메뉴 건너뛰기




Volumn 11, Issue 4, 2000, Pages 325-330

Designed evolution of enzymatic properties

Author keywords

[No Author keywords available]

Indexed keywords

ENZYME; UNSPECIFIC MONOOXYGENASE;

EID: 0033908030     PISSN: 09581669     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0958-1669(00)00107-5     Document Type: Review
Times cited : (153)

References (39)
  • 3
    • 0033976143 scopus 로고    scopus 로고
    • Directed evolution of enantioselective enzymes for organic chemistry
    • Jaeger K.E., Reetz M.T. Directed evolution of enantioselective enzymes for organic chemistry. Curr Opin Chem Biol. 4:2000;68-73.
    • (2000) Curr Opin Chem Biol , vol.4 , pp. 68-73
    • Jaeger, K.E.1    Reetz, M.T.2
  • 4
    • 0027205210 scopus 로고
    • Tuning the activity of an enzyme for unusual environments - sequential random mutagenesis of subtilisin E for catalysis in dimethylformamide
    • Chen K.Q., Arnold F.H. Tuning the activity of an enzyme for unusual environments - sequential random mutagenesis of subtilisin E for catalysis in dimethylformamide. Proc Natl Acad Sci USA. 90:1993;5618-5622.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 5618-5622
    • Chen, K.Q.1    Arnold, F.H.2
  • 5
    • 0032491867 scopus 로고    scopus 로고
    • Creation of enantioselective biocatalysts for organic chemistry by in vitro evolution
    • Reetz M.T., Zonta A., Schimossek K., Liebeton K., Jaeger K.E. Creation of enantioselective biocatalysts for organic chemistry by in vitro evolution. Angew Chem Int Ed Engl. 36:1997;2830-2832.
    • (1997) Angew Chem Int Ed Engl , vol.36 , pp. 2830-2832
    • Reetz, M.T.1    Zonta, A.2    Schimossek, K.3    Liebeton, K.4    Jaeger, K.E.5
  • 6
    • 0028050350 scopus 로고
    • Rapid evolution of a protein in vitro by DNA shuffling
    • Stemmer W.P.C. Rapid evolution of a protein in vitro by DNA shuffling. Nature. 370:1994;389-391.
    • (1994) Nature , vol.370 , pp. 389-391
    • Stemmer, W.P.C.1
  • 7
    • 0031909113 scopus 로고    scopus 로고
    • Molecular evolution by staggered extension process (StEP) in vitro recombination
    • Zhao H., Giver L., Affholter J.A., Arnold F.H. Molecular evolution by staggered extension process (StEP) in vitro recombination. Nat Biotechnol. 16:1998;258-261.
    • (1998) Nat Biotechnol , vol.16 , pp. 258-261
    • Zhao, H.1    Giver, L.2    Affholter, J.A.3    Arnold, F.H.4
  • 8
    • 0032518266 scopus 로고    scopus 로고
    • DNA shuffling of a family of genes from diverse species accelerates directed evolution
    • Crameri A., Raillard S.A., Bermudez E., Stemmer W.P.C. DNA shuffling of a family of genes from diverse species accelerates directed evolution. Nature. 391:1998;288-291.
    • (1998) Nature , vol.391 , pp. 288-291
    • Crameri, A.1    Raillard, S.A.2    Bermudez, E.3    Stemmer, W.P.C.4
  • 9
    • 0033578095 scopus 로고    scopus 로고
    • Laboratory evolution of peroxide-mediated cytochrome P450 hydroxylation
    • The rapid evolution of a cofactor-free monooxygenase is achieved with the aid of a well-designed, high-throughput screen.
    • Joo H., Lin Z., Arnold F.H. Laboratory evolution of peroxide-mediated cytochrome P450 hydroxylation. Nature. 399:1999;670-673. The rapid evolution of a cofactor-free monooxygenase is achieved with the aid of a well-designed, high-throughput screen.
