메뉴 건너뛰기




Volumn 44, Issue 18, 1999, Pages 1641-1648

New strategies of protein engineering - Directed evolution of enzyme in vitro

Author keywords

Directed evolution; Enzyme; Protein engineering

Indexed keywords


EID: 0003398810     PISSN: 10016538     EISSN: None     Source Type: Journal    
DOI: 10.1007/BF03183480     Document Type: Review
Times cited : (4)

References (54)
  • 1
    • 0029969577 scopus 로고    scopus 로고
    • Directed evolution of subtilisin E in Bacillus subtilis to enhance total activity in aqueous dimethylformamide
    • You, L., Arnold, F. H., Directed evolution of subtilisin E in Bacillus subtilis to enhance total activity in aqueous dimethylformamide, Protein Eng., 1996, 9: 77.
    • (1996) Protein Eng. , vol.9 , pp. 77
    • You, L.1    Arnold, F.H.2
  • 2
    • 0002694056 scopus 로고
    • A method for random mutagenesis of a defined DNA segment using a modified polymerase chain reaction
    • Leung, D. W., Chen, E., Goeddel, D. V., A method for random mutagenesis of a defined DNA segment using a modified polymerase chain reaction, Technique, 1989, 1: 11.
    • (1989) Technique , vol.1 , pp. 11
    • Leung, D.W.1    Chen, E.2    Goeddel, D.V.3
  • 3
    • 0028272110 scopus 로고
    • New York: Cold Spring Harbor Laboratory Press
    • Cadwell, R. C., Joyce, G. F., Mutagenic PCR, New York: Cold Spring Harbor Laboratory Press, 1994.
    • (1994) Mutagenic PCR
    • Cadwell, R.C.1    Joyce, G.F.2
  • 4
    • 0026334373 scopus 로고
    • Enzyme engineering for nonaqueous solvents: Random mutagenesis to enhance activity of subtilisin E inpolar organic media
    • Chen, K., Arnold, F. H., Enzyme engineering for nonaqueous solvents: random mutagenesis to enhance activity of subtilisin E inpolar organic media, Bio/Technology, 1991, 9: 1073.
    • (1991) Bio/Technology , vol.9 , pp. 1073
    • Chen, K.1    Arnold, F.H.2
  • 5
    • 0027205210 scopus 로고
    • Tuning the activity of an enzyme for unusual environments: Sequential random mutagenesis of subtilisin E for catalysis in dimethylformamide
    • Chen, K., 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, 1993, 90: 5618.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 5618
    • Chen, K.1    Arnold, F.H.2
  • 6
    • 0028110130 scopus 로고
    • DNA shuffling by random fragmentation and reassembly-in vitro recombination for molecular evolution
    • Stemmer, W. P. C., DNA shuffling by random fragmentation and reassembly-in vitro recombination for molecular evolution, Proc. Natl. Acad. Sci. USA, 1994a, 91: 10747.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 10747
    • Stemmer, W.P.C.1
  • 7
    • 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, 1994b, 340: 389.
    • (1994) Nature , vol.340 , pp. 389
    • Stemmer, W.P.C.1
  • 8
    • 0029821726 scopus 로고    scopus 로고
    • A strategy of exon shuffling for making large peptide repertories displayed on filamentous bacteriophage
    • Fisch, I., Kontermann, R. E., Finnern, R. et al., A strategy of exon shuffling for making large peptide repertories displayed on filamentous bacteriophage, Proc. Natl. Acad. Sci. USA, 1996, 93: 7761.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 7761
    • Fisch, I.1    Kontermann, R.E.2    Finnern, R.3
  • 9
    • 0029001752 scopus 로고
    • Searching sequence space using recombination to search more efficiently and thoroughly instead of making bigger combinational libraries
    • Stemmer, W. P. C., Searching sequence space using recombination to search more efficiently and thoroughly instead of making bigger combinational libraries, Bio/Technology, 1995, 13: 549.
    • (1995) Bio/Technology , vol.13 , pp. 549
    • Stemmer, W.P.C.1
  • 10
    • 0032518266 scopus 로고    scopus 로고
    • DNA shuffling of a family of genes from diverse species accelerates directed evolution
    • Crameri, A. C., Raillard, S., Stemmer, W. P. C., DNA shuffling of a family of genes from diverse species accelerates directed evolution, Nature, 1997, 391: 288.
    • (1997) Nature , vol.391 , pp. 288
    • Crameri, A.C.1    Raillard, S.2    Stemmer, W.P.C.3
  • 11
    • 0030989062 scopus 로고    scopus 로고
    • Evolution of an effective fucosidase from a galactosidase by DNA shuffling
