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Volumn 12, Issue 1, 2017, Pages 291-299

Engineering cyclohexanone monooxygenase for the production of methyl propanoate

Author keywords

[No Author keywords available]

Indexed keywords

2 BUTANONE; CYCLOHEXANONE MONOOXYGENASE; METHYL PROPANOATE; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; PROPIONIC ACID DERIVATIVE; UNCLASSIFIED DRUG; UNSPECIFIC MONOOXYGENASE; ALKANONE; CYCLOHEXANONE OXYGENASE; HYBRID PROTEIN; HYDROGEN PEROXIDE; METHYLETHYL KETONE; NAD PHOSPHITE OXIDOREDUCTASE; OXIDOREDUCTASE; OXYGENASE;

EID: 85022045666     PISSN: 15548929     EISSN: 15548937     Source Type: Journal    
DOI: 10.1021/acschembio.6b00965     Document Type: Article
Times cited : (28)

References (45)
  • 1
    • 79960605776 scopus 로고    scopus 로고
    • Baeyer-Villiger monooxygenases: More than just green chemistry
    • Leisch, H., Morley, K., and Lau, P. C. K. (2011) Baeyer-Villiger monooxygenases: more than just green chemistry. Chem. Rev. 111, 4165-4222.
    • (2011) Chem. Rev. , vol.111 , pp. 4165-4222
    • Leisch, H.1    Morley, K.2    Lau, P.C.K.3
  • 2
    • 78049304724 scopus 로고    scopus 로고
    • Recent developments in the application of Baeyer-Villiger mono-oxygenases as biocatalysts
    • de Gonzalo, G., Mihovilovic, M. D., and Fraaije, M. W. (2010) Recent developments in the application of Baeyer-Villiger mono-oxygenases as biocatalysts. ChemBioChem 11, 2208-2231.
    • (2010) ChemBioChem , vol.11 , pp. 2208-2231
    • De Gonzalo, G.1    Mihovilovic, M.D.2    Fraaije, M.W.3
  • 3
    • 84903148559 scopus 로고    scopus 로고
    • Broadening the scope of Baeyer-Villiger monooxygenase activities toward α, ß-unsaturated ketones: A promising route to chiral enol-lactones and ene-lactones
    • Reignier, T., de Berardinis, V., Petit, J. L., Mariage, A., Hamze, K., Duquesne, K., and Alphand, V. (2014) Broadening the scope of Baeyer-Villiger monooxygenase activities toward α, ß-unsaturated ketones: a promising route to chiral enol-lactones and ene-lactones. Chem. Commun. 50, 7793-7796.
    • (2014) Chem. Commun. , vol.50 , pp. 7793-7796
    • Reignier, T.1    De Berardinis, V.2    Petit, J.L.3    Mariage, A.4    Hamze, K.5    Duquesne, K.6    Alphand, V.7
  • 4
    • 0035909090 scopus 로고    scopus 로고
    • Mechanistic studies of cyclohexanone monooxygenase: Chemical properties of intermediates involved in catalysis
    • Sheng, D., Ballou, D. P., and Massey, V. (2001) Mechanistic studies of cyclohexanone monooxygenase: chemical properties of intermediates involved in catalysis. Biochemistry 40, 11156-11167.
    • (2001) Biochemistry , vol.40 , pp. 11156-11167
    • Sheng, D.1    Ballou, D.P.2    Massey, V.3
  • 5
    • 0020490705 scopus 로고
    • Mechanistic studies on cyclohexanone oxygenase
    • Ryerson, C. C., Ballou, D. P., and Walsh, C. (1982) Mechanistic studies on cyclohexanone oxygenase. Biochemistry 21, 2644-2655.
    • (1982) Biochemistry , vol.21 , pp. 2644-2655
    • Ryerson, C.C.1    Ballou, D.P.2    Walsh, C.3
  • 6
    • 41449109033 scopus 로고    scopus 로고
    • Kinetic mechanism of phenylacetone monooxygenase from Thermobifida fusca
    • Torres Pazmino, D. E., Baas, B. J., Janssen, D. B., and Fraaije, M. W. (2008) Kinetic mechanism of phenylacetone monooxygenase from Thermobifida fusca. Biochemistry 47, 4082-4093.
