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Volumn 9, Issue 2, 2005, Pages 210-216

High-throughput screens and selections of enzyme-encoding genes

Author keywords

[No Author keywords available]

Indexed keywords

DNA METHYLTRANSFERASE; DNA POLYMERASE; ENDONUCLEASE; ENZYME; NUCLEASE;

EID: 13844250741     PISSN: 13675931     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cbpa.2005.02.002     Document Type: Review
Times cited : (158)

References (55)
  • 2
    • 0036897839 scopus 로고    scopus 로고
    • Milestones in directed enzyme evolution
    • H. Tao, and V.W. Cornish Milestones in directed enzyme evolution Curr Opin Chem Biol 6 2002 858 864
    • (2002) Curr Opin Chem Biol , vol.6 , pp. 858-864
    • Tao, H.1    Cornish, V.W.2
  • 3
    • 0037011406 scopus 로고    scopus 로고
    • Screening and selection methods for large-scale analysis of protein function
    • H. Lin, and V.W. Cornish Screening and selection methods for large-scale analysis of protein function Angew Chem Int Ed Engl 41 2002 4402 4425
    • (2002) Angew Chem Int Ed Engl , vol.41 , pp. 4402-4425
    • Lin, H.1    Cornish, V.W.2
  • 4
    • 0042430535 scopus 로고    scopus 로고
    • Optimising enzyme function by directed evolution
    • P.A. Dalby Optimising enzyme function by directed evolution Curr Opin Struct Biol 13 2003 500 505
    • (2003) Curr Opin Struct Biol , vol.13 , pp. 500-505
    • Dalby, P.A.1
  • 5
    • 2542563521 scopus 로고    scopus 로고
    • Chemical and biochemical strategies for the randomization of protein encoding DNA sequences: Library construction methods for directed evolution
    • C. Neylon Chemical and biochemical strategies for the randomization of protein encoding DNA sequences: library construction methods for directed evolution Nucleic Acids Res 32 2004 1448 1459
    • (2004) Nucleic Acids Res , vol.32 , pp. 1448-1459
    • Neylon, C.1
  • 6
    • 3543106035 scopus 로고    scopus 로고
    • Novel methods for directed evolution of enzymes: Quality, not quantity
    • S. Lutz, and W.M. Patrick Novel methods for directed evolution of enzymes: quality, not quantity Curr Opin Biotechnol 15 2004 291 297
    • (2004) Curr Opin Biotechnol , vol.15 , pp. 291-297
    • Lutz, S.1    Patrick, W.M.2
  • 7
  • 8
    • 0036903280 scopus 로고    scopus 로고
    • Methods to increase enantioselectivity of lipases and esterases
    • U.T. Bornscheuer Methods to increase enantioselectivity of lipases and esterases Curr Opin Biotechnol 13 2002 543 547
    • (2002) Curr Opin Biotechnol , vol.13 , pp. 543-547
    • Bornscheuer, U.T.1
  • 10
    • 3543116602 scopus 로고    scopus 로고
    • Enzyme assays for high-throughput screening
    • J.P. Goddard, and J.L. Reymond Enzyme assays for high-throughput screening Curr Opin Biotechnol 15 2004 314 322
    • (2004) Curr Opin Biotechnol , vol.15 , pp. 314-322
    • Goddard, J.P.1    Reymond, J.L.2
  • 11
    • 4444346508 scopus 로고    scopus 로고
    • Rapid and ultra-sensitive determination of enzyme activities using surface-enhanced resonance Raman scattering
    • B.D. Moore, L. Stevenson, A. Watt, S. Flitsch, N.J. Turner, C. Cassidy, and D. Graham Rapid and ultra-sensitive determination of enzyme activities using surface-enhanced resonance Raman scattering Nat Biotechnol 22 2004 1133 1138
    • (2004) Nat Biotechnol , vol.22 , pp. 1133-1138
    • Moore, B.D.1    Stevenson, L.2    Watt, A.3    Flitsch, S.4    Turner, N.J.5    Cassidy, C.6    Graham, D.7
  • 12
    • 0033013283 scopus 로고    scopus 로고
