J. Bacteriol. 191, 4996-5009. doi: 10.1128/JB.00307-09
    • (2009) J. Bacteriol. , vol.191 , pp. 4996-5009
    • Tischler, D.1    Eulberg, D.2    Lakner, S.3    Kaschabek, S.R.4    van Berkel, W.J.5    Schlomann, M.6
  • 105
    • 77957365781 scopus 로고    scopus 로고
    • StyA1 and StyA2B from Rhodococcus opacus 1CP: a multifunctional styrene monooxygenase system
    • doi: 10.1128/JB.00723-10
    • Tischler, D., Kermer, R., Groning, J. A., Kaschabek, S. R., van Berkel, W. J., and Schlomann, M. (2010). StyA1 and StyA2B from Rhodococcus opacus 1CP: a multifunctional styrene monooxygenase system. J. Bacteriol. 192, 5220-5227. doi: 10.1128/JB.00723-10
    • (2010) J. Bacteriol. , vol.192 , pp. 5220-5227
    • Tischler, D.1    Kermer, R.2    Groning, J.A.3    Kaschabek, S.R.4    van Berkel, W.J.5    Schlomann, M.6
  • 106
    • 41449109033 scopus 로고    scopus 로고
    • Kinetic mechanism of phenylacetone monooxygenase from Thermobifida fusca
    • doi: 10.1021/bi702296k
    • Torres Pazmiño, D. E., Baas, B. J., Janssen, D. B., and Fraaije, M. W. (2008a). Kinetic mechanism of phenylacetone monooxygenase from Thermobifida fusca. Biochemistry 47, 4082-4093. doi: 10.1021/bi702296k
    • (2008) Biochemistry , vol.47 , pp. 4082-4093
    • Torres Pazmiño, D.E.1    Baas, B.J.2    Janssen, D.B.3    Fraaije, M.W.4
  • 107
    • 41049111588 scopus 로고    scopus 로고
    • Self-sufficient Baeyer-Villiger monooxygenases: effective coenzyme regeneration for biooxygenation by fusion engineering
    • doi: 10.1002/anie.200704630
    • Torres Pazmiño, D. E., Snajdrova, R., Baas, B. J., Ghobrial, M., Mihovilovic, M. D., and Fraaije, M. W. (2008b). Self-sufficient Baeyer-Villiger monooxygenases: effective coenzyme regeneration for biooxygenation by fusion engineering. Angew. Chem. Int. Ed Engl. 47, 2275-2278. doi: 10.1002/anie.200704630
    • (2008) Angew. Chem. Int. Ed Engl. , vol.47 , pp. 2275-2278
    • Torres Pazmiño, D.E.1    Snajdrova, R.2    Baas, B.J.3    Ghobrial, M.4    Mihovilovic, M.D.5    Fraaije, M.W.6
  • 108
    • 77949897676 scopus 로고    scopus 로고
    • Baeyer-Villiger monooxygenases: recent advances and future challenges
    • doi: 10.1016/j.cbpa.2009.11.017
    • Torres Pazmiño, D. E., Dudek, H. M., and Fraaije, M. W. (2010a). Baeyer-Villiger monooxygenases: recent advances and future challenges. Curr. Opin. Chem. Biol. 14, 138-144. doi: 10.1016/j.cbpa.2009.11.017
    • (2010) Curr. Opin. Chem. Biol. , vol.14 , pp. 138-144
    • Torres Pazmiño, D.E.1    Dudek, H.M.2    Fraaije, M.W.3
  • 109
    • 77349127553 scopus 로고    scopus 로고
    • Monooxygenases as biocatalysts: classification, mechanistic aspects and biotechnological applications
    • doi: 10.1016/j.jbiotec.2010.01.021
    • Torres Pazmiño, D. E., Winkler, M., Glieder, A., and Fraaije, M. W. (2010b). Monooxygenases as biocatalysts: classification, mechanistic aspects and biotechnological applications. J. Biotechnol. 146, 9-24. doi: 10.1016/j.jbiotec.2010.01.021
    • (2010) J. Biotechnol. , vol.146 , pp. 9-24
    • Torres Pazmiño, D.E.1    Winkler, M.2    Glieder, A.3    Fraaije, M.W.4
  • 110
    • 71049192404 scopus 로고    scopus 로고
    • Efficient biooxidations catalyzed by a new generation of self-sufficient Baeyer-Villiger monooxygenases
    • doi: 10.1002/cbic.200900480