    • (1999) Nature , vol.399 , pp. 670-673
    • Joo, H.1    Lin, Z.2    Arnold, F.H.3
  • 10
    • 0033214642 scopus 로고    scopus 로고
    • The power of evolution: Accessing the synthetic potential of P450s
    • Roberts G.C.K. The power of evolution: accessing the synthetic potential of P450s. Chem Biol. 6:1999;R269-R272.
    • (1999) Chem Biol , vol.6
    • Roberts, G.C.K.1
  • 11
    • 0033213940 scopus 로고    scopus 로고
    • A high-throughput digital imaging screen for the discovery and directed evolution of oxygenases
    • Joo H., Arisawa A., Lin Z., Arnold F.H. A high-throughput digital imaging screen for the discovery and directed evolution of oxygenases. Chem Biol. 6:1999;699-706.
    • (1999) Chem Biol , vol.6 , pp. 699-706
    • Joo, H.1    Arisawa, A.2    Lin, Z.3    Arnold, F.H.4
  • 12
    • 0032738825 scopus 로고    scopus 로고
    • A microfabricated fluorescence-activated cell sorter
    • Describes construction of a disposable, microfabricated fluorescence-activated cell sorter that can be used to screen microbial libraries.
    • Fu A.Y., Spence C., Scherer A., Arnold F.H., Quake S.R. A microfabricated fluorescence-activated cell sorter. Nat Biotechnol. 17:1999;1109-1111. Describes construction of a disposable, microfabricated fluorescence-activated cell sorter that can be used to screen microbial libraries.
    • (1999) Nat Biotechnol , vol.17 , pp. 1109-1111
    • Fu, A.Y.1    Spence, C.2    Scherer, A.3    Arnold, F.H.4    Quake, S.R.5
  • 13
    • 0034088553 scopus 로고    scopus 로고
    • Functional expression of horseradish peroxidase in Saccharomyces cerevisiae and Pichia pastoris
    • in press.
    • Morawski B., Lin Z., Cirino P., Joo H., Bandara G., Arnold F.H. Functional expression of horseradish peroxidase in Saccharomyces cerevisiae and Pichia pastoris. Protein Eng. 2000;. in press.
    • (2000) Protein Eng
    • Morawski, B.1    Lin, Z.2    Cirino, P.3    Joo, H.4    Bandara, G.5    Arnold, F.H.6
  • 14
    • 0028249225 scopus 로고
    • Horseradish peroxidase: The analyst's friend
    • Ryan O., Smyth M.R., Fágáin C.O. Horseradish peroxidase: the analyst's friend. Essays Biochem. 28:1994;129-146.
    • (1994) Essays Biochem , vol.28 , pp. 129-146
    • Ryan, O.1    Smyth, M.R.2    Fágáin, C.O.3
  • 16
    • 0033015460 scopus 로고    scopus 로고
    • Rapid protein-folding assay using green fluorescent protein
    • GFP expressed as a carboxy-terminal fusion to cytosolic proteins acts as a reporter for protein folding and enables identification of variants that fold efficiently in E. coli.
    • Waldo G.S., Standish B.M., Berendzen J., Terwilliger T.C. Rapid protein-folding assay using green fluorescent protein. Nat Biotechnol. 17:1999;691-695. GFP expressed as a carboxy-terminal fusion to cytosolic proteins acts as a reporter for protein folding and enables identification of variants that fold efficiently in E. coli.
    • (1999) Nat Biotechnol , vol.17 , pp. 691-695
    • Waldo, G.S.1    Standish, B.M.2    Berendzen, J.3    Terwilliger, T.C.4
  • 17
    • 0034059496 scopus 로고    scopus 로고
    • Inverting enantioselectivity and increasing total activity of a key enzyme in a multi-enzyme synthesis creates a viable process for production of l-methionine
    • Enantioselectivity of a hydantoinase has been inverted by directed evolution. No hydantoinase with selectivity for the L-hydantoin has yet been found in nature.
