메뉴 건너뛰기




Volumn 98, Issue 9, 2014, Pages 4009-4020

Extending the substrate scope of a Baeyer-Villiger monooxygenase by multiple-site mutagenesis

Author keywords

Baeyer Villiger monooxygenase; Biocatalysis; OmniChange mutagenesis; Oxygenation; Protein engineering

Indexed keywords

KETONES; OXYGENATION;

EID: 84899956948     PISSN: 01757598     EISSN: 14320614     Source Type: Journal    
DOI: 10.1007/s00253-013-5364-1     Document Type: Article
Times cited : (37)

References (38)
  • 1
    • 84863953159 scopus 로고    scopus 로고
    • Discovery, application and protein engineering of Baeyer-Villiger monooxygenases for organic synthesis
    • Balke K, KadowM, Mallin H, Saß S, Bornscheuer UT (2012) Discovery, application and protein engineering of Baeyer-Villiger monooxygenases for organic synthesis. Org Biomol Chem 10:6249-6265
    • (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
  • 4
    • 0033942392 scopus 로고    scopus 로고
    • Simultaneous identification of two cyclohexanone oxidation genes from an environmental Brevibacterium isolate using MRNA differential display
    • DOI 10.1128/JB.182.15.4241-4248.2000
    • Brzostowicz PC, Gibson KL, Thomas SM, Blasko MS, Rouviere PE (2000) Simultaneous identification of two cyclohexanone oxidation genes from an environmental Brevibacterium isolate using mRNA differential display. J Bacteriol 182:4241-4248 (Pubitemid 30463788)
    • (2000) Journal of Bacteriology , vol.182 , Issue.15 , pp. 4241-4248
    • Brzostowicz, P.C.1    Gibson, K.L.2    Thomas, S.M.3    Blasko, M.S.4    Rouviere, P.E.5
  • 5
    • 12744280848 scopus 로고    scopus 로고
    • Proposed involvement of a soluble methane monooxygenase homologue in the cyclohexane-dependent growth of a new Brachymonas species
    • Brzostowicz PC, Walters DM, Jackson RE, Halsey KH, Ni H, Rouviere PE (2005) Proposed involvement of a soluble methane monooxygenase homologue in the cyclohexane-dependent growth of a new Brachymonas species. Environ Microbiol 7:179-190
    • (2005) Environ Microbiol , vol.7 , pp. 179-190
    • Brzostowicz, P.C.1    Walters, D.M.2    Jackson, R.E.3    Halsey, K.H.4    Ni, H.5    Rouviere, P.E.6
  • 6
    • 0037229833 scopus 로고    scopus 로고
    • mRNA differential display in a microbial enrichment culture: Simultaneous identification of three cyclohexanone monooxygenases from three species
    • DOI 10.1128/AEM.69.1.334-342.2003
    • Brzostowicz PC, Walters DM, Thomas SM, Nagarajan V, Rouviere PE (2003) mRNA differential display in a microbial enrichment culture: simultaneous identification of three cyclohexanone monooxygenases from three species. Appl Environ Microbiol 69:334-342 (Pubitemid 36077493)
    • (2003) Applied and Environmental Microbiology , vol.69 , Issue.1 , pp. 334-342
    • Brzostowicz, P.C.1    Walters, D.M.2    Thomas, S.M.3    Nagarajan, V.4    Rouviere, P.E.5
  • 7
    • 0023958999 scopus 로고
    • Acinetobacter cyclohexanone monooxygenase: Gene cloning and sequence determination
    • Chen YC, Peoples OP, Walsh CT (1988) Acinetobacter cyclohexanone monooxygenase: gene cloning and sequence determination. J Bacteriol 170:781-789
    • (1988) J Bacteriol , vol.170 , pp. 781-789
    • Chen, Y.C.1    Peoples, O.P.2    Walsh, C.T.3
  • 8
    • 78049304724 scopus 로고    scopus 로고
    • Recent developments in the application of Baeyer-Villiger monooxygenases as biocatalysts
    • de Gonzalo G, Mihovilovic MD, Fraaije MW (2010) Recent developments in the application of Baeyer-Villiger monooxygenases 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
  • 9
    • 24944565284 scopus 로고    scopus 로고
    • Oxidations catalyzed by phenylacetone monooxygenase from Thermobifida fusca