    • Torres Pazmiño, D. E., Riebel, A., de Lange, J., Rudroff, F., Mihovilovic, M. D., and Fraaije, M. W. (2009). Efficient biooxidations catalyzed by a new generation of self-sufficient Baeyer-Villiger monooxygenases. ChemBioChem 10, 2595-2598. doi: 10.1002/cbic.200900480
    • (2009) ChemBioChem , vol.10 , pp. 2595-2598
    • Torres Pazmiño, D.E.1    Riebel, A.2    de Lange, J.3    Rudroff, F.4    Mihovilovic, M.D.5    Fraaije, M.W.6
  • 111
    • 34547170108 scopus 로고    scopus 로고
    • Altering the substrate specificity and enantioselectivity of phenylacetone monooxygenase by structure-inspired enzyme redesign
    • doi: 10.1002/adsc.200700045
    • Torres Pazmiño, D. E., Snajdrova, R., Rial, D. V., Mihovilovic, M. D., and Fraaije, M. W. (2007). Altering the substrate specificity and enantioselectivity of phenylacetone monooxygenase by structure-inspired enzyme redesign. Adv. Synth. Catal. 349, 1361-1368. doi: 10.1002/adsc.200700045
    • (2007) Adv. Synth. Catal. , vol.349 , pp. 1361-1368
    • Torres Pazmiño, D.E.1    Snajdrova, R.2    Rial, D.V.3    Mihovilovic, M.D.4    Fraaije, M.W.5
  • 112
    • 77749252741 scopus 로고    scopus 로고
    • Structure and ligand binding properties of the epoxidase component of styrene monooxygenase
    • doi: 10.1021/bi901693u
    • Ukaegbu, U. E., Kantz, A., Beaton, M., Gassner, G. T., and Rosenzweig, A. C. (2010). Structure and ligand binding properties of the epoxidase component of styrene monooxygenase. Biochemistry 49, 1678-1688. doi: 10.1021/bi901693u
    • (2010) Biochemistry , vol.49 , pp. 1678-1688
    • Ukaegbu, U.E.1    Kantz, A.2    Beaton, M.3    Gassner, G.T.4    Rosenzweig, A.C.5
  • 113
    • 33745991798 scopus 로고    scopus 로고
    • Flavoprotein monooxygenases, a diverse class of oxidative biocatalysts
    • doi: 10.1016/j.jbiotec.2006.03.044
    • van Berkel, W. J., Kamerbeek, N. M., and Fraaije, M. W. (2006). Flavoprotein monooxygenases, a diverse class of oxidative biocatalysts. J. Biotechnol. 124, 670-689. doi: 10.1016/j.jbiotec.2006.03.044
    • (2006) J. Biotechnol. , vol.124 , pp. 670-689
    • van Berkel, W.J.1    Kamerbeek, N.M.2    Fraaije, M.W.3
  • 114
    • 0026457258 scopus 로고
    • Substitution of Arg214 at the substrate-binding site of p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens
    • doi: 10.1111/j.1432-1033.1992.tb17436.x
    • van Berkel, W., Westphal, A., Eschrich, K., Eppink, M., and de Kok, A. (1992). Substitution of Arg214 at the substrate-binding site of p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens. Eur. J. Biochem. 210, 411-419. doi: 10.1111/j.1432-1033.1992.tb17436.x
    • (1992) Eur. J. Biochem. , vol.210 , pp. 411-419
    • van Berkel, W.1    Westphal, A.2    Eschrich, K.3    Eppink, M.4    de Kok, A.5
  • 115
    • 84862505690 scopus 로고    scopus 로고
    • A stepwise approach for the reproducible optimization of PAMO expression in Escherichia coli for whole-cell biocatalysis
    • doi: 10.1186/1472-6750-12-31
    • van Bloois, E., Dudek, H. M., Duetz, W. A., and Fraaije, M. W. (2012). A stepwise approach for the reproducible optimization of PAMO expression in Escherichia coli for whole-cell biocatalysis. BMC Biotechnol. 12:31. doi: 10.1186/1472-6750-12-31
    • (2012) BMC Biotechnol. , vol.12 , pp. 31
