메뉴 건너뛰기




Volumn 11, Issue 4, 2000, Pages 338-353

Man-made enzymes - From design to in vitro compartmentalisation

Author keywords

[No Author keywords available]

Indexed keywords

ENZYME;

EID: 0033908031     PISSN: 09581669     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0958-1669(00)00109-9     Document Type: Review
Times cited : (117)

References (84)
  • 1
    • 0019053306 scopus 로고
    • Relationship between structure and function of α/β-proteins
    • Branden C-I. Relationship between structure and function of α/β-proteins. Quart Rev Biophys. 13:1980;317-338.
    • (1980) Quart Rev Biophys , vol.13 , pp. 317-338
    • Branden, C.-I.1
  • 2
    • 85031615417 scopus 로고    scopus 로고
    • Combinatorial design principles in α/β-barrel proteins for the creation of novel biocatalysts
    • in press.
    • Altamirano M.M., Fersht A.R. Combinatorial design principles in α/β-barrel proteins for the creation of novel biocatalysts. Proc Natl Acad Sci USA. 2000;. in press.
    • (2000) Proc Natl Acad Sci USA
    • Altamirano, M.M.1    Fersht, A.R.2
  • 3
    • 0032176603 scopus 로고    scopus 로고
    • Mechanistically diverse enzyme superfamilies: The importance of chemistry in the evolution of catalysis
    • Gerlt J., Babbitt P. Mechanistically diverse enzyme superfamilies: the importance of chemistry in the evolution of catalysis. Curr Opin Chem Biol. 2:1998;607-612.
    • (1998) Curr Opin Chem Biol , vol.2 , pp. 607-612
    • Gerlt, J.1    Babbitt, P.2
  • 5
    • 0032859140 scopus 로고    scopus 로고
    • Evolution of protein function, from a structural perspective
    • Todd A.E., Orengo C.A., Thornton J.M. Evolution of protein function, from a structural perspective. Curr Opin Chem Biol. 3:1999;548-556.
    • (1999) Curr Opin Chem Biol , vol.3 , pp. 548-556
    • Todd, A.E.1    Orengo, C.A.2    Thornton, J.M.3
  • 6
    • 0033037012 scopus 로고    scopus 로고
    • Directed evolution of thymidine kinase for AZT phosphorylation using DNA family shuffling
    • M) towards AZT (versus the natural substrate thymidine) relative to the wild-type viral TKs.
    • M) towards AZT (versus the natural substrate thymidine) relative to the wild-type viral TKs.
    • (1999) Nat Biotechnol , vol.17 , pp. 259-264
    • Christians, F.C.1    Scapozza, L.2    Crameri, A.3    Folkers, G.4    Stemmer, W.P.5
  • 7
    • 0032793110 scopus 로고    scopus 로고
    • Recombinant proteins for genetic disease
    • Russell C.S., Clarke L.A. Recombinant proteins for genetic disease. Clin Genet. 55:1999;389-394.
    • (1999) Clin Genet , vol.55 , pp. 389-394
    • Russell, C.S.1    Clarke, L.A.2
  • 8
    • 0033152865 scopus 로고    scopus 로고
    • Protein evolution by molecular breeding
    • Minshull J., Stemmer W.P. Protein evolution by molecular breeding. Curr Opin Chem Biol. 3:1999;284-290.
    • (1999) Curr Opin Chem Biol , vol.3 , pp. 284-290
    • Minshull, J.1    Stemmer, W.P.2
  • 10
    • 0033951945 scopus 로고    scopus 로고
    • Biotechnology in the 21st century
    • Cantor C.R. Biotechnology in the 21st century. Trends Biotechnol. 18:2000;6-7.
    • (2000) Trends Biotechnol , vol.18 , pp. 6-7
    • Cantor, C.R.1
  • 12
    • 0029969102 scopus 로고    scopus 로고
    • On the failure of de-novo designed peptides as biocatalysts
    • Corey M., Corey E. On the failure of de-novo designed peptides as biocatalysts. Proc Natl Acad Sci USA. 93:1996;11428-11434.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 11428-11434
    • Corey, M.1    Corey, E.2
  • 13
    • 0033117461 scopus 로고    scopus 로고
    • Catalytic promiscuity and the evolution of new enzymatic activities
    • This review describes enzymes and non-catalytic proteins that catalyse reactions other than those involved in their normal biological activities. Promiscuous catalytic activities might have served as 'starting points' for the evolution of new enzymes in nature (via gene duplication and diversification) and could also be used for directed evolution in vitro.