    • DOI 10.1016/j.tetasy.2005.08.004, PII S0957416605005902
    • de Gonzalo G, Torres Pazmiño DE, Ottolina G, Fraaije MW, Carrea G (2005) Oxidations catalyzed by phenylacetone monooxygenase from Thermobifida fusca. Tetrahedron Asymmetry 16:3077-3083 (Pubitemid 41317549)
    • (2005) Tetrahedron Asymmetry , vol.16 , Issue.18 , pp. 3077-3083
    • De Gonzalo, G.1    Torres, P.D.E.2    Ottolina, G.3    Fraaije, M.W.4    Carrea, G.5
  • 11
    • 80054785847 scopus 로고    scopus 로고
    • OmniChange: The sequence independent method for simultaneous site-saturation of five codons
    • Dennig A, Shivange AV, Marienhagen J, Schwaneberg U (2011) OmniChange: the sequence independent method for simultaneous site-saturation of five codons. PLoS ONE 6:e26222
    • (2011) PLoS ONE , vol.6
    • Dennig, A.1    Shivange, A.V.2    Marienhagen, J.3    Schwaneberg, U.4
  • 13
  • 14
    • 84871090417 scopus 로고    scopus 로고
    • Quantitative comparison of chiral catalysts selectivity and performance: A generic concept illustrated with cyclododecanone monooxygenase as Baeyer-Villiger biocatalyst
    • Fink MJ, Rial DV, Kapitanova P, Lengar A, Rehdorf J, Cheng Q, Rudroff F, Mihovilovic MD (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
    • (2012) Adv Synth Catal , vol.354 , pp. 3491-3500
    • Fink, M.J.1    Rial, D.V.2    Kapitanova, P.3    Lengar, A.4    Rehdorf, J.5    Cheng, Q.6    Rudroff, F.7    Mihovilovic, M.D.8
  • 15
    • 84874196267 scopus 로고    scopus 로고
    • Single operation stereoselective synthesis of aerangis lactones: Combining continuous flow hydrogenation and biocatalysts in a chemoenzymatic sequence
    • Fink MJ, Schoen M, Rudroff F, Schnuerch M, Mihovilovic MD (2013) Single operation stereoselective synthesis of aerangis lactones: combining continuous flow hydrogenation and biocatalysts in a chemoenzymatic sequence. ChemCatChem 5:724-727
    • (2013) ChemCatChem , vol.5 , pp. 724-727
    • Fink, M.J.1    Schoen, M.2    Rudroff, F.3    Schnuerch, M.4    Mihovilovic, M.D.5
  • 16
    • 23944462537 scopus 로고    scopus 로고
    • Statistics of protein library construction
    • DOI 10.1093/bioinformatics/bti516
    • Firth AE, Patrick WM (2005) Statistics of protein library construction. Bioinformatics 21:3314-3315 (Pubitemid 41418448)
    • (2005) Bioinformatics , vol.21 , Issue.15 , pp. 3314-3315
    • Firth, A.E.1    Patrick, W.M.2
  • 17
    • 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 LR, 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
  • 19
    • 84863313527 scopus 로고    scopus 로고
    • Exploring the structural basis of substrate preferences in Baeyer-Villiger monooxygenases: Insight from steroid monooxygenase
    • Franceschini S, van Beek HL, Pennetta A, Martinoli C, Fraaije MW, Mattevi A (2012) Exploring the structural basis of substrate preferences in Baeyer-Villiger monooxygenases: insight from steroid monooxygenase. J Biol Chem 287:22626-22634
    • (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
  • 20
    • 0036841620 scopus 로고    scopus 로고
    • Cloning and characterization of a gene cluster involved in cyclopentanol metabolism in Comamonas sp. strain NCIMB 9872 and biotransformations effected by Escherichia coli-expressed cyclopentanone 1,2-monooxygenase
    • Iwaki H, Hasegawa Y, Wang S, Kayser MM, Lau PC (2002) Cloning and characterization of a gene cluster involved in cyclopentanol metabolism in Comamonas sp. strain NCIMB 9872 and biotransformations effected by Escherichia coli-expressed cyclopentanone 1,2-monooxygenase. Appl Environ Microbiol 68:5671-5684 (Pubitemid 35265707)
