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Volumn 107, Issue 7, 2010, Pages 2775-2780

Induced allostery in the directed evolution of an enantioselective Baeyer-Villiger monooxygenase

Author keywords

Allosteric effects; Enzymes; Molecular dynamics simulations; Protein engineering

Indexed keywords

UNSPECIFIC MONOOXYGENASE;

EID: 77649260900     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0911656107     Document Type: Article
Times cited : (115)

References (40)
  • 1
    • 48249141040 scopus 로고    scopus 로고
    • Allostery and cooperativity revisited
    • Cui Q, Karplus M (2008) Allostery and cooperativity revisited. Protein Sci 17:1295-1307.
    • (2008) Protein Sci , vol.17 , pp. 1295-1307
    • Cui, Q.1    Karplus, M.2
  • 2
    • 60649109828 scopus 로고    scopus 로고
    • Protein allostery, signal transmission and dynamics: A classification scheme of allosteric mechanisms
    • Tsai C-J, del Sol A, Nussinov R (2009) Protein allostery, signal transmission and dynamics: A classification scheme of allosteric mechanisms. Mol Biosyst 5:207-216.
    • (2009) Mol Biosyst , vol.5 , pp. 207-216
    • Tsai, C.-J.1    del Sol, A.2    Nussinov, R.3
  • 3
    • 47649125643 scopus 로고    scopus 로고
    • Allosteric regulation and catalysis emerge via a common route
    • Goodey NM, Benkovic SJ (2008) Allosteric regulation and catalysis emerge via a common route. Nat Chem Biol 4:474-482.
    • (2008) Nat Chem Biol , vol.4 , pp. 474-482
    • Goodey, N.M.1    Benkovic, S.J.2
  • 4
    • 30044437590 scopus 로고    scopus 로고
    • Mechanistic insight into the allosteric activation of a ubiquitin-conjugating enzyme by RING-type ubiquitin ligases
    • Ozkan E, Yu H, Deisenhofer J (2005) Mechanistic insight into the allosteric activation of a ubiquitin-conjugating enzyme by RING-type ubiquitin ligases. P Natl Acad Sci USA 102:18890-18895.
    • (2005) P Natl Acad Sci USA , vol.102 , pp. 18890-18895
    • Ozkan, E.1    Yu, H.2    Deisenhofer, J.3
  • 5
    • 33746911627 scopus 로고    scopus 로고
    • Dynamic coupling and allosteric behavior in a nonallosteric protein
    • Clarkson MW, Gilmore SA, Edgell MH, Lee AL (2006) Dynamic coupling and allosteric behavior in a nonallosteric protein. Biochemistry 45:7693-7699.
    • (2006) Biochemistry , vol.45 , pp. 7693-7699
    • Clarkson, M.W.1    Gilmore, S.A.2    Edgell, M.H.3    Lee, A.L.4
  • 6
    • 23844465160 scopus 로고    scopus 로고
    • Directed evolution of protein switches and their application to the creation of ligand-binding proteins
    • Guntas G, Mansell TJ, Kim JR, Ostermeier M (2005) Directed evolution of protein switches and their application to the creation of ligand-binding proteins. P Natl Acad Sci USA 102:11224-11229.
    • (2005) P Natl Acad Sci USA , vol.102 , pp. 11224-11229
    • Guntas, G.1    Mansell, T.J.2    Kim, J.R.3    Ostermeier, M.4
  • 8
    • 68049106179 scopus 로고    scopus 로고
    • Directed evolution drives the next generation of biocatalysts
    • Turner NJ (2009) Directed evolution drives the next generation of biocatalysts. Nat Chem Biol 5:567-573.
    • (2009) Nat Chem Biol , vol.5 , pp. 567-573
    • Turner, N.J.1
  • 10
    • 43049123356 scopus 로고    scopus 로고
    • Advances in laboratory evolution of enzymes
    • Bershtein S, Tawfik DS (2008) Advances in laboratory evolution of enzymes. Curr Opin Chem Biol 12:151-158.
    • (2008) Curr Opin Chem Biol , vol.12 , pp. 151-158
    • Bershtein, S.1    Tawfik, D.S.2
  • 11
    • 84891038850 scopus 로고    scopus 로고