    • (2008) Biochemistry , vol.47 , pp. 4082-4093
    • Torres Pazmino, D.E.1    Baas, B.J.2    Janssen, D.B.3    Fraaije, M.W.4
  • 8
    • 84856732583 scopus 로고    scopus 로고
    • Quantum mechanical/molecular mechanical study on the mechanism of the enzymatic Baeyer-Villiger reaction
    • Polyak, I., Reetz, M. T., and Thiel, W. (2012) Quantum mechanical/molecular mechanical study on the mechanism of the enzymatic Baeyer-Villiger reaction. J. Am. Chem. Soc. 134, 2732-2741.
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 2732-2741
    • Polyak, I.1    Reetz, M.T.2    Thiel, W.3
  • 9
    • 66149089180 scopus 로고    scopus 로고
    • Enzymatic baeyer-villiger oxidation of benzo-fused ketones: Formation of regiocomplementary lactones
    • Rioz-Martínez, A., de Gonzalo, G., Torres Pazmino, 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. 15, 2526-2532.
    • (2009) Eur. J. Org. Chem. , vol.15 , pp. 2526-2532
    • Rioz-Martínez, A.1    De Gonzalo, G.2    Torres Pazmino, D.E.3    Fraaije, M.W.4    Gotor, V.5
  • 10
    • 84952918064 scopus 로고    scopus 로고
    • Regio- and stereoselective synthesis of chiral nitrilolactones using Baeyer-Villiger monooxygenases
    • Fink, M. J., Snajdrova, R., Winninger, A., and Mihovilovic, M. D. (2016) Regio- and stereoselective synthesis of chiral nitrilolactones using Baeyer-Villiger monooxygenases. Tetrahedron 72, 7241-7248.
    • (2016) Tetrahedron , vol.72 , pp. 7241-7248
    • Fink, M.J.1    Snajdrova, R.2    Winninger, A.3    Mihovilovic, M.D.4
  • 11
    • 84955273067 scopus 로고    scopus 로고
    • Switching the regioselectivity of a cyclohexanone monooxygenase toward (+)-trans-dihydrocarvone by rational protein design
    • Balke, K., Schmidt, S., Genz, M., and Bornscheuer, U. T. (2016) Switching the regioselectivity of a cyclohexanone monooxygenase toward (+)-trans-dihydrocarvone by rational protein design. ACS Chem. Biol. 11, 38-43.
    • (2016) ACS Chem. Biol. , vol.11 , pp. 38-43
    • Balke, K.1    Schmidt, S.2    Genz, M.3    Bornscheuer, U.T.4
  • 12
    • 67649660098 scopus 로고    scopus 로고
    • Kinetic resolution of aliphatic acyclic ß-hydroxyketones by recombinant whole-cell Baeyer-Villiger monooxygenases-Formation of enantiocomplementary regioisomeric esters
    • Rehdorf, J., Lengar, A., Bornscheuer, U. T., and Mihovilovic, M. D. (2009) Kinetic resolution of aliphatic acyclic ß-hydroxyketones by recombinant whole-cell Baeyer-Villiger monooxygenases-Formation of enantiocomplementary regioisomeric esters. Bioorg. Med. Chem. Lett. 19, 3739-3743.
    • (2009) Bioorg. Med. Chem. Lett. , vol.19 , pp. 3739-3743
    • Rehdorf, J.1    Lengar, A.2    Bornscheuer, U.T.3    Mihovilovic, M.D.4
  • 13
    • 77953676536 scopus 로고    scopus 로고
    • Exploiting the regioselectivity of Baeyer-Villiger monooxygenases for the formation of ß-amino acids and ß-amino alcohols
    • Rehdorf, J., Mihovilovic, M. D., and Bornscheuer, U. T. (2010) Exploiting the regioselectivity of Baeyer-Villiger monooxygenases for the formation of ß-amino acids and ß-amino alcohols. Angew. Chem., Int. Ed. 49, 4506-4508.