    • Screening, nucleotide sequence, and biochemical characterization of an esterase from Pseudomonas fluorescens with high activity towards lactones
    • V. Khalameyzer, I. Fischer, U.T. Bornscheuer, and J. Altenbuchner Screening, nucleotide sequence, and biochemical characterization of an esterase from Pseudomonas fluorescens with high activity towards lactones Appl Environ Microbiol 65 1999 477 482
    • (1999) Appl Environ Microbiol , vol.65 , pp. 477-482
    • Khalameyzer, V.1    Fischer, I.2    Bornscheuer, U.T.3    Altenbuchner, J.4
  • 13
    • 3543087310 scopus 로고    scopus 로고
    • Trends and innovations in industrial biocatalysis for the production of fine chemicals
    • S. Panke, M. Held, and M. Wubbolts Trends and innovations in industrial biocatalysis for the production of fine chemicals Curr Opin Biotechnol 15 2004 272 279
    • (2004) Curr Opin Biotechnol , vol.15 , pp. 272-279
    • Panke, S.1    Held, M.2    Wubbolts, M.3
  • 14
    • 0142248496 scopus 로고    scopus 로고
    • Directed evolution of enzymes for applied biocatalysis
    • N.J. Turner Directed evolution of enzymes for applied biocatalysis Trends Biotechnol 21 2003 474 478
    • (2003) Trends Biotechnol , vol.21 , pp. 474-478
    • Turner, N.J.1
  • 15
  • 16
    • 0035424963 scopus 로고    scopus 로고
    • In vitro display technologies: Novel developments and applications
    • P. Amstutz, P. Forrer, C. Zahnd, and A. Pluckthun In vitro display technologies: novel developments and applications Curr Opin Biotechnol 12 2001 400 405
    • (2001) Curr Opin Biotechnol , vol.12 , pp. 400-405
    • Amstutz, P.1    Forrer, P.2    Zahnd, C.3    Pluckthun, A.4
  • 17
    • 0037333841 scopus 로고    scopus 로고
    • MRNA display: Ligand discovery, interaction analysis and beyond
    • T.T. Takahashi, R.J. Austin, and R.W. Roberts mRNA display: ligand discovery, interaction analysis and beyond Trends Biochem Sci 28 2003 159 165
    • (2003) Trends Biochem Sci , vol.28 , pp. 159-165
    • Takahashi, T.T.1    Austin, R.J.2    Roberts, R.W.3
  • 18
    • 3543063987 scopus 로고    scopus 로고
    • Ultra-high-throughput screening based on cell-surface display and fluorescence-activated cell sorting for the identification of novel biocatalysts
    • S. Becker, H.U. Schmoldt, T.M. Adams, S. Wilhelm, and H. Kolmar Ultra-high-throughput screening based on cell-surface display and fluorescence-activated cell sorting for the identification of novel biocatalysts Curr Opin Biotechnol 15 2004 323 329
    • (2004) Curr Opin Biotechnol , vol.15 , pp. 323-329
    • Becker, S.1    Schmoldt, H.U.2    Adams, T.M.3    Wilhelm, S.4    Kolmar, H.5
  • 19
    • 0033908031 scopus 로고    scopus 로고
    • Man-made enzymes-from design to in vitro compartmentalisation
    • A.D. Griffiths, and D.S. Tawfik Man-made enzymes-from design to in vitro compartmentalisation Curr Opin Biotechnol 11 2000 338 353
    • (2000) Curr Opin Biotechnol , vol.11 , pp. 338-353
    • Griffiths, A.D.1    Tawfik, D.S.2
  • 20
    • 1842578052 scopus 로고    scopus 로고
    • GigaMatrix: A novel ultrahigh throughput protein optimization and discovery platform
    • M. Lafferty, and M.J. Dycaico GigaMatrix: a novel ultrahigh throughput protein optimization and discovery platform Methods Enzymol 388 2004 119 134
    • (2004) Methods Enzymol , vol.388 , pp. 119-134
    • Lafferty, M.1    Dycaico, M.J.2
  • 21
    • 0042926892 scopus 로고    scopus 로고
    • Phage display as a tool for the directed evolution of enzymes
    • A. Fernandez-Gacio, M. Uguen, and J. Fastrez Phage display as a tool for the directed evolution of enzymes Trends Biotechnol 21 2003 408 414