    • O'Brien P.J., Herschlag D. Catalytic promiscuity and the evolution of new enzymatic activities. Chem Biol. 6:1999;R91-R105. This review describes enzymes and non-catalytic proteins that catalyse reactions other than those involved in their normal biological activities. Promiscuous catalytic activities might have served as 'starting points' for the evolution of new enzymes in nature (via gene duplication and diversification) and could also be used for directed evolution in vitro.
    • (1999) Chem Biol , vol.6
    • O'Brien, P.J.1    Herschlag, D.2
  • 14
    • 0031584270 scopus 로고    scopus 로고
    • The rational construction of an antibody against cystatin: Lessons from the crystal structure of an artificial Fab fragment
    • Schiweck W., Skerra A. The rational construction of an antibody against cystatin: lessons from the crystal structure of an artificial Fab fragment. J Mol Biol. 268:1997;934-951.
    • (1997) J Mol Biol , vol.268 , pp. 934-951
    • Schiweck, W.1    Skerra, A.2
  • 15
    • 0031933840 scopus 로고    scopus 로고
    • Strategies for selection of antibodies by phage display
    • Griffiths A.D., Duncan A.R. Strategies for selection of antibodies by phage display. Curr Opin Biotechnol. 9:1998;102-108.
    • (1998) Curr Opin Biotechnol , vol.9 , pp. 102-108
    • Griffiths, A.D.1    Duncan, A.R.2
  • 16
    • 17444363724 scopus 로고    scopus 로고
    • A combinatorial approach to hybrid enzymes independent of DNA homology
    • A novel methodology is described (ITCHY) that creates combinatorial fusion libraries between genes in a manner that is independent of DNA homology (non-homologuous recombination).
    • Ostermeier M., Shim J.H., Benkovic S.J. A combinatorial approach to hybrid enzymes independent of DNA homology. Nat Biotechnol. 17:1999;1205-1209. A novel methodology is described (ITCHY) that creates combinatorial fusion libraries between genes in a manner that is independent of DNA homology (non-homologuous recombination).
    • (1999) Nat Biotechnol , vol.17 , pp. 1205-1209
    • Ostermeier, M.1    Shim, J.H.2    Benkovic, S.J.3
  • 17
    • 0018567632 scopus 로고
    • Theoretical studies of clonal selection: Minimal antibody repertoire size and reliability of self-non-self discrimination
    • Perelson A.S., Oster G.F. Theoretical studies of clonal selection: minimal antibody repertoire size and reliability of self-non-self discrimination. J Theor Biol. 81:1979;645-670.
    • (1979) J Theor Biol , vol.81 , pp. 645-670
    • Perelson, A.S.1    Oster, G.F.2
  • 18
    • 0025739164 scopus 로고
    • Mechanism of allergic cross-reactions-I. Multispecific binding of ligands to a mouse monoclonal anti-DNP IgE antibody
    • Varga J.M., Kalchschmid G., Klein G.F., Fritsch P. Mechanism of allergic cross-reactions-I. Multispecific binding of ligands to a mouse monoclonal anti-DNP IgE antibody. Mol Immunol. 28:1991;641-654.
    • (1991) Mol Immunol , vol.28 , pp. 641-654
    • Varga, J.M.1    Kalchschmid, G.2    Klein, G.F.3    Fritsch, P.4
  • 19
    • 0027414469 scopus 로고
    • Probability model for molecular recognition in biological receptor repertoires: Significance to the olfactory system
    • Lancet D., Sadovsky E., Seidemann E. Probability model for molecular recognition in biological receptor repertoires: significance to the olfactory system. Proc Natl Acad Sci USA. 90:1993;3715-3719.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 3715-3719
    • Lancet, D.1    Sadovsky, E.2    Seidemann, E.3
  • 23
    • 0030807838 scopus 로고    scopus 로고
    • Efficient catalysis of proton transfer by synzymes
    • Hollfelder F., Kirby A.J., Tawfik D.S. Efficient catalysis of proton transfer by synzymes. J Am Chem Soc. 119:1997;9578-9579.
    • (1997) J Am Chem Soc , vol.119 , pp. 9578-9579
    • Hollfelder, F.1    Kirby, A.J.2    Tawfik, D.S.3
  • 24
    • 0001683534 scopus 로고
    • Concluding remarks
    • Perutz M. Concluding remarks. Proc Roy Soc Lon. B167:1967;448.