    • van Bloois, E.1    Dudek, H.M.2    Duetz, W.A.3    Fraaije, M.W.4
  • 116
    • 34648825060 scopus 로고    scopus 로고
    • Discovery of a novel styrene monooxygenase originating from the metagenome
    • doi: 10.1128/AEM.02708-06
    • van Hellemond, E. W., Janssen, D. B., and Fraaije, M. W. (2007). Discovery of a novel styrene monooxygenase originating from the metagenome. Appl. Environ. Microbiol. 73, 5832-5839. doi: 10.1128/AEM.02708-06
    • (2007) Appl. Environ. Microbiol. , vol.73 , pp. 5832-5839
    • van Hellemond, E.W.1    Janssen, D.B.2    Fraaije, M.W.3
  • 117
    • 84990161999 scopus 로고
    • Enzymic Baeyer-Villiger oxidations by flavin-dependent monooxygenases
    • doi: 10.1002/anie.198803331
    • Walsh, C. T., and Chen, Y. C. J. (1988). Enzymic Baeyer-Villiger oxidations by flavin-dependent monooxygenases. Angew. Chem. Int. Ed Engl. 27, 333-343. doi: 10.1002/anie.198803331
    • (1988) Angew. Chem. Int. Ed Engl. , vol.27 , pp. 333-343
    • Walsh, C.T.1    Chen, Y.C.J.2
  • 118
    • 0036010274 scopus 로고    scopus 로고
    • An efficient enzymatic Baeyer-Villiger oxidation by engineered Escherichia coli cells under non-growing conditions
    • doi: 10.1021/bp010177c
    • Walton, A. Z., and Stewart, J. D. (2002). An efficient enzymatic Baeyer-Villiger oxidation by engineered Escherichia coli cells under non-growing conditions. Biotechnol. Prog. 18, 262-268. doi: 10.1021/bp010177c
    • (2002) Biotechnol. Prog. , vol.18 , pp. 262-268
    • Walton, A.Z.1    Stewart, J.D.2
  • 119
    • 84892831820 scopus 로고    scopus 로고
    • Improvement of NADPH bioavailability in Escherichia coli by replacing NAD+-dependent glyceraldehyde-3-phosphate dehydrogenase GapA with NADP+-dependent GapB from Bacillus subtilis and addition of NAD kinase
    • doi: 10.1007/s10295-013-1335-x
    • Wang, Y., San, K.-Y., and Bennett, G. N. (2013). Improvement of NADPH bioavailability in Escherichia coli by replacing NAD+-dependent glyceraldehyde-3-phosphate dehydrogenase GapA with NADP+-dependent GapB from Bacillus subtilis and addition of NAD kinase. J. Ind. Microbiol. Biotechnol. 40, 1449-1460. doi: 10.1007/s10295-013-1335-x
    • (2013) J. Ind. Microbiol. Biotechnol. , vol.40 , pp. 1449-1460
    • Wang, Y.1    San, K.-Y.2    Bennett, G.N.3
  • 120
    • 84879368654 scopus 로고    scopus 로고
    • Permanent draft genome sequence of Comamonas testosteroni KF-1
    • doi: 10.4056/sigs.387890
    • Weiss, M., Kesberg, A. I., Labutti, K. M., Pitluck, S., Bruce, D., Hauser, L., et al. (2013). Permanent draft genome sequence of Comamonas testosteroni KF-1. Stand. Genomic Sci. 8, 239-254. doi: 10.4056/sigs.387890
    • (2013) Stand. Genomic Sci. , vol.8 , pp. 239-254
    • Weiss, M.1    Kesberg, A.I.2    Labutti, K.M.3    Pitluck, S.4    Bruce, D.5    Hauser, L.6
  • 121
    • 0031081656 scopus 로고    scopus 로고
    • Structural studies and synthetic applications of Baeyer-Villiger monooxygenases
    • doi: 10.1016/S0167-7799(97)84204-7
    • Willetts, A. (1997). Structural studies and synthetic applications of Baeyer-Villiger monooxygenases. Trends Biotechnol. 15, 55-62. doi: 10.1016/S0167-7799(97)84204-7
    • (1997) Trends Biotechnol. , vol.15 , pp. 55-62
    • Willetts, A.1
  • 122
    • 77649260900 scopus 로고    scopus 로고
    • Induced allostery in the directed evolution of an enantioselective Baeyer-Villiger monooxygenase