    • (2003) Trends Biotechnol , vol.21 , pp. 408-414
    • Fernandez-Gacio, A.1    Uguen, M.2    Fastrez, J.3
  • 22
    • 0029008514 scopus 로고
    • Glutathione transferases with novel active sites isolated by phage display from a library of random mutants
    • M. Widersten, and B. Mannervik Glutathione transferases with novel active sites isolated by phage display from a library of random mutants J Mol Biol 250 1995 115 122
    • (1995) J Mol Biol , vol.250 , pp. 115-122
    • Widersten, M.1    Mannervik, B.2
  • 24
    • 0033578390 scopus 로고    scopus 로고
    • Selection for improved subtiligases by phage display
    • S. Atwell, and J.A. Wells Selection for improved subtiligases by phage display Proc Natl Acad Sci USA 96 1999 9497 9502
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 9497-9502
    • Atwell, S.1    Wells, J.A.2
  • 25
    • 0038023153 scopus 로고    scopus 로고
    • Turnover-based in vitro selection and evolution of biocatalysts from a fully synthetic antibody library
    • S. Cesaro-Tadic, D. Lagos, A. Honegger, J.H. Rickard, L.J. Partridge, G.M. Blackburn, and A. Pluckthun Turnover-based in vitro selection and evolution of biocatalysts from a fully synthetic antibody library Nat Biotechnol 21 2003 679 685 A recent advance in the application of phage display to the directed evolution of enzymatic catalysts. The article describes the selection of efficient catalytic antibodies exhibiting alkaline phosphatase activity under turnover conditions.
    • (2003) Nat Biotechnol , vol.21 , pp. 679-685
    • Cesaro-Tadic, S.1    Lagos, D.2    Honegger, A.3    Rickard, J.H.4    Partridge, L.J.5    Blackburn, G.M.6    Pluckthun, A.7
  • 26
    • 1642279542 scopus 로고    scopus 로고
    • A catalysis-based selection for peroxidase antibodies with increased activity
    • J. Yin, J.H. Mills, and P.G. Schultz A catalysis-based selection for peroxidase antibodies with increased activity J Am Chem Soc 126 2004 3006 3007
    • (2004) J Am Chem Soc , vol.126 , pp. 3006-3007
    • Yin, J.1    Mills, J.H.2    Schultz, P.G.3
  • 27
    • 0033582608 scopus 로고    scopus 로고
    • A strategy for the isolation of catalytic activities from repertoires of enzymes displayed on phage
    • S. Demartis, A. Huber, F. Viti, L. Lozzi, L. Giovannoni, P. Neri, G. Winter, and D. Neri A strategy for the isolation of catalytic activities from repertoires of enzymes displayed on phage J Mol Biol 286 1999 617 633
    • (1999) J Mol Biol , vol.286 , pp. 617-633
    • Demartis, S.1    Huber, A.2    Viti, F.3    Lozzi, L.4    Giovannoni, L.5    Neri, P.6    Winter, G.7    Neri, D.8
  • 28
    • 0033583548 scopus 로고    scopus 로고
    • A method for the selection of catalytic activity using phage display and proximity coupling
    • J.L. Jestin, P. Kristensen, and G. Winter A method for the selection of catalytic activity using phage display and proximity coupling Angew Chem Int Ed 38 1999 1124 1127
    • (1999) Angew Chem Int Ed , vol.38 , pp. 1124-1127
    • Jestin, J.L.1    Kristensen, P.2    Winter, G.3
  • 29
    • 0043237806 scopus 로고    scopus 로고
    • In vitro selection for enzymatic activity: A model study using adenylate cyclase
    • H. Strobel, D. Ladant, and J.L. Jestin In vitro selection for enzymatic activity: a model study using adenylate cyclase J Mol Biol 332 2003 1 7 This article describes a strategy for selection of adenylate cyclase displayed on phage. A model selection was based on covalent attachment of the substrate to the phage particle, and affinity purification of phages linked to the cAMP product.