    • (2010) Angew. Chem., Int. Ed. , vol.49 , pp. 4506-4508
    • Rehdorf, J.1    Mihovilovic, M.D.2    Bornscheuer, U.T.3
  • 14
    • 0942287234 scopus 로고    scopus 로고
    • The prodrug activator EtaA from Mycobacterium tuberculosis is a Baeyer-Villiger monooxygenase
    • Fraaije, M. W., Kamerbeek, N. M., Heidekamp, A. J., Fortin, R., and Janssen, D. B. (2004) The prodrug activator EtaA from Mycobacterium tuberculosis is a Baeyer-Villiger monooxygenase. J. Biol. Chem. 279, 3354-3360.
    • (2004) J. Biol. Chem. , vol.279 , pp. 3354-3360
    • Fraaije, M.W.1    Kamerbeek, N.M.2    Heidekamp, A.J.3    Fortin, R.4    Janssen, D.B.5
  • 15
    • 84907803198 scopus 로고    scopus 로고
    • Synthesis of methyl propanoate by Baeyer-Villiger monooxygenases
    • van Beek, H. L., Winter, R. T., Eastham, G. R., and Fraaije, M. W. (2014) Synthesis of methyl propanoate by Baeyer-Villiger monooxygenases. Chem. Commun. 50, 13034-13036.
    • (2014) Chem. Commun. , vol.50 , pp. 13034-13036
    • Van Beek, H.L.1    Winter, R.T.2    Eastham, G.R.3    Fraaije, M.W.4
  • 16
    • 84890840051 scopus 로고    scopus 로고
    • Acrylics for the future
    • Harris, B. (2010) Acrylics for the future. Ingenia 45, 18-23.
    • (2010) Ingenia , vol.45 , pp. 18-23
    • Harris, B.1
  • 17
    • 84893818789 scopus 로고    scopus 로고
    • Biological production of 2-butanone in Escherichia coli
    • Yoneda, H., Tantillo, D. J., and Atsumi, S. (2014) Biological production of 2-butanone in Escherichia coli. ChemSusChem 7, 92-95.
    • (2014) ChemSusChem , vol.7 , pp. 92-95
    • Yoneda, H.1    Tantillo, D.J.2    Atsumi, S.3
  • 19
    • 0025885032 scopus 로고
    • PPL-catalyzed resolution of 1, 2- and 1, 3-diols in methyl propionate as solvent. An application of the tandem use of enzymes
    • Janssen, A. J. M., Zwanenburg, B., and Klunder, A. H. (1991) PPL-catalyzed resolution of 1, 2- and 1, 3-diols in methyl propionate as solvent. An application of the tandem use of enzymes. Tetrahedron 47, 7409-7416.
    • (1991) Tetrahedron , vol.47 , pp. 7409-7416
    • Janssen, A.J.M.1    Zwanenburg, B.2    Klunder, A.H.3
  • 21
    • 84894354808 scopus 로고    scopus 로고
    • Stabilization of cyclohexanone monooxygenase by a computationally designed disulfide bond spanning only one residue
    • van Beek, H. L., Wijma, H. J., Fromont, L., Janssen, D. B., and Fraaije, M. W. (2014) Stabilization of cyclohexanone monooxygenase by a computationally designed disulfide bond spanning only one residue. FEBS Open Bio 4, 168-174.
    • (2014) FEBS Open Bio , vol.4 , pp. 168-174
    • Van Beek, H.L.1    Wijma, H.J.2    Fromont, L.3    Janssen, D.B.4    Fraaije, M.W.5
  • 24
    • 70350292190 scopus 로고    scopus 로고
    • Laboratory evolution of robust and enantioselective Baeyer-Villiger monooxygenases for asymmetric catalysis
    • 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.