    • (1967) Proc Roy Soc Lon , vol.167 , pp. 448
    • Perutz, M.1
  • 25
    • 0011112119 scopus 로고
    • Enzyme Structure and Mechanism
    • New York: WH Freeman
    • Fersht A. Enzyme Structure and Mechanism. edn 2:1985;WH Freeman, New York.
    • (1985) Edn 2
    • Fersht, A.1
  • 26
    • 0029793086 scopus 로고    scopus 로고
    • Off-the-shelf proteins that rival tailor-made antibodies as catalysts
    • Hollfelder F., Kirby A.J., Tawfik D.S. Off-the-shelf proteins that rival tailor-made antibodies as catalysts. Nature. 383:1996;60-62.
    • (1996) Nature , vol.383 , pp. 60-62
    • Hollfelder, F.1    Kirby, A.J.2    Tawfik, D.S.3
  • 27
    • 0032853242 scopus 로고    scopus 로고
    • In vitro selection of functional nucleic acids
    • Szostak J.W., Wilson D.S. In vitro selection of functional nucleic acids. Annu Rev Biochem. 68:1999;611-647.
    • (1999) Annu Rev Biochem , vol.68 , pp. 611-647
    • Szostak, J.W.1    Wilson, D.S.2
  • 28
    • 0034708337 scopus 로고    scopus 로고
    • Constructing high complexity synthetic libraries of long ORFs using in vitro selection
    • 13 variants were generated and selected for binding by creating mRNA-peptide fusions. In the future, very large protein and peptide libraries may be made routinely in vitro and selected for binding (Figure 2), and perhaps also for catalysis. For the time being, however, the phage-display libraries used in most binding selections, and in vivo selections for catalysis, rely on much smaller library sizes.
    • 13 variants were generated and selected for binding by creating mRNA-peptide fusions. In the future, very large protein and peptide libraries may be made routinely in vitro and selected for binding (Figure 2), and perhaps also for catalysis. For the time being, however, the phage-display libraries used in most binding selections, and in vivo selections for catalysis, rely on much smaller library sizes.
    • (2000) J Mol Biol , vol.297 , pp. 309-319
    • Cho, G.1    Keefe, A.D.2    Liu, R.3    Wilson, D.S.4    Szostak, J.W.5
  • 29
    • 0034628501 scopus 로고    scopus 로고
    • Directed evolution of new catalytic activity using the alpha/beta-barrel scaffold
    • Phosphoribosylanthranilate isomerase (PRAI) activity was evolved from the scaffold of indole-3-glycerol-phosphate synthase (IGPS). In vitro mutagenesis and recombination followed by in vivo selection in an auxotrophic strain gave a new PRAI with catalytic properties that rival those of natural PRAI.
    • Altamirano M.M., Blackburn J.M., Aguayo C., Fersht A.R. Directed evolution of new catalytic activity using the alpha/beta-barrel scaffold. Nature. 403:2000;617-622. Phosphoribosylanthranilate isomerase (PRAI) activity was evolved from the scaffold of indole-3-glycerol-phosphate synthase (IGPS). In vitro mutagenesis and recombination followed by in vivo selection in an auxotrophic strain gave a new PRAI with catalytic properties that rival those of natural PRAI.
    • (2000) Nature , vol.403 , pp. 617-622
    • Altamirano, M.M.1    Blackburn, J.M.2    Aguayo, C.3    Fersht, A.R.4
  • 30
    • 0033052969 scopus 로고    scopus 로고
    • A hierarchical approach to protein molecular evolution
    • An evolutionary experiment was simulated, in which a binding function was evolved by iterative rounds of mutation and selection starting from completely randomised 'libraries'. The Monte-Carlo simulations demonstrate that nonhomologous recombination is the rate-limiting step in the evolution of fold and binding function.
    • Bogarad L.D., Deem M.W. A hierarchical approach to protein molecular evolution. Proc Natl Acad Sci USA. 96:1999;2591-2595. An evolutionary experiment was simulated, in which a binding function was evolved by iterative rounds of mutation and selection starting from completely randomised 'libraries'. The Monte-Carlo simulations demonstrate that nonhomologous recombination is the rate-limiting step in the evolution of fold and binding function.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 2591-2595
    • Bogarad, L.D.1    Deem, M.W.2
  • 32
    • 0032191388 scopus 로고    scopus 로고
    • Recent advances in producing and selecting functional proteins by using cell-free translation
    • Jermutus L., Ryabova L.A., Pluckthun A. Recent advances in producing and selecting functional proteins by using cell-free translation. Curr Opin Biotechnol. 9:1998;534-548.