    • Directed evolution as a means to engineer enantioselective enzymes
    • ed Gotor V Wiley-VCH, Weinheim
    • Reetz MT (2008) Directed evolution as a means to engineer enantioselective enzymes. Asymmetric Organic Synthesis with Enzymes, ed Gotor V (Wiley-VCH, Weinheim).
    • (2008) Asymmetric Organic Synthesis with Enzymes
    • Reetz, M.T.1
  • 12
    • 77649253152 scopus 로고    scopus 로고
    • Reetz MT, Wang L-W, Bocola M (2006) Directed evolution of enantioselective enzymes: Iterative cycles of CASTing for probing protein-sequence space. Angew Chem 118:1258-1263 Erratum 2556; Angew Chem Int Ed 45:1236-1241; Erratum 2494.
    • Reetz MT, Wang L-W, Bocola M (2006) Directed evolution of enantioselective enzymes: Iterative cycles of CASTing for probing protein-sequence space. Angew Chem 118:1258-1263 Erratum 2556; Angew Chem Int Ed 45:1236-1241; Erratum 2494.
  • 13
    • 33845288649 scopus 로고    scopus 로고
    • Iterative saturation mutagenesis on the basis of B-factors as a strategy for increasing protein thermostability. Angew Chem
    • Reetz MT, Carballeira JD, Vogel A (2006) Iterative saturation mutagenesis on the basis of B-factors as a strategy for increasing protein thermostability. Angew Chem 118:7909-7915 Angew Chem Int Ed 45:7745-7751.
    • (2006) Angew Chem Int Ed , vol.45 , pp. 7745-7751
    • Reetz, M.T.1    Carballeira, J.D.2    Vogel, A.3
  • 14
    • 34248567845 scopus 로고    scopus 로고
    • Iterative saturation mutagenesis (ISM) for rapid directed evolution of functional enzymes
    • Reetz MT, Carballeira JD (2007) Iterative saturation mutagenesis (ISM) for rapid directed evolution of functional enzymes. Nat Protoc 2:891-903.
    • (2007) Nat Protoc , vol.2 , pp. 891-903
    • Reetz, M.T.1    Carballeira, J.D.2
  • 15
    • 18744380681 scopus 로고    scopus 로고
    • Impact of distal mutations on the network of coupled motions correlated to hydride transfer in dihydrofolate reductase
    • Wong KF, Selzer T, Benkovic SJ, Hammes-Schiffer S (2005) Impact of distal mutations on the network of coupled motions correlated to hydride transfer in dihydrofolate reductase. P Natl Acad Sci USA 102:6807-6812.
    • (2005) P Natl Acad Sci USA , vol.102 , pp. 6807-6812
    • Wong, K.F.1    Selzer, T.2    Benkovic, S.J.3    Hammes-Schiffer, S.4
  • 16
    • 33846302851 scopus 로고    scopus 로고
    • Learning from directed evolution: Further lessons from theoretical investigations into cooperative mutations in lipase enantioselectivity
    • Reetz MT, et al. (2007) Learning from directed evolution: Further lessons from theoretical investigations into cooperative mutations in lipase enantioselectivity. ChemBioChem 8:106-112.
    • (2007) ChemBioChem , vol.8 , pp. 106-112
    • Reetz, M.T.1
  • 17
    • 57749198860 scopus 로고    scopus 로고
    • Designer reagents' recombinant microorganisms: New and powerful tools for organic synthesis
    • Kayser MM (2009) 'Designer reagents' recombinant microorganisms: New and powerful tools for organic synthesis. Tetrahedron 65:947-974.
    • (2009) Tetrahedron , vol.65 , pp. 947-974
    • Kayser, M.M.1
  • 18
    • 0031838334 scopus 로고    scopus 로고
    • Cyclohexanone monooxygenase: A useful reagent for asymmetric Baeyer-Villiger reactions
    • Stewart JD (1998) Cyclohexanone monooxygenase: A useful reagent for asymmetric Baeyer-Villiger reactions. Curr Org Chem 2:195-216.
    • (1998) Curr Org Chem , vol.2 , pp. 195-216
    • Stewart, J.D.1
  • 19
    • 33745743032 scopus 로고    scopus 로고