    • May O., Nguyen P.T., Arnold F.H. Inverting enantioselectivity and increasing total activity of a key enzyme in a multi-enzyme synthesis creates a viable process for production of l-methionine. Nat Biotechnol. 18:2000;317-320. Enantioselectivity of a hydantoinase has been inverted by directed evolution. No hydantoinase with selectivity for the L-hydantoin has yet been found in nature.
    • (2000) Nat Biotechnol , vol.18 , pp. 317-320
    • May, O.1    Nguyen, P.T.2    Arnold, F.H.3
  • 18
    • 0033553835 scopus 로고    scopus 로고
    • A method for high-throughput screening of enantioselective catalysts
    • Reetz M.T., Becker M.H., Klein H.W., Stockigt D. A method for high-throughput screening of enantioselective catalysts. Angew Chem Int Ed Engl. 38:1999;1758-1761.
    • (1999) Angew Chem Int Ed Engl , vol.38 , pp. 1758-1761
    • Reetz, M.T.1    Becker, M.H.2    Klein, H.W.3    Stockigt, D.4
  • 19
    • 0033553799 scopus 로고    scopus 로고
    • Measurement of enantiomeric excess by kinetic resolution and mass spectrometry
    • Guo J., Wu J., Siuzdak G., Finn M.G. Measurement of enantiomeric excess by kinetic resolution and mass spectrometry. Angew Chem Int Ed Engl. 38:1999;1755-1758.
    • (1999) Angew Chem Int Ed Engl , vol.38 , pp. 1755-1758
    • Guo, J.1    Wu, J.2    Siuzdak, G.3    Finn, M.G.4
  • 20
    • 0032538361 scopus 로고    scopus 로고
    • Time-resolved IR-thermographic detection and screening of enantioselectivity in catalytic reactions
    • Reetz M.T., Becker M.H., Kuhling K.M., Holzwarth A. Time-resolved IR-thermographic detection and screening of enantioselectivity in catalytic reactions. Angew Chem Int Ed Engl. 37:1998;2647-2650.
    • (1998) Angew Chem Int Ed Engl , vol.37 , pp. 2647-2650
    • Reetz, M.T.1    Becker, M.H.2    Kuhling, K.M.3    Holzwarth, A.4
  • 21
    • 0033280672 scopus 로고    scopus 로고
    • Exploring nonnatural evolutionary pathways by saturation mutagenesis: Rapid improvement of protein function
    • Miyazaki K., Arnold F.H. Exploring nonnatural evolutionary pathways by saturation mutagenesis: rapid improvement of protein function. J Mol Evol. 49:1999;716-720.
    • (1999) J Mol Evol , vol.49 , pp. 716-720
    • Miyazaki, K.1    Arnold, F.H.2
  • 22
    • 0034615775 scopus 로고    scopus 로고
    • Directed evolution study of temperature adaptation in a psychrophilic enzyme
    • Although rarely observed in nature, it is physically possible to enhance enzyme thermostability and catalytic activity at low temperature simultaneously.
    • Miyazaki K., Wintrode P.L., Grayling R.A., Rubingh D.N., Arnold F.H. Directed evolution study of temperature adaptation in a psychrophilic enzyme. J Mol Biol. 297:2000;1015-1026. Although rarely observed in nature, it is physically possible to enhance enzyme thermostability and catalytic activity at low temperature simultaneously.
    • (2000) J Mol Biol , vol.297 , pp. 1015-1026
    • Miyazaki, K.1    Wintrode, P.L.2    Grayling, R.A.3    Rubingh, D.N.4    Arnold, F.H.5
  • 25
    • 0034712678 scopus 로고    scopus 로고
    • Tryptophan phosphorescence study of enzyme flexibility and unfolding in laboratory-evolved thermostable esterases
    • Gershenson A., Schauerte J.A., Giver L., Arnold F.H. Tryptophan phosphorescence study of enzyme flexibility and unfolding in laboratory-evolved thermostable esterases. Biochemistry. 39:2000;4658-4665.