    • (1998) Curr Opin Biotechnol , vol.9 , pp. 534-548
    • Jermutus, L.1    Ryabova, L.A.2    Pluckthun, A.3
  • 33
    • 0033152942 scopus 로고    scopus 로고
    • Totally in vitro protein selection using mRNA-protein fusions and ribosome display
    • Roberts R.W. Totally in vitro protein selection using mRNA-protein fusions and ribosome display. Curr Opin Chem Biol. 3:1999;268-273.
    • (1999) Curr Opin Chem Biol , vol.3 , pp. 268-273
    • Roberts, R.W.1
  • 34
  • 35
    • 0031012062 scopus 로고    scopus 로고
    • Display of heterologous proteins on the surface of microorganisms: From the screening of combinatorial libraries to live recombinant vaccines
    • Georgiou G., Stathopoulos C., Daugherty P.S., Nayak A.R., Iverson B.L., Curtiss R. III Display of heterologous proteins on the surface of microorganisms: from the screening of combinatorial libraries to live recombinant vaccines. Nat Biotechnol. 15:1997;29-34.
    • (1997) Nat Biotechnol , vol.15 , pp. 29-34
    • Georgiou, G.1    Stathopoulos, C.2    Daugherty, P.S.3    Nayak, A.R.4    Iverson, B.L.5    Curtiss R. III6
  • 36
    • 0033179060 scopus 로고    scopus 로고
    • In vitro selection of nucleic acids and proteins: What are we learning?
    • Roberts R.W., Ja W.W. In vitro selection of nucleic acids and proteins: what are we learning? Curr Opin Struct Biol. 9:1999;521-529.
    • (1999) Curr Opin Struct Biol , vol.9 , pp. 521-529
    • Roberts, R.W.1    Ja, W.W.2
  • 37
    • 0033578390 scopus 로고    scopus 로고
    • Selection for improved subtiligases by phage display
    • 9 variants) of subtiligase (a mutant of subtilisin that catalyzes the ligation of peptides) was displayed on phage and selected by the 'intramolecular single-turnover' mode (see Figure 3 and text). Some of the selected mutants had increased ligase activity (albeit ~2 fold), but the selection yielded mainly ligases with mutations that are correlated with increased stability and oxidative resistance of the protein.
    • 9 variants) of subtiligase (a mutant of subtilisin that catalyzes the ligation of peptides) was displayed on phage and selected by the 'intramolecular single-turnover' mode (see Figure 3 and text). Some of the selected mutants had increased ligase activity (albeit ~2 fold), but the selection yielded mainly ligases with mutations that are correlated with increased stability and oxidative resistance of the protein.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 9497-9502
    • Atwell, S.1    Wells, J.A.2
  • 39
    • 0033582608 scopus 로고    scopus 로고
    • A strategy for the isolation of catalytic activities from repertoires of enzymes displayed on phage
    • The paper describes model selections of enzymes displayed on phage by the 'intramolecular single-turnover' selection mode (Figure 3). The enzyme-substrate tethering was achieved non-covalently, by displaying calmodulin together with the enzyme and using substrates linked to a calmodulin-binding peptide.
    • Demartis S., Huber A., Viti F., Lozzi L., Giovannoni L., Neri P., Winter G., Neri D. A strategy for the isolation of catalytic activities from repertoires of enzymes displayed on phage. J Mol Biol. 286:1999;617-633. The paper describes model selections of enzymes displayed on phage by the 'intramolecular single-turnover' selection mode (Figure 3). The enzyme-substrate tethering was achieved non-covalently, by displaying calmodulin together with the enzyme and using substrates linked to a calmodulin-binding peptide.
    • (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
  • 40
    • 0033583548 scopus 로고    scopus 로고
    • A method for the selection of catalytic activity using phage display and proximity coupling
    • A model selection for a DNA-polymerase displayed on phage. The enzyme-product tethering was achieved after the reaction (i.e. the substrate was not tethered to the displayed enzyme), by proximity (the product, once formed, reacted with the phage).
    • Jestin J.L., Kristensen P., Winter G. A method for the selection of catalytic activity using phage display and proximity coupling. Angew Chem Int Ed. 38:1999;1124-1127. A model selection for a DNA-polymerase displayed on phage. The enzyme-product tethering was achieved after the reaction (i.e. the substrate was not tethered to the displayed enzyme), by proximity (the product, once formed, reacted with the phage).