    • (2003) J Mol Biol , vol.332 , pp. 1-7
    • Strobel, H.1    Ladant, D.2    Jestin, J.L.3
  • 30
    • 0037076311 scopus 로고    scopus 로고
    • Directed evolution of novel polymerase activities: Mutation of a DNA polymerase into an efficient RNA polymerase
    • G. Xia, L. Chen, T. Sera, M. Fa, P.G. Schultz, and F.E. Romesberg Directed evolution of novel polymerase activities: mutation of a DNA polymerase into an efficient RNA polymerase Proc Natl Acad Sci USA 99 2002 6597 6602
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 6597-6602
    • Xia, G.1    Chen, L.2    Sera, T.3    Fa, M.4    Schultz, P.G.5    Romesberg, F.E.6
  • 31
    • 1242314258 scopus 로고    scopus 로고
    • Expanding the substrate repertoire of a DNA polymerase by directed evolution
    • M. Fa, A. Radeghieri, A.A. Henry, and F.E. Romesberg Expanding the substrate repertoire of a DNA polymerase by directed evolution J Am Chem Soc 126 2004 1748 1754 The article describes recent advances in the directed evolution of DNA polymerases using phage display. New polymerase variants were selected for their ability to incorporate unnatural nucleotide analogues.
    • (2004) J Am Chem Soc , vol.126 , pp. 1748-1754
    • Fa, M.1    Radeghieri, A.2    Henry, A.A.3    Romesberg, F.E.4
  • 32
    • 0035795425 scopus 로고    scopus 로고
    • Selection of metalloenzymes by catalytic activity using phage display and catalytic elution
    • I. Ponsard, M. Galleni, P. Soumillion, and J. Fastrez Selection of metalloenzymes by catalytic activity using phage display and catalytic elution ChemBioChem 2 2001 253 259
    • (2001) ChemBioChem , vol.2 , pp. 253-259
    • Ponsard, I.1    Galleni, M.2    Soumillion, P.3    Fastrez, J.4
  • 34
    • 0642334596 scopus 로고    scopus 로고
    • Enhanced crossover SCRATCHY: Construction and high-throughput screening of a combinatorial library containing multiple non-homologous crossovers
    • Y. Kawarasaki, K.E. Griswold, J.D. Stevenson, T. Selzer, S.J. Benkovic, B.L. Iverson, and G. Georgiou Enhanced crossover SCRATCHY: construction and high-throughput screening of a combinatorial library containing multiple non-homologous crossovers Nucl Acid Res 31 2003 A library of chimeras of two glutathione S-transferase (GST) genes exhibiting low homology was constructed. The library was cloned into E. coli, and cells were sorted by flow cytometry (FACS) using a fluorogenic product that was contained within the cells.
    • (2003) Nucl Acid Res , vol.31
    • Kawarasaki, Y.1    Griswold, K.E.2    Stevenson, J.D.3    Selzer, T.4    Benkovic, S.J.5    Iverson, B.L.6    Georgiou, G.7
  • 36
  • 37
    • 1842578294 scopus 로고    scopus 로고
    • Screening of large protein libraries by the cell immobilized on adsorbed bead approach
    • A. Freeman, N. Cohen-Hadar, S. Abramov, R. Modai-Hod, Y. Dror, and G. Georgiou Screening of large protein libraries by the cell immobilized on adsorbed bead approach Biotechnol Bioeng 86 2004 196 200 A new HTS approach is described based on growth of bacterial micro-colonies on beads, and screening with a chromogenic or fluorogenic substrate.