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 15424-15432
    • Reetz, M.T.1    Wu, S.2
  • 25
    • 84919668855 scopus 로고    scopus 로고
    • Lactone-bound structures of cyclohexanone monooxygenase provide insight into the stereochemistry of catalysis
    • Yachnin, B. J., McEvoy, M. B., MacCuish, R. J. D., Morley, K. L., Lau, P. C. K., and Berghuis, A. M. (2014) Lactone-bound structures of cyclohexanone monooxygenase provide insight into the stereochemistry of catalysis. ACS Chem. Biol. 9, 2843-2851.
    • (2014) ACS Chem. Biol. , vol.9 , pp. 2843-2851
    • Yachnin, B.J.1    McEvoy, M.B.2    MacCuish, R.J.D.3    Morley, K.L.4    Lau, P.C.K.5    Berghuis, A.M.6
  • 26
    • 54349090614 scopus 로고    scopus 로고
    • Addressing the numbers problem in directed evolution
    • Reetz, M. T., Kahakeaw, D., and Lohmer, R. (2008) Addressing the numbers problem in directed evolution. ChemBioChem 9, 1797-1804.
    • (2008) ChemBioChem , vol.9 , pp. 1797-1804
    • Reetz, M.T.1    Kahakeaw, D.2    Lohmer, R.3
  • 27
    • 55849090547 scopus 로고    scopus 로고
    • Self-sufficient baeyer-villiger monooxygenases: Effective coenzyme regeneration for biooxygenation by fusion engineering
    • Torres Pazmino, D. E., Snajdrova, R., Baas, B. J., Ghobrial, M., Mihovilovic, M. D., and Fraaije, M. W. (2008) Self-sufficient baeyer-villiger monooxygenases: effective coenzyme regeneration for biooxygenation by fusion engineering. Angew. Chem. 120, 2307-2310.
    • (2008) Angew. Chem. , vol.120 , pp. 2307-2310
    • Torres Pazmino, D.E.1    Snajdrova, R.2    Baas, B.J.3    Ghobrial, M.4    Mihovilovic, M.D.5    Fraaije, M.W.6
  • 28
    • 71049192404 scopus 로고    scopus 로고
    • Efficient biooxidations catalyzed by a new generation of self-sufficient Baeyer-Villiger monooxygenases
    • Torres Pazmino, 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.
    • (2009) ChemBioChem , vol.10 , pp. 2595-2598
    • Torres Pazmino, D.E.1    Riebel, A.2    De Lange, J.3    Rudroff, F.4    Mihovilovic, M.D.5    Fraaije, M.W.6
  • 29
    • 0037023928 scopus 로고    scopus 로고
    • Use of isolated cyclohexanone monooxygenase from recombinant Escherichia coli as a biocatalyst for Baeyer-Villiger and sulfide oxidations
    • Zambianchi, F., Pasta, P., Carrea, G., Colonna, S., Gaggero, N., and Woodley, J. M. (2002) Use of isolated cyclohexanone monooxygenase from recombinant Escherichia coli as a biocatalyst for Baeyer-Villiger and sulfide oxidations. Biotechnol. Bioeng. 78, 489-496.
    • (2002) Biotechnol. Bioeng. , vol.78 , pp. 489-496
    • Zambianchi, F.1    Pasta, P.2    Carrea, G.3    Colonna, S.4    Gaggero, N.5    Woodley, J.M.6
  • 30
    • 84944882705 scopus 로고    scopus 로고
    • The effect of disulfide bond introduction and related Cys/Ser mutations on the stability of a cyclohexanone monooxygenase
    • Schmidt, S., Genz, M., Balke, K., and Bornscheuer, U. T. (2015) The effect of disulfide bond introduction and related Cys/Ser mutations on the stability of a cyclohexanone monooxygenase. J. Biotechnol. 214, 199-211.