    • (1999) Angew Chem Int Ed , vol.38 , pp. 1124-1127
    • Jestin, J.L.1    Kristensen, P.2    Winter, G.3
  • 41
    • 0031854986 scopus 로고    scopus 로고
    • Man-made cell-like compartments for molecular evolution
    • Tawfik D.S., Griffiths A.D. 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
  • 42
  • 44
    • 0001515944 scopus 로고    scopus 로고
    • Pharmaceutical emulsions, double emulsions and microemulsions
    • S. Benita. New York: Marcel Dekker
    • Garti N., Aserin A. Pharmaceutical emulsions, double emulsions and microemulsions. Benita S. Microencapsulation: Methods and Industrial Applications. 1996;411-534 Marcel Dekker, New York.
    • (1996) Microencapsulation: Methods and Industrial Applications , pp. 411-534
    • Garti, N.1    Aserin, A.2
  • 45
    • 0032772534 scopus 로고    scopus 로고
    • STABLE: Protein-DNA fusion system for screening of combinatorial protein libraries in vitro
    • A library of biotinylated DNA, encoding peptides fused to streptavidin, was transcribed and translated in vitro in water-in-oil emulsions [41]. This resulted in a 'protein-DNA fusion' library that was subsequently selected for binding by affinity purification. This work demonstrated the application of in vitro compartmentalisation to create protein-display libraries and select them for binding, albeit with very limited efficiency.
    • Doi N., Yanagawa H. STABLE: protein-DNA fusion system for screening of combinatorial protein libraries in vitro. FEBS Lett. 457:1999;227-230. A library of biotinylated DNA, encoding peptides fused to streptavidin, was transcribed and translated in vitro in water-in-oil emulsions [41]. This resulted in a 'protein-DNA fusion' library that was subsequently selected for binding by affinity purification. This work demonstrated the application of in vitro compartmentalisation to create protein-display libraries and select them for binding, albeit with very limited efficiency.
    • (1999) FEBS Lett , vol.457 , pp. 227-230
    • Doi, N.1    Yanagawa, H.2
  • 46
  • 47
    • 0032509131 scopus 로고    scopus 로고
    • Probing the importance of second sphere residues in an esterolytic antibody by phage display
    • Arkin M.R., Wells J.A. Probing the importance of second sphere residues in an esterolytic antibody by phage display. J Mol Biol. 284:1998;1083-1094.
    • (1998) J Mol Biol , vol.284 , pp. 1083-1094
    • Arkin, M.R.1    Wells, J.A.2
  • 48
    • 0030924508 scopus 로고    scopus 로고
    • Phage display of a catalytic antibody to optimize affinity for transition-state analog binding
    • Baca M., Scanlan T.S., Stephenson R.C., Wells J.A. Phage display of a catalytic antibody to optimize affinity for transition-state analog binding. Proc Natl Acad Sci USA. 94:1997;10063-10068.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 10063-10068
    • Baca, M.1    Scanlan, T.S.2    Stephenson, R.C.3    Wells, J.A.4
  • 49
    • 0029653368 scopus 로고
    • Kinetic and affinity limits on antibodies produced during immune responses
    • Foote J., Eisen H.N. Kinetic and affinity limits on antibodies produced during immune responses. Proc Natl Acad Sci USA. 92:1995;1254-1256.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 1254-1256
    • Foote, J.1    Eisen, H.N.2
  • 50
    • 0029018511 scopus 로고
    • Transition-state stabilization as a measure of the efficiency of antibody catalysis
    • Stewart J.D., Benkovic S.J. Transition-state stabilization as a measure of the efficiency of antibody catalysis. Nature. 375:1995;388-391.
    • (1995) Nature , vol.375 , pp. 388-391
    • Stewart, J.D.1    Benkovic, S.J.2
  • 51
    • 0030093768 scopus 로고    scopus 로고
    • The potential of catalytic antibodies
    • Kirby A.J. The potential of catalytic antibodies. Acta Chemica Scandinavica. 50:1996;203-210.