    • Enzyme mediated Baeyer-Villiger oxidations
    • Mihovilovic MD (2006) Enzyme mediated Baeyer-Villiger oxidations. Curr Org Chem 10:1265-1287.
    • (2006) Curr Org Chem , vol.10 , pp. 1265-1287
    • Mihovilovic, M.D.1
  • 20
    • 84990161999 scopus 로고
    • Enzymic Baeyer-Villiger oxidations by flavin-dependent monooxygenases. Angew Chem
    • Walsh CT, Chen Y-CJ (1988) Enzymic Baeyer-Villiger oxidations by flavin-dependent monooxygenases. Angew Chem 100:342-352 Angew Chem, Int Ed Engl 27:333-343.
    • (1988) Angew Chem, Int Ed Engl , vol.27 , pp. 333-343
    • Walsh, C.T.1    Chen, Y.-C.J.2
  • 21
    • 28844495429 scopus 로고    scopus 로고
    • Microbial transformations 59: First kilogram scale asymmetric microbial Baeyer-Villiger oxidation with optimized productivity using a resin-based in situ SFPR strategy
    • Hilker I, Wohlgemuth R, Alphand V, Furstoss R (2005) Microbial transformations 59: First kilogram scale asymmetric microbial Baeyer-Villiger oxidation with optimized productivity using a resin-based in situ SFPR strategy. Biotechnol Bioeng 92:702-710.
    • (2005) Biotechnol Bioeng , vol.92 , pp. 702-710
    • Hilker, I.1    Wohlgemuth, R.2    Alphand, V.3    Furstoss, R.4
  • 22
    • 12144285047 scopus 로고    scopus 로고
    • Discovery of a thermostable Baeyer-Villiger monooxygenase by genome mining
    • Fraaije MW, et al. (2005) Discovery of a thermostable Baeyer-Villiger monooxygenase by genome mining. Appl Microbiol Biotechnol 66:393-400.
    • (2005) Appl Microbiol Biotechnol , vol.66 , pp. 393-400
    • Fraaije, M.W.1
  • 24
    • 34447096667 scopus 로고    scopus 로고
    • Titration and assignment of residues that regulate the enantioselectivity of phenylacetone monooxygenase
    • Zambianchi F, et al. (2007) Titration and assignment of residues that regulate the enantioselectivity of phenylacetone monooxygenase. Adv Synth Catal 349:1327-1331.
    • (2007) Adv Synth Catal , vol.349 , pp. 1327-1331
    • Zambianchi, F.1
  • 25
    • 20544433645 scopus 로고    scopus 로고
    • Converting phenylacetone monooxygenase into phenylcyclohexanone monooxygenase by rational design: Towards practical Baeyer-Villiger monooxygenases
    • Bocola M, et al. (2005) Converting phenylacetone monooxygenase into phenylcyclohexanone monooxygenase by rational design: Towards practical Baeyer-Villiger monooxygenases. Adv Synth Catal 347:979-986.
    • (2005) Adv Synth Catal , vol.347 , pp. 979-986
    • Bocola, M.1
  • 26
    • 55849148481 scopus 로고    scopus 로고
    • Greatly reduced amino acid alphabets in directed evolution: Making the right choice for saturation mutagenesis at homologous enzyme positions
    • 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 pp 5499-5501.
    • (2008) Chem Commun , pp. 5499-5501
    • Reetz, M.T.1    Wu, S.2
  • 27
    • 67649607265 scopus 로고    scopus 로고
    • Crystal structures of cyclohexanone monooxygenase reveal complex domain movements and a sliding cofactor
    • Mirza IA, et al. (2009) Crystal structures of cyclohexanone monooxygenase reveal complex domain movements and a sliding cofactor. J Am Chem Soc 131:8848-8854.
    • (2009) J Am Chem Soc , vol.131 , pp. 8848-8854
    • Mirza, I.A.1
  • 28
    • 0031015603 scopus 로고    scopus 로고
    • A mutation at the interface between domains causes rearrangement of domains in 3-isopropylmalate dehydrogenase
    • Qu C, Akanuma S, Moriyama H, Tanaka N, Oshima T (1997) A mutation at the interface between domains causes rearrangement of domains in 3-isopropylmalate dehydrogenase. Protein Eng 10:45-52.