    • (2004) Biotechnol Bioeng , vol.86 , pp. 196-200
    • Freeman, A.1    Cohen-Hadar, N.2    Abramov, S.3    Modai-Hod, R.4    Dror, Y.5    Georgiou, G.6
  • 38
    • 0019874718 scopus 로고
    • Changes in the substrate specificities of an enzyme during directed evolution of new functions
    • B.G. Hall Changes in the substrate specificities of an enzyme during directed evolution of new functions Biochemistry 20 1981 4042 4049
    • (1981) Biochemistry , vol.20 , pp. 4042-4049
    • Hall, B.G.1
  • 39
    • 2542529286 scopus 로고    scopus 로고
    • A new activity for an old enzyme: Escerichia coli bacterial alkaline phosphatase is a phosphite-dependent hydrogenase
    • K. Yang, and W.W. Metcalf A new activity for an old enzyme: Escerichia coli bacterial alkaline phosphatase is a phosphite-dependent hydrogenase Proc Natl Acad Sci USA 101 2004 7919 7924 Engineered E. coli strains using transposon mutagenesis were used to identify a promiscuous activity of alkaline phosphatase.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 7919-7924
    • Yang, K.1    Metcalf, W.W.2
  • 40
    • 2542594077 scopus 로고    scopus 로고
    • Identifying latent enzyme activities: Substrate ambiguity within modern bacterial sugar kinases
    • •]). A bacterium strain was generated in which glucose phosphorylation enzymes were knocked out so that this strain cannot utilize glucose. A plasmid-encoded genomic library of E. coli was transformed and expressed from a strong promoter. Selection on glucose as the sole carbon source led to the identification of three E. coli genes that can complement the auxotrophy of this strain. The corresponding proteins function as glucokinases but promiscuously catalyze the phosphorylation of glucose.
    • (2004) Biochemistry , vol.43 , pp. 6387-6392
    • Miller, B.G.1    Raines, R.T.2
  • 42
    • 9344270529 scopus 로고    scopus 로고
    • Directed Evolution of a Glycosynthase via Chemical Complementation
    • H. Lin, H. Tao, and V. Cornish Directed Evolution of a Glycosynthase via Chemical Complementation J Am Chem Soc 126 2004 15051 15059 A recent expansion of the 'chemical complementation' approach for enzyme selections using the 3-hybrid system in yeast. A selection from a small library of glycosynthase variants was demonstrated.
    • (2004) J Am Chem Soc , vol.126 , pp. 15051-15059
    • Lin, H.1    Tao, H.2    Cornish, V.3
  • 43
    • 0031854986 scopus 로고    scopus 로고
    • Man-made cell-like compartments for molecular evolution
    • D.S. Tawfik, and A.D. Griffiths Man-made cell-like compartments for molecular evolution Nat Biotechnol 16 1998 652 656
    • (1998) Nat Biotechnol , vol.16 , pp. 652-656
    • Tawfik, D.S.1    Griffiths, A.D.2
  • 44
    • 0037413687 scopus 로고    scopus 로고
    • Directed evolution of an extremely fast phosphotriesterase by in vitro compartmentalization
    • 7 variants led to the isolation of a mutant of bacterial phosphotriesterase with an extremely fast turnover rate.
    • (2003) EMBO J , vol.22 , pp. 24-35
    • Griffiths, A.D.1    Tawfik, D.S.2
  • 45
    • 0037112614 scopus 로고    scopus 로고
    • Investigating the target recognition of DNA cytosine-5 methyltransferase HhaI by library selection using in vitro compartmentalisation
    • Y.F. Lee, D.S. Tawfik, and A.D. Griffiths Investigating the target recognition of DNA cytosine-5 methyltransferase HhaI by library selection using in vitro compartmentalisation Nucleic Acids Res 30 2002 4937 4944
    • (2002) Nucleic Acids Res , vol.30 , pp. 4937-4944
    • Lee, Y.F.1    Tawfik, D.S.2    Griffiths, A.D.3
  • 46
    • 0842313326 scopus 로고    scopus 로고
    • Altering the sequence specificity of HaeIII methyltransferase by directed evolution using in vitro compartmentalization
    • H.M. Cohen, D.S. Tawfik, and A.D. Griffiths Altering the sequence specificity of HaeIII methyltransferase by directed evolution using in vitro compartmentalization Protein Eng Des Sel 17 2004 3 11 Selection by in vitro compartmentalization led to a DNA methyltransferase with a broad DNA target specificity and the ability to methylate non-palindromic DNA targets.