    • (1996) Acta Chemica Scandinavica , vol.50 , pp. 203-210
    • Kirby, A.J.1
  • 52
    • 0030575802 scopus 로고    scopus 로고
    • Isolation of picomolar affinity anti-c-erbB-2 single-chain Fv by molecular evolution of the complementarity determining regions in the center of the antibody binding site
    • Schier R., McCall A., Adams G.P., Marshall K.W., Merritt H., Yim M., Crawford R.S., Weiner L.M., Marks C., Marks J.D. Isolation of picomolar affinity anti-c-erbB-2 single-chain Fv by molecular evolution of the complementarity determining regions in the center of the antibody binding site. J Mol Biol. 263:1996;551-567.
    • (1996) J Mol Biol , vol.263 , pp. 551-567
    • Schier, R.1    McCall, A.2    Adams, G.P.3    Marshall, K.W.4    Merritt, H.5    Yim, M.6    Crawford, R.S.7    Weiner, L.M.8    Marks, C.9    Marks, J.D.10
  • 53
    • 0029564921 scopus 로고
    • CDR walking mutagenesis for the affinity maturation of a potent human anti-HIV-1 antibody into the picomolar range
    • Yang W.P., Green K., Pinz-Sweeney S., Briones A.T., Burton D.R., Barbas C.F. III CDR walking mutagenesis for the affinity maturation of a potent human anti-HIV-1 antibody into the picomolar range. J Mol Biol. 254:1995;392-403.
    • (1995) J Mol Biol , vol.254 , pp. 392-403
    • Yang, W.P.1    Green, K.2    Pinz-Sweeney, S.3    Briones, A.T.4    Burton, D.R.5    Barbas C.F. III6
  • 54
    • 0032564346 scopus 로고    scopus 로고
    • Ribosome display efficiently selects and evolves high-affinity antibodies in vitro from immune libraries
    • Hanes J., Jermutus L., Weber-Bornhauser S., Bosshard H.R., Pluckthun A. Ribosome display efficiently selects and evolves high-affinity antibodies in vitro from immune libraries. Proc Natl Acad Sci USA. 95:1998;14130-14135.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 14130-14135
    • Hanes, J.1    Jermutus, L.2    Weber-Bornhauser, S.3    Bosshard, H.R.4    Pluckthun, A.5
  • 58
    • 0033576651 scopus 로고    scopus 로고
    • Broadening the aldolase catalytic antibody repertoire by combining reactive immunization and transition state theory: New enantio- And diastereoselectivities
    • 8 (exceptionally high for catalytic antibodies and comparable to natural aldolases) and efficient turnover.
    • 8 (exceptionally high for catalytic antibodies and comparable to natural aldolases) and efficient turnover.
    • (1999) Angew Chem Int Ed , vol.38 , pp. 3738-3741
    • Zhong, G.F.1    Lerner, R.A.2    Barbas, C.F.3
  • 59
    • 0030469331 scopus 로고    scopus 로고
    • Catalytic antibodies - reaching adolescence?
    • Thomas N. Catalytic antibodies - reaching adolescence? Natural Products Rep. 1996;479-511.
    • (1996) Natural Products Rep , pp. 479-511
    • Thomas, N.1
  • 60
    • 0031063010 scopus 로고    scopus 로고
    • In vivo versus in vitro screening or selection for catalytic activity in enzymes and abzymes
    • Fastrez J. In vivo versus in vitro screening or selection for catalytic activity in enzymes and abzymes. Mol Biotechnol. 7:1997;37-55.
    • (1997) Mol Biotechnol , vol.7 , pp. 37-55
    • Fastrez, J.1
  • 61
    • 0030898510 scopus 로고    scopus 로고
    • A general purpose RNA-cleaving DNA enzyme
    • Santoro S.W., Joyce G.F. A general purpose RNA-cleaving DNA enzyme. Proc Natl Acad Sci USA. 94:1997;4262-4266.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 4262-4266
    • Santoro, S.W.1    Joyce, G.F.2
  • 62
    • 0033102314 scopus 로고    scopus 로고
    • A small catalytic RNA motif with Diels-Alderase activity
    • Seelig B., Jaschke A. A small catalytic RNA motif with Diels-Alderase activity. Chem Biol. 6:1999;167-176.
    • (1999) Chem Biol , vol.6 , pp. 167-176
    • Seelig, B.1    Jaschke, A.2
  • 63
    • 0030963855 scopus 로고    scopus 로고
    • RNA-catalysed carbon-carbon bond formation
    • Tarasow T.M., Tarasow S.L., Eaton B.E. RNA-catalysed carbon-carbon bond formation. Nature. 389:1997;54-57.