    • (1997) Protein Eng , vol.10 , pp. 45-52
    • Qu, C.1    Akanuma, S.2    Moriyama, H.3    Tanaka, N.4    Oshima, T.5
  • 29
    • 0033593453 scopus 로고    scopus 로고
    • Redesigning the substrate specificity of an enzyme by cumulative effects of the mutations of non-active site residues
    • Oue S, Okamoto A, Yano T, Kagamiyama H (1999) Redesigning the substrate specificity of an enzyme by cumulative effects of the mutations of non-active site residues. J Biol Chem 274:2344-2349.
    • (1999) J Biol Chem , vol.274 , pp. 2344-2349
    • Oue, S.1    Okamoto, A.2    Yano, T.3    Kagamiyama, H.4
  • 30
    • 56949104426 scopus 로고    scopus 로고
    • The structure of monoamine oxidase from Aspergillus niger provides a molecular context for improvements in activity obtained by directed evolution
    • Atkin KE, et al. (2008) The structure of monoamine oxidase from Aspergillus niger provides a molecular context for improvements in activity obtained by directed evolution. J Mol Biol 384:1218-1231.
    • (2008) J Mol Biol , vol.384 , pp. 1218-1231
    • Atkin, K.E.1
  • 31
    • 0036841628 scopus 로고    scopus 로고
    • Creating randomized amino acid libraries with the QuikChange® multi site-directed mutagenesis kit
    • Hogrefe HH, Cline J, Youngblood GL, Allen RM (2002) Creating randomized amino acid libraries with the QuikChange® multi site-directed mutagenesis kit. BioTechniques 33:1158-1165.
    • (2002) BioTechniques , vol.33 , pp. 1158-1165
    • Hogrefe, H.H.1    Cline, J.2    Youngblood, G.L.3    Allen, R.M.4
  • 32
    • 0026746253 scopus 로고
    • Asymmetric reduction of ketoesters with alcohol dehydrogenase from Thermoanaerobacter ethanolicus
    • Zheng C, Pham VT, Philips RS (1992) Asymmetric reduction of ketoesters with alcohol dehydrogenase from Thermoanaerobacter ethanolicus. Bioorg Med Chem Lett 2:619-622.
    • (1992) Bioorg Med Chem Lett , vol.2 , pp. 619-622
    • Zheng, C.1    Pham, V.T.2    Philips, R.S.3
  • 34
    • 1642489328 scopus 로고    scopus 로고
    • Enzyme stabilization - recent experimental progress
    • Ó'Fágáin C (2003) Enzyme stabilization - recent experimental progress. Enzyme Microb Tech 33:137-149.
    • (2003) Enzyme Microb Tech , vol.33 , pp. 137-149
    • Ó'Fágáin, C.1
  • 37
    • 16344389701 scopus 로고    scopus 로고
    • Cation-pi interactions in protein-protein interfaces
    • Crowley PB, Golovin A (2005) Cation-pi interactions in protein-protein interfaces. Proteins 59:231-239.
    • (2005) Proteins , vol.59 , pp. 231-239
    • Crowley, P.B.1    Golovin, A.2
  • 38
    • 0026076090 scopus 로고
    • Collective motions in proteins: A covariance analysis of atomic fluctuations in molecular dynamics and normal mode simulations
    • Ichiye T, Karplus M (1994) Collective motions in proteins: A covariance analysis of atomic fluctuations in molecular dynamics and normal mode simulations. Proteins 11:205-217.
    • (1994) Proteins , vol.11 , pp. 205-217
    • Ichiye, T.1    Karplus, M.2
  • 39
    • 38949190032 scopus 로고    scopus 로고
    • Allosteric effects in the marginally stable von Hippel-Lindau tumor suppressor protein and allostery-based rescue mutant design
    • Liu J, Nussinov R (2008) Allosteric effects in the marginally stable von Hippel-Lindau tumor suppressor protein and allostery-based rescue mutant design. P Natl Acad Sci USA 105:901-906.
    • (2008) P Natl Acad Sci USA , vol.105 , pp. 901-906
    • Liu, J.1    Nussinov, R.2


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