    • (2002) Applied and Environmental Microbiology , vol.68 , Issue.11 , pp. 5671-5684
    • Iwaki, H.1    Hasegawa, Y.2    Wang, S.3    Kayser, M.M.4    Lau, P.C.K.5
  • 21
    • 40549136846 scopus 로고    scopus 로고
    • Cloning and characterization of a cyclohexanone monooxygenase gene from Arthrobacter sp. L661
    • Kim YM, Jung SH, Chung YH, Yu CB, Rhee IK (2008) Cloning and characterization of a cyclohexanone monooxygenase gene from Arthrobacter sp. L661. Biotechnol Bioprocess Eng 13:40-47
    • (2008) Biotechnol Bioprocess Eng , vol.13 , pp. 40-47
    • Kim, Y.M.1    Jung, S.H.2    Chung, Y.H.3    Yu, C.B.4    Rhee, I.K.5
  • 23
    • 79960605776 scopus 로고    scopus 로고
    • Baeyer-Villiger monooxygenases: More than just green chemistry
    • Leisch H, Morley K, Lau PC (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.3
  • 27
    • 4644335310 scopus 로고    scopus 로고
    • Directed evolution as a method to create enantioselective cyclohexanone monooxygenases for catalysis in Baeyer-Villiger reactions
    • DOI 10.1002/anie.200460272
    • Reetz MT, Brunner B, Schneider T, Schulz F, Clouthier CM, Kayser MM (2004a) Directed evolution as a method to create enantioselective cyclohexanone monooxygenases for catalysis in Baeye-Villiger reactions. Angew Chem Int Ed Engl 43:4075-4078 (Pubitemid 39268851)
    • (2004) Angewandte Chemie - International Edition , vol.43 , Issue.31 , pp. 4075-4078
    • Reetz, M.T.1    Brunner, B.2    Schneider, T.3    Schulz, F.4    Clouthier, C.M.5    Kayser, M.M.6
  • 28
    • 4544342882 scopus 로고    scopus 로고
    • Directed evolution of cyclohexanone monooxygenases: Enantioselective biocatalysts for the oxidation of prochiral thioethers
    • DOI 10.1002/anie.200460311
    • Reetz MT, Daligault F, Brunner B, Hinrichs H, Deege A (2004b) Directed evolution of cyclohexanone monooxygenases: enantioselective biocatalysts for the oxidation of prochiral thioethers. Angew Chem Int Ed Engl 43:4078-4081 (Pubitemid 39257458)
    • (2004) Angewandte Chemie - International Edition , vol.43 , Issue.31 , pp. 4078-4081
    • Reetz, M.T.1    Daligault, F.2    Brunner, B.3    Hinrichs, H.4    Deege, A.5
  • 29
    • 55849148481 scopus 로고    scopus 로고
    • Greatly reduced amino acid alphabets in directed evolution: Making the right choice for saturation mutagenesis at homologous enzyme positions
    • Camb
    • Reetz MT, Wu S (2008) Greatly reduced amino acid alphabets in directed evolution: Making the right choice for saturation mutagenesis at homologous enzyme positions. Chem Commun (Camb) 5499-5501
    • (2008) Chem Commun , pp. 5499-5501
    • Reetz, M.T.1    Wu, S.2
  • 30
    • 70350292190 scopus 로고    scopus 로고
    • Laboratory evolution of robust and enantioselective Baeyer-Villiger monooxygenases for asymmetric catalysis
    • Reetz MT, 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
  • 31
    • 84872036176 scopus 로고    scopus 로고
    • Expanding the set of rhodococcal Baeyer-Villiger monooxygenases by high-throughput cloning, expression and substrate screening
    • Riebel A, Dudek HM, de Gonzalo G, Stȩpniak P, Rychlewski L, Fraaije MW (2012) Expanding the set of rhodococcal Baeyer-Villiger monooxygenases by high-throughput cloning, expression and substrate screening. Appl Microbiol Biotechnol 95:1479-1489
    • (2012) Appl Microbiol Biotechnol , vol.95 , pp. 1479-1489
    • Riebel, A.1    Dudek, H.M.2    De Gonzalo, G.3    Stȩpniak, P.4    Rychlewski, L.5    Fraaije, M.W.6
  • 32
    • 34447092984 scopus 로고    scopus 로고
    • Enzymatic kinetic resolution of racemic ketones catalyzed by Baeyer-Villiger monooxygenases
    • DOI 10.1016/j.tetasy.2007.05.033, PII S0957416607004168