    • (2015) J. Biotechnol. , vol.214 , pp. 199-211
    • Schmidt, S.1    Genz, M.2    Balke, K.3    Bornscheuer, U.T.4
  • 31
    • 65349155431 scopus 로고    scopus 로고
    • ThermoFAD, a Thermofluor®-adapted flavin ad hoc detection system for protein folding and ligand binding
    • Forneris, F., Orru, R., Bonivento, D., Chiarelli, L. R., and Mattevi, A. (2009) ThermoFAD, a Thermofluor®-adapted flavin ad hoc detection system for protein folding and ligand binding. FEBS J. 276, 2833-2840.
    • (2009) FEBS J , vol.276 , pp. 2833-2840
    • Forneris, F.1    Orru, R.2    Bonivento, D.3    Chiarelli, L.R.4    Mattevi, A.5
  • 32
    • 0022980412 scopus 로고
    • Reactions of the 4a-hydroperoxide of liver microsomal flavin-containing monooxygenase with nucleophilic and electrophilic substrates
    • Jones, K. C., and Ballou, D. P. (1986) Reactions of the 4a-hydroperoxide of liver microsomal flavin-containing monooxygenase with nucleophilic and electrophilic substrates. J. Biol. Chem. 261, 2553-2559.
    • (1986) J. Biol. Chem. , vol.261 , pp. 2553-2559
    • Jones, K.C.1    Ballou, D.P.2
  • 33
    • 78650947225 scopus 로고    scopus 로고
    • Ph-dependent studies reveal an efficient hydroxylation mechanism of the oxygenase component of p-hydroxyphenylacetate 3-hydroxylase
    • Ruangchan, N., Tongsook, C., Sucharitakul, J., and Chaiyen, P. (2011) pH-dependent studies reveal an efficient hydroxylation mechanism of the oxygenase component of p-hydroxyphenylacetate 3-hydroxylase. J. Biol. Chem. 286, 223-233.
    • (2011) J. Biol. Chem. , vol.286 , pp. 223-233
    • Ruangchan, N.1    Tongsook, C.2    Sucharitakul, J.3    Chaiyen, P.4
  • 34
    • 84898067298 scopus 로고    scopus 로고
    • How pH modulates the reactivity and selectivity of a siderophore-associated flavin monooxygenase
    • Frederick, R. E., Ojha, S., Lamb, A., and DuBois, J. L. (2014) How pH modulates the reactivity and selectivity of a siderophore-associated flavin monooxygenase. Biochemistry 53, 2007-2016.
    • (2014) Biochemistry , vol.53 , pp. 2007-2016
    • Frederick, R.E.1    Ojha, S.2    Lamb, A.3    DuBois, J.L.4
  • 35
    • 84883802943 scopus 로고    scopus 로고
    • Mechanistic aspects regarding the elimination of H2O2 from C (4a)-hydroperoxyflavin. The role of a proton shuttle required for H2O2 elimination
    • Bach, R. D., and Mattevi, A. (2013) Mechanistic aspects regarding the elimination of H2O2 from C (4a)-hydroperoxyflavin. The role of a proton shuttle required for H2O2 elimination. J. Org. Chem. 78, 8585-8593.
    • (2013) J. Org. Chem. , vol.78 , pp. 8585-8593
    • Bach, R.D.1    Mattevi, A.2
  • 36
    • 0034161331 scopus 로고    scopus 로고
    • Flavoenzymes: Diverse catalysts with recurrent features
    • Fraaije, M. W., and Mattevi, A. (2000) Flavoenzymes: diverse catalysts with recurrent features. Trends Biochem. Sci. 25, 126-132.
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 126-132
    • Fraaije, M.W.1    Mattevi, A.2
  • 37
    • 80051480273 scopus 로고    scopus 로고
    • Stabilization of C4a-hydroperoxyflavin in a two-component flavin-dependent monooxygenase is achieved through interactions at flavin N5 and C4a atoms
    • Thotsaporn, K., Chenprakhon, P., Sucharitakul, J., Mattevi, A., and Chaiyen, P. (2011) Stabilization of C4a-hydroperoxyflavin in a two-component flavin-dependent monooxygenase is achieved through interactions at flavin N5 and C4a atoms. J. Biol. Chem. 286, 28170-28180.