    • (2000) Biochemistry , vol.39 , pp. 4658-4665
    • Gershenson, A.1    Schauerte, J.A.2    Giver, L.3    Arnold, F.H.4
  • 27
    • 0033054580 scopus 로고    scopus 로고
    • Directed evolution of the surface chemistry of the reporter enzyme β-glucuronidase
    • A nice example of directed evolution with a surprising solution: only one of the multiple amino acid substitutions that confer glutaraldehyde resistance to GUS occurs at a lysine residue.
    • Matsamura I., Wallingford J.B., Surana N.K., Vize P.D., Ellington A.D. Directed evolution of the surface chemistry of the reporter enzyme β-glucuronidase. Nat Biotechnol. 17:1999;696-701. A nice example of directed evolution with a surprising solution: only one of the multiple amino acid substitutions that confer glutaraldehyde resistance to GUS occurs at a lysine residue.
    • (1999) Nat Biotechnol , vol.17 , pp. 696-701
    • Matsamura, I.1    Wallingford, J.B.2    Surana, N.K.3    Vize, P.D.4    Ellington, A.D.5
  • 28
    • 0034628501 scopus 로고    scopus 로고
    • Directed evolution of new catalytic activity using the α/β-barrel scaffold
    • A remarkable example of evolution of a novel function in the scaffold of an α/β-barrel protein. Critical to the success of this study was the combination of rational and evolutionary design principles.
    • Altamirano M.M., Blackburn J.M., Aguayo C., Fersht A.R. Directed evolution of new catalytic activity using the α/β-barrel scaffold. Nature. 403:2000;617-622. A remarkable example of evolution of a novel function in the scaffold of an α/β-barrel protein. Critical to the success of this study was the combination of rational and evolutionary design principles.
    • (2000) Nature , vol.403 , pp. 617-622
    • Altamirano, M.M.1    Blackburn, J.M.2    Aguayo, C.3    Fersht, A.R.4
  • 29
    • 0032956429 scopus 로고    scopus 로고
    • Engineering a regulatable enzyme for homogenous immunoassays
    • This paper describes how phage display can be exploited to generate regulatable variants of β-lactamase.
    • Legendre D., Soumillon P., Fastrez J. Engineering a regulatable enzyme for homogenous immunoassays. Nat Biotechnol. 17:1999;67-72. This paper describes how phage display can be exploited to generate regulatable variants of β-lactamase.
    • (1999) Nat Biotechnol , vol.17 , pp. 67-72
    • Legendre, D.1    Soumillon, P.2    Fastrez, J.3
  • 30
    • 0032784511 scopus 로고    scopus 로고
    • Design of generic biosensors based on green fluorescent proteins with allosteric sites by directed evolution
    • Doi N., Yanagawa H. Design of generic biosensors based on green fluorescent proteins with allosteric sites by directed evolution. FEBS Lett. 453:1999;305-307.
    • (1999) FEBS Lett , vol.453 , pp. 305-307
    • Doi, N.1    Yanagawa, H.2
  • 31
    • 0033037012 scopus 로고    scopus 로고
    • Directed evolution of thymidine kinase for AZT phosphorylation using DNA family shuffling
    • DNA family shuffling of two genes results in the creation of chimeras with function that is significantly improved over any of the parental enzymes.
    • Christians F.C., Scapozza L., Crameri A., Folkers G., Stemmer W.P.C. Directed evolution of thymidine kinase for AZT phosphorylation using DNA family shuffling. Nat Biotechnol. 17:1999;259-264. DNA family shuffling of two genes results in the creation of chimeras with function that is significantly improved over any of the parental enzymes.