    • Rodríguez C, de Gonzalo G, Fraaije MW, Gotor V (2007) Enzymatic kinetic resolution of racemic ketones catalyzed by Baeyer-Villiger monooxygenases. Tetrahedron Asymmetry 18:1338-1344 (Pubitemid 47030896)
    • (2007) Tetrahedron Asymmetry , vol.18 , Issue.11 , pp. 1338-1344
    • Rodriguez, C.1    De Gonzalo, G.2    Fraaije, M.W.3    Gotor, V.4
  • 33
    • 78751538650 scopus 로고    scopus 로고
    • Effects of water miscible organic solvents on the activity and conformation of the Baeyer-Villiger monooxygenases from Thermobifida fusca and Acinetobacter calcoaceticus: A comparative study
    • Secundo F, Fiala S, Fraaije MW, de Gonzalo G, Meli M, Zambianchi F, Ottolina G (2011) Effects of water miscible organic solvents on the activity and conformation of the Baeyer-Villiger monooxygenases from Thermobifida fusca and Acinetobacter calcoaceticus : a comparative study. Biotechnol Bioeng 108:491-499
    • (2011) Biotechnol Bioeng , vol.108 , pp. 491-499
    • Secundo, F.1    Fiala, S.2    Fraaije, M.W.3    De Gonzalo, G.4    Meli, M.5    Zambianchi, F.6    Ottolina, G.7
  • 34
    • 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
    • Szolkowy C, Eltis LD, Bruce NC, Grogan G (2009) Insights into sequence-activity relationships amongst Baeyer-Villiger monooxygenases as revealed by the intragenomic complement of enzymes from Rhodococcus jostii RHA1. ChemBioChem10:1208-1217
    • (2009) ChemBioChem , vol.10 , pp. 1208-1217
    • Szolkowy, C.1    Eltis, L.D.2    Bruce, N.C.3    Grogan, G.4
  • 35
    • 41449109033 scopus 로고    scopus 로고
    • Kinetic mechanism of phenylacetone monooxygenase from Thermobifida fusca
    • DOI 10.1021/bi702296k
    • Torres Pazmiño DE, Baas BJ, Janssen DB, Fraaije MW (2008) Kinetic mechanism of phenylacetone monooxygenase from Thermobifida fusca. Biochemistry 47:4082-4093 (Pubitemid 351458122)
    • (2008) Biochemistry , vol.47 , Issue.13 , pp. 4082-4093
    • Torres, P.D.E.1    Baas, B.-J.2    Janssen, D.B.3    Fraaije, M.W.4
  • 36
    • 34547170108 scopus 로고    scopus 로고
    • Altering the substrate specificity and enantioselectivity of phenylacetone monooxygenase by structure-inspired enzyme redesign
    • Torres Pazmiño DE, Snajdrova R, Rial DV, Mihovilovic MD, Fraaije MW (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
    • Torres Pazmiño, D.E.1    Snajdrova, R.2    Rial, D.V.3    Mihovilovic, M.D.4    Fraaije, M.W.5
  • 37
    • 0037345547 scopus 로고    scopus 로고
    • Cloning of Baeyer-Villiger monooxygenases from Comamonas, Xanthobacter and Rhodococcus using polymerase chain reaction with highly degenerate primers
    • DOI 10.1046/j.1462-2920.2003.00401.x
    • van Beilen JB, Mourlane F, Seeger MA, Kovac J, Li Z, Smits TH, Fritsche U, Witholt B (2003) Cloning of Baeyer-Villiger monooxygenases from Comamonas, Xanthobacter and Rhodococcus using polymerase chain reaction with highly degenerate primers. Environ Microbiol 5:174-182 (Pubitemid 36352437)
    • (2003) Environmental Microbiology , vol.5 , Issue.3 , pp. 174-182
    • Van Beilen, J.B.1    Mourlane, F.2    Seeger, M.A.3    Kovac, J.4    Li, Z.5    Smits, T.H.M.6    Fritsche, U.7    Witholt, B.8
  • 38
    • 77649260900 scopus 로고    scopus 로고
    • Induced allostery in the directed evolution of an enantioselective Baeyer-Villiger monooxygenase
    • Wu S, Acevedo JP, Reetz MT (2010) Induced allostery in the directed evolution of an enantioselective Baeyer-Villiger monooxygenase. Proc Natl Acad Sci U S A 107:2775-2780
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 2775-2780
    • Wu, S.1    Acevedo, J.P.2    Reetz, M.T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.