    • (2011) J. Biol. Chem. , vol.286 , pp. 28170-28180
    • Thotsaporn, K.1    Chenprakhon, P.2    Sucharitakul, J.3    Mattevi, A.4    Chaiyen, P.5
  • 39
    • 38349156041 scopus 로고    scopus 로고
    • Structural analysis of the catalytic mechanism and stereoselectivity in Streptomyces coelicolor alditol oxidase
    • Forneris, F., Heuts, D. P. H. M., Delvecchio, M., Rovida, S., Fraaije, M. W., and Mattevi, A. (2008) Structural analysis of the catalytic mechanism and stereoselectivity in Streptomyces coelicolor alditol oxidase. Biochemistry 47, 978-985.
    • (2008) Biochemistry , vol.47 , pp. 978-985
    • Forneris, F.1    Heuts, D.P.H.M.2    Delvecchio, M.3    Rovida, S.4    Fraaije, M.W.5    Mattevi, A.6
  • 40
    • 79952094721 scopus 로고    scopus 로고
    • Importance of a serine proximal to the C (4a) and N (5) flavin atoms for hydride transfer in choline oxidase
    • Yuan, H., and Gadda, G. (2011) Importance of a serine proximal to the C (4a) and N (5) flavin atoms for hydride transfer in choline oxidase. Biochemistry 50, 770-779.
    • (2011) Biochemistry , vol.50 , pp. 770-779
    • Yuan, H.1    Gadda, G.2
  • 41
    • 33847669697 scopus 로고    scopus 로고
    • Modulation of the redox properties of the flavin cofactor through hydrogen-bonding interactions with the N (5) atom: Role of αSer254 in the electron-transfer flavoprotein from the methylotrophic bacterium W3A1
    • Yang, K.-Y., and Swenson, R. P. (2007) Modulation of the redox properties of the flavin cofactor through hydrogen-bonding interactions with the N (5) atom: role of αSer254 in the electron-transfer flavoprotein from the methylotrophic bacterium W3A1. Biochemistry 46, 2289-2297.
    • (2007) Biochemistry , vol.46 , pp. 2289-2297
    • Yang, K.-Y.1    Swenson, R.P.2
  • 42
    • 84918551429 scopus 로고    scopus 로고
    • Finding the switch: Turning a baeyer-villiger monooxygenase into a NADPH oxidase
    • Brondani, P. B., Dudek, H. M., Martinoli, C., Mattevi, A., and Fraaije, M. W. (2014) Finding the switch: turning a baeyer-villiger monooxygenase into a NADPH oxidase. J. Am. Chem. Soc. 136, 16966-16969.
    • (2014) J. Am. Chem. Soc. , vol.136 , pp. 16966-16969
    • Brondani, P.B.1    Dudek, H.M.2    Martinoli, C.3    Mattevi, A.4    Fraaije, M.W.5
  • 44
    • 34547170108 scopus 로고    scopus 로고
    • Altering the substrate specificity and enantioselectivity of phenylacetone monooxygenase by structure-inspired enzyme redesign
    • Pazmino, D. E. T., 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.
    • (2007) Adv. Synth. Catal. , vol.349 , pp. 1361-1368
    • Pazmino, D.E.T.1    Snajdrova, R.2    Rial, D.V.3    Mihovilovic, M.D.4    Fraaije, M.W.5
  • 45
    • 0035909090 scopus 로고    scopus 로고
    • Mechanistic studies of cyclohexanone monooxygenase: Chemical properties of intermediates involved in catalysis
    • Sheng, D., Ballou, D. P., and Massey, V. (2001) Mechanistic studies of cyclohexanone monooxygenase: chemical properties of intermediates involved in catalysis. Biochemistry 40, 11156-11167.
    • (2001) Biochemistry , vol.40 , pp. 11156-11167
    • Sheng, D.1    Ballou, D.P.2    Massey, V.3


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