    • (1997) Nature , vol.389 , pp. 54-57
    • Tarasow, T.M.1    Tarasow, S.L.2    Eaton, B.E.3
  • 65
    • 0029159746 scopus 로고
    • Forced evolution of glutathione S-transferase to create a more efficient drug detoxication enzyme
    • Gulick A.M., Fahl W.E. Forced evolution of glutathione S-transferase to create a more efficient drug detoxication enzyme. Proc Natl Acad Sci USA. 92:1995;8140-8144.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 8140-8144
    • Gulick, A.M.1    Fahl, W.E.2
  • 66
    • 0034059496 scopus 로고    scopus 로고
    • Inverting enantioselectivity by directed evolution of hydantoinase for improved production of L-methionine
    • The enantioselectivity and total activity of hydantoinase was increased by random mutagenesis and screening, thus leading to a significant improvement of a key enzyme in a 'whole-cell catalyst' producing L-methionine.
    • May O., Nguyen P.T., Arnold F.H. Inverting enantioselectivity by directed evolution of hydantoinase for improved production of L-methionine. Nat Biotechnol. 18:2000;317-320. The enantioselectivity and total activity of hydantoinase was increased by random mutagenesis and screening, thus leading to a significant improvement of a key enzyme in a 'whole-cell catalyst' producing L-methionine.
    • (2000) Nat Biotechnol , vol.18 , pp. 317-320
    • May, O.1    Nguyen, P.T.2    Arnold, F.H.3
  • 67
    • 0030864556 scopus 로고    scopus 로고
    • 3D structural information as a guide to protein engineering using genetic selection
    • Kast P., Hilvert D. 3D structural information as a guide to protein engineering using genetic selection. Curr Opin Struct Biol. 7:1997;470-479.
    • (1997) Curr Opin Struct Biol , vol.7 , pp. 470-479
    • Kast, P.1    Hilvert, D.2
  • 68
    • 0030864811 scopus 로고    scopus 로고
    • Combinatorial protein design: Strategies for screening protein libraries
    • Zhao H., Arnold F.H. Combinatorial protein design: strategies for screening protein libraries. Curr Opin Struct Biol. 7:1997;480-485.
    • (1997) Curr Opin Struct Biol , vol.7 , pp. 480-485
    • Zhao, H.1    Arnold, F.H.2
  • 69
    • 0033578095 scopus 로고    scopus 로고
    • Laboratory evolution of peroxide-mediated cytochrome P450 hydroxylation
    • A sensitive throughput screen was applied to select mutants of P450 that hydroxylate naphthalene in the absence of cofactors and with more than 20-fold higher activity than the native enzyme.
    • Joo H., Lin Z., Arnold F.H. Laboratory evolution of peroxide-mediated cytochrome P450 hydroxylation. Nature. 399:1999;670-673. A sensitive throughput screen was applied to select mutants of P450 that hydroxylate naphthalene in the absence of cofactors and with more than 20-fold higher activity than the native enzyme.
    • (1999) Nature , vol.399 , pp. 670-673
    • Joo, H.1    Lin, Z.2    Arnold, F.H.3
  • 70
    • 0026550717 scopus 로고
    • Detection of catalytic monoclonal antibodies
    • Tawfik D.S., Green B.S., Eshhar Z. Detection of catalytic monoclonal antibodies. Anal Biochem. 202:1992;35-39.
    • (1992) Anal Biochem , vol.202 , pp. 35-39
    • Tawfik, D.S.1    Green, B.S.2    Eshhar, Z.3
  • 71
    • 0028178511 scopus 로고
    • Catalytic antibodies: Perusing combinatorial libraries
    • Posner B., Smiley J., Lee I., Benkovic S. Catalytic antibodies: perusing combinatorial libraries. Trends Biochem Sci. 19:1994;145-150.
    • (1994) Trends Biochem Sci , vol.19 , pp. 145-150
    • Posner, B.1    Smiley, J.2    Lee, I.3    Benkovic, S.4
  • 72
    • 0028918401 scopus 로고
    • A proficient enzyme
    • Radzicka A., Wolfenden R. A proficient enzyme. Science. 267:1995;90-93.
    • (1995) Science , vol.267 , pp. 90-93
    • Radzicka, A.1    Wolfenden, R.2
  • 73
    • 15844422678 scopus 로고    scopus 로고
    • The X-ray structure of a transition state analog complex reveals the molecular origins of the catalytic power and substrate specificity of acetylcholinesterase
    • Harel M., Quinn D.M., Nair H.K., Silman I., Sussman J.L. The X-ray structure of a transition state analog complex reveals the molecular origins of the catalytic power and substrate specificity of acetylcholinesterase. J Am Chem Soc. 118:1996;2340-2346.