    • doi: 10.1073/pnas.0911656107
    • Wu, S., Acevedo, J. P., and Reetz, M. T. (2010). Induced allostery in the directed evolution of an enantioselective Baeyer-Villiger monooxygenase. Proc. Natl. Acad. Sci. U.S.A. 107, 2775-2780. doi: 10.1073/pnas.0911656107
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 2775-2780
    • Wu, S.1    Acevedo, J.P.2    Reetz, M.T.3
  • 123
    • 84860849697 scopus 로고    scopus 로고
    • The substrate-bound crystal structure of a Baeyer-Villiger monooxygenase exhibits a Criegee-like conformation
    • doi: 10.1021/ja211876p
    • Yachnin, B. J., Sprules, T., Mcevoy, M. B., Lau, P. C., and Berghuis, A. M. (2012). The substrate-bound crystal structure of a Baeyer-Villiger monooxygenase exhibits a Criegee-like conformation. J. Am. Chem. Soc. 134, 7788-7795. doi: 10.1021/ja211876p
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 7788-7795
    • Yachnin, B.J.1    Sprules, T.2    Mcevoy, M.B.3    Lau, P.C.4    Berghuis, A.M.5
  • 124
    • 34447096667 scopus 로고    scopus 로고
    • Titration and assignment of residues that regulate the enantioselectivity of phenylacetone monooxygenase
    • doi: 10.1002/adsc.200600598
    • Zambianchi, F., Fraaije, M. W., Carrea, G., de Gonzalo, G., Rodríguez, C., Gotor, V., et al. (2007). Titration and assignment of residues that regulate the enantioselectivity of phenylacetone monooxygenase. Adv. Synth. Catal. 349, 1327-1331. doi: 10.1002/adsc.200600598
    • (2007) Adv. Synth. Catal. , vol.349 , pp. 1327-1331
    • Zambianchi, F.1    Fraaije, M.W.2    Carrea, G.3    de Gonzalo, G.4    Rodríguez, C.5    Gotor, V.6
  • 125
    • 84880844116 scopus 로고    scopus 로고
    • Development of a whole-cell biocatalyst with NADPH regeneration system for biosulfoxidation
    • doi: 10.1007/s10295-013-1288-0
    • Zhai, X.-H., Ma, Y.-H., Lai, D.-Y., Zhou, S., and Chen, Z.-M. (2013). Development of a whole-cell biocatalyst with NADPH regeneration system for biosulfoxidation. J. Ind. Microbiol. Biotechnol. 40, 797-803. doi: 10.1007/s10295-013-1288-0
    • (2013) J. Ind. Microbiol. Biotechnol. , vol.40 , pp. 797-803
    • Zhai, X.-H.1    Ma, Y.-H.2    Lai, D.-Y.3    Zhou, S.4    Chen, Z.-M.5
  • 126
    • 84864621472 scopus 로고    scopus 로고
    • Protein engineering of stereoselective Baeyer-Villiger monooxygenases
    • doi: 10.1002/chem.201202163
    • Zhang, Z. G., Parra, L. P., and Reetz, M. T. (2012). Protein engineering of stereoselective Baeyer-Villiger monooxygenases. Chem. Eur. J. 18, 10160-10172. doi: 10.1002/chem.201202163
    • (2012) Chem. Eur. J. , vol.18 , pp. 10160-10172
    • Zhang, Z.G.1    Parra, L.P.2    Reetz, M.T.3
  • 127
    • 84872198112 scopus 로고    scopus 로고
    • A new type of stereoselectivity in Baeyer-Villiger reactions: access to E-and Z-olefins
    • doi: 10.1002/adsc.201200759
    • Zhang, Z. G., Roiban, G. D., Acevedo, J. P., Polyak, I., and Reetz, M. T. (2013). A new type of stereoselectivity in Baeyer-Villiger reactions: access to E-and Z-olefins. Adv. Synth. Catal. 355, 99-106. doi: 10.1002/adsc.201200759
    • (2013) Adv. Synth. Catal. , vol.355 , pp. 99-106
    • Zhang, Z.G.1    Roiban, G.D.2    Acevedo, J.P.3    Polyak, I.4    Reetz, M.T.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.