    • (2004) Protein Eng des Sel , vol.17 , pp. 3-11
    • Cohen, H.M.1    Tawfik, D.S.2    Griffiths, A.D.3
  • 47
    • 3042855579 scopus 로고    scopus 로고
    • In vitro selection of restriction endonucleases by in vitro compartmentalization
    • N. Doi, S. Kumadaki, Y. Oishi, N. Matsumura, and H. Yanagawa In vitro selection of restriction endonucleases by in vitro compartmentalization Nucleic Acids Res 32 2004 e95 The application of in vitro compartmentalization (IVC) for the selection of libraries of the restriction endonuclease FokI has been demonstrated.
    • (2004) Nucleic Acids Res , vol.32 , pp. 95
    • Doi, N.1    Kumadaki, S.2    Oishi, Y.3    Matsumura, N.4    Yanagawa, H.5
  • 48
    • 0035836707 scopus 로고    scopus 로고
    • Directed evolution of polymerase function by compartmentalized self-replication
    • F.J. Ghadessy, J.L. Ong, and P. Holliger Directed evolution of polymerase function by compartmentalized self-replication Proc Natl Acad Sci USA 98 2001 4552 4557
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 4552-4557
    • Ghadessy, F.J.1    Ong, J.L.2    Holliger, P.3
  • 49
    • 2542525398 scopus 로고    scopus 로고
    • Generic expansion of the substrate spectrum of a DNA polymerase by directed evolution
    • F.J. Ghadessy, N. Ramsay, F. Boudsocq, D. Loakes, A. Brown, S. Iwai, A. Vaisman, R. Woodgate, and P. Holliger Generic expansion of the substrate spectrum of a DNA polymerase by directed evolution Nat Biotechnol 22 2004 755 759 Taq polymerase variants that can extend mismatches and efficiently incorporate a variety of unnatural base analogues were selected using in vitro compartmentalization (IVC).
    • (2004) Nat Biotechnol , vol.22 , pp. 755-759
    • Ghadessy, F.J.1    Ramsay, N.2    Boudsocq, F.3    Loakes, D.4    Brown, A.5    Iwai, S.6    Vaisman, A.7    Woodgate, R.8    Holliger, P.9
  • 50
    • 18744362702 scopus 로고    scopus 로고
    • Microbead display by in vitro compartmentalisation: Selection for binding using flow cytometry
    • A. Sepp, D.S. Tawfik, and A.D. Griffiths Microbead display by in vitro compartmentalisation: selection for binding using flow cytometry FEBS Lett 532 2002 455 458
    • (2002) FEBS Lett , vol.532 , pp. 455-458
    • Sepp, A.1    Tawfik, D.S.2    Griffiths, A.D.3
  • 52
    • 0032772534 scopus 로고    scopus 로고
    • STABLE: Protein-DNA fusion system for screening of combinatorial protein libraries in vitro
    • N. Doi, and H. Yanagawa STABLE: protein-DNA fusion system for screening of combinatorial protein libraries in vitro FEBS Lett 457 1999 227 230
    • (1999) FEBS Lett , vol.457 , pp. 227-230
    • Doi, N.1    Yanagawa, H.2
  • 53
    • 11844273937 scopus 로고    scopus 로고
    • Directed evolution of protein inhibitors of DNA-nucleases by in vitro compartmentalization (IVC) and nanodroplet delivery
    • in press.
    • Bernath K, Magdassi S, Tawfik DS: Directed evolution of protein inhibitors of DNA-nucleases by in vitro compartmentalization (IVC) and nanodroplet delivery. J Mol Biol 2005, in press.
    • (2005) J Mol Biol
    • Bernath, K.1    Magdassi, S.2    Tawfik, D.S.3
  • 55
    • 3042647616 scopus 로고    scopus 로고
    • Anchored periplasmic expression, a versatile technology for the isolation of high-affinity antibodies from Escherichia coli-expressed libraries
    • B.R. Harvey, G. Georgiou, A. Hayhurst, K.J. Jeong, B.L. Iverson, and G.K. Rogers Anchored periplasmic expression, a versatile technology for the isolation of high-affinity antibodies from Escherichia coli-expressed libraries Proc Natl Acad Sci USA 101 2004 9193 9198
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 9193-9198
    • Harvey, B.R.1    Georgiou, G.2    Hayhurst, A.3    Jeong, K.J.4    Iverson, B.L.5    Rogers, G.K.6


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