    • (1996) J Am Chem Soc , vol.118 , pp. 2340-2346
    • Harel, M.1    Quinn, D.M.2    Nair, H.K.3    Silman, I.4    Sussman, J.L.5
  • 74
    • 0025085590 scopus 로고
    • Catalysis of RNA cleavage by the Tetrahymena thermophila ribozyme. 1. Kinetic description of the reaction of an RNA substrate complementary to the active site
    • Herschlag D., Cech T.R. Catalysis of RNA cleavage by the Tetrahymena thermophila ribozyme. 1. Kinetic description of the reaction of an RNA substrate complementary to the active site. Biochemistry. 29:1990;10159-10171.
    • (1990) Biochemistry , vol.29 , pp. 10159-10171
    • Herschlag, D.1    Cech, T.R.2
  • 75
    • 0028349315 scopus 로고
    • Can small cyclic peptides have the activity and specificity of proteolytic enzymes?
    • Matthews B.W., Craik C.S., Neurath H. Can small cyclic peptides have the activity and specificity of proteolytic enzymes? Proc Natl Acad Sci USA. 91:1994;4103-4105.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 4103-4105
    • Matthews, B.W.1    Craik, C.S.2    Neurath, H.3
  • 76
    • 0030954291 scopus 로고    scopus 로고
    • Toward an efficient DNAzyme
    • Li Y., Sen D. Toward an efficient DNAzyme. Biochemistry. 36:1997;5589-5599.
    • (1997) Biochemistry , vol.36 , pp. 5589-5599
    • Li, Y.1    Sen, D.2
  • 77
    • 0000783913 scopus 로고
    • Monovalent phage display: A method for selecting variant proteins from random libraries
    • Lowman H., Wells J. Monovalent phage display: a method for selecting variant proteins from random libraries. Methods: A Companion to Methods in Enzymology. 3:1991;205-216.
    • (1991) Methods: A Companion to Methods in Enzymology , vol.3 , pp. 205-216
    • Lowman, H.1    Wells, J.2
  • 79
    • 0031945007 scopus 로고    scopus 로고
    • Evolving catalytic antibodies in a phage-displayed combinatorial library
    • Fujii I., Fukuyama S., Iwabuchi Y., Tanimura R. Evolving catalytic antibodies in a phage-displayed combinatorial library. Nat Biotechnol. 16:1998;463-467.
    • (1998) Nat Biotechnol , vol.16 , pp. 463-467
    • Fujii, I.1    Fukuyama, S.2    Iwabuchi, Y.3    Tanimura, R.4
  • 80
    • 0025170858 scopus 로고
    • Antibody-catalyzed porphyrin metallation
    • Cochran A.G., Schultz P.G. Antibody-catalyzed porphyrin metallation. Science. 249:1990;781-783.
    • (1990) Science , vol.249 , pp. 781-783
    • Cochran, A.G.1    Schultz, P.G.2
  • 81
    • 0008451711 scopus 로고    scopus 로고
    • Porphyrin metalation catalyzed by a small RNA molecule
    • Conn M.M., Prudent J.R., Schultz P.G. Porphyrin metalation catalyzed by a small RNA molecule. J Am Chem Soc. 118:1996;7012-7013.
    • (1996) J Am Chem Soc , vol.118 , pp. 7012-7013
    • Conn, M.M.1    Prudent, J.R.2    Schultz, P.G.3
  • 82
    • 0029746712 scopus 로고    scopus 로고
    • A catalytic DNA for porphyrin metallation
    • Li Y.F., Sen D. A catalytic DNA for porphyrin metallation. Nat Struct Biol. 3:1996;743-747.
    • (1996) Nat Struct Biol , vol.3 , pp. 743-747
    • Li, Y.F.1    Sen, D.2
  • 84
    • 0030135720 scopus 로고    scopus 로고
    • A general method for the spatially defined immobilization of biomolecules on glass surfaces using "caged" biotin
    • Pirrung M.C., Huang C.Y. A general method for the spatially defined immobilization of biomolecules on glass surfaces using "caged" biotin. Bioconjug Chem. 7:1996;317-321.
    • (1996) Bioconjug Chem , vol.7 , pp. 317-321
    • Pirrung, M.C.1    Huang, C.Y.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.