    • (1999) Nat Biotechnol , vol.17 , pp. 259-264
    • Christians, F.C.1    Scapozza, L.2    Crameri, A.3    Folkers, G.4    Stemmer, W.P.C.5
  • 32
    • 0040684812 scopus 로고    scopus 로고
    • Tuning biphenyl dioxygenase for extended substrate specificity
    • Bruhlmann F., Chen W. Tuning biphenyl dioxygenase for extended substrate specificity. Biotechnol Bioeng. 63:1999;544-551.
    • (1999) Biotechnol Bioeng , vol.63 , pp. 544-551
    • Bruhlmann, F.1    Chen, W.2
  • 33
    • 0032814117 scopus 로고    scopus 로고
    • Novel family shuffling methods for the in vitro evolution of enzymes
    • Kikuchi M., Ohnishi K., Harayama S. Novel family shuffling methods for the in vitro evolution of enzymes. Gene. 236:1999;159-167.
    • (1999) Gene , vol.236 , pp. 159-167
    • Kikuchi, M.1    Ohnishi, K.2    Harayama, S.3
  • 34
    • 0032966050 scopus 로고    scopus 로고
    • Improving enzymes for cancer gene therapy
    • Encell L.P., Landis D.M., Loeb L.A. Improving enzymes for cancer gene therapy. Nat Biotechnol. 17:1999;143-147.
    • (1999) Nat Biotechnol , vol.17 , pp. 143-147
    • Encell, L.P.1    Landis, D.M.2    Loeb, L.A.3
  • 35
    • 0032885231 scopus 로고    scopus 로고
    • DNA shuffling of subgenomic sequences of subtilisin
    • Chimeras possessing all combinations of properties of individual parents and chimeras significantly improved over any of the parental enzymes for each single property are identified in a family shuffling library.
    • Ness J.E., Welch M., Giver L., Bueno M., Cherry J.R., Borchert T.V., Stemmer W.P.C., Minshull J. DNA shuffling of subgenomic sequences of subtilisin. Nat Biotechnol. 17:1999;893-896. Chimeras possessing all combinations of properties of individual parents and chimeras significantly improved over any of the parental enzymes for each single property are identified in a family shuffling library.
    • (1999) Nat Biotechnol , vol.17 , pp. 893-896
    • Ness, J.E.1    Welch, M.2    Giver, L.3    Bueno, M.4    Cherry, J.R.5    Borchert, T.V.6    Stemmer, W.P.C.7    Minshull, J.8
  • 37
    • 17444363724 scopus 로고    scopus 로고
    • A combinatorial approach to hybrid enzymes independent of DNA homology
    • The authors describe a method to create functional interspecies hybrids in a manner independent of DNA sequence homology.
    • Ostermeier M., Shim J.H., Benkovic S.J. A combinatorial approach to hybrid enzymes independent of DNA homology. Nat Biotechnol. 17:1999;1205-1209. The authors describe a method to create functional interspecies hybrids in a manner independent of DNA sequence homology.
    • (1999) Nat Biotechnol , vol.17 , pp. 1205-1209
    • Ostermeier, M.1    Shim, J.H.2    Benkovic, S.J.3
  • 38
    • 0032850532 scopus 로고    scopus 로고
    • Incremental truncation as a strategy in the engineering of novel biocatalysts
    • Ostermeier M., Nixon A.E., Benkovic S.J. Incremental truncation as a strategy in the engineering of novel biocatalysts. Bioorg Med Chem. 7:1999;2139-2144.
    • (1999) Bioorg Med Chem , vol.7 , pp. 2139-2144
    • Ostermeier, M.1    Nixon, A.E.2    Benkovic, S.J.3
  • 39
    • 0033567665 scopus 로고    scopus 로고
    • Recombination and chimeragenesis by in vitro heteroduplex formation and in vivo repair
    • Volkov A.A., Shao Z., Arnold F.H. Recombination and chimeragenesis by in vitro heteroduplex formation and in vivo repair. Nucleic Acids Res. 27:1999;e18.
    • (1999) Nucleic Acids Res , vol.27 , pp. 18
    • Volkov, A.A.1    Shao, Z.2    Arnold, F.H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.