    • Zhang, J., Dawes, G., Stemmer, W. P. C., Evolution of an effective fucosidase from a galactosidase by DNA shuffling, Proc. Natl. Acad. Sci. USA, 1997, 94: 4504.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 4504
    • Zhang, J.1    Dawes, G.2    Stemmer, W.P.C.3
  • 12
    • 0029670577 scopus 로고    scopus 로고
    • Directed evolution of a para-nitrobenzyl esterase
    • Moore, J. C., Arnold, F. H., Directed evolution of a para-nitrobenzyl esterase, Nature Biotechnol., 1996, 14: 458.
    • (1996) Nature Biotechnol. , vol.14 , pp. 458
    • Moore, J.C.1    Arnold, F.H.2
  • 13
    • 0031587291 scopus 로고    scopus 로고
    • Strategies for the in vitro evolution of protein function: Enzyme evolution by random recombination of improved sequences
    • Moore, J. C., Jin, H. M., Kuchner, O. et al., Strategies for the in vitro evolution of protein function: enzyme evolution by random recombination of improved sequences, J. Mol. Biol., 1997, 272: 336.
    • (1997) J. Mol. Biol. , vol.272 , pp. 336
    • Moore, J.C.1    Jin, H.M.2    Kuchner, O.3
  • 14
    • 0030483509 scopus 로고    scopus 로고
    • Directed evolution: Creating biocatalysis for the future
    • Arnold, F. H., Directed evolution: creating biocatalysis for the future, Chemical. Eng. Sci., 1996, 51: 5091.
    • (1996) Chemical. Eng. Sci. , vol.51 , pp. 5091
    • Arnold, F.H.1
  • 16
    • 0030754926 scopus 로고    scopus 로고
    • Optimization of DNA shuffling for high-fidelity recombination
    • Zhao, H. M., Arnold, F. H., Optimization of DNA shuffling for high-fidelity recombination, Nucleic Acids Research, 1997, 25: 1307.
    • (1997) Nucleic Acids Research , vol.25 , pp. 1307
    • Zhao, H.M.1    Arnold, F.H.2
  • 18
    • 0030600761 scopus 로고    scopus 로고
    • Attempt to convert chymotrypsin to trypsin
    • Venekei, I., Szilagyi, L., Graf, L. et al., Attempt to convert chymotrypsin to trypsin, FEBS Lett., 1996, 379: 143.
    • (1996) FEBS Lett. , vol.379 , pp. 143
    • Venekei, I.1    Szilagyi, L.2    Graf, L.3
  • 19
    • 0029913564 scopus 로고    scopus 로고
    • Furilisin: A variant of subtilisin BPN' engineering for cleaving tribasic substrates
    • Ballinger, M. D., Tom, J., Wells, J. A., Furilisin: a variant of subtilisin BPN' engineering for cleaving tribasic substrates, Biochem., 1996, 35: 13579.
    • (1996) Biochem. , vol.35 , pp. 13579
    • Ballinger, M.D.1    Tom, J.2    Wells, J.A.3
  • 20
    • 0002455957 scopus 로고    scopus 로고
    • Strategies for the design of novel proteins
    • ed. Carey, P. R., San Diego: Academic Press
    • Hecht, M. H., Strategies for the design of novel proteins in Protein Engineering and Design (ed. Carey, P. R.), San Diego: Academic Press, 1996.
    • (1996) Protein Engineering and Design
    • Hecht, M.H.1
  • 21
    • 0031027267 scopus 로고    scopus 로고
    • Assembly of an active enzyme by the linkage of two protein modules
    • Nixon, A. E., Werren, M. S., Benkovic, S. J., Assembly of an active enzyme by the linkage of two protein modules, Proc. Natl. Acad. Sci. USA, 1997, 94: 1069.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 1069
    • Nixon, A.E.1    Werren, M.S.2    Benkovic, S.J.3
  • 22
    • 0030998438 scopus 로고    scopus 로고
    • Functional analyses of a variety of chimeric dioxygenases constructed from two biphenyl dioxygenases that are similar structurally but different functionally
    • Kimura, N., Nishi, A., Goto, M. et al., Functional analyses of a variety of chimeric dioxygenases constructed from two biphenyl dioxygenases that are similar structurally but different functionally, J. Bacteriol., 1997, 179(12): 3936.
    • (1997) J. Bacteriol. , vol.179 , Issue.12 , pp. 3936
    • Kimura, N.1    Nishi, A.2    Goto, M.3
  • 23
    • 0030924302 scopus 로고    scopus 로고
    • Resign of soluble fatty acid desaturases from plants for altered substrate specificity and double bond position
    • Cahhon, E. B., Lindqvist, Y., Schneider, G. et al., Resign of soluble fatty acid desaturases from plants for altered substrate specificity and double bond position, Proc. Natl. Acad. Sci. USA., 1997, 94: 4872.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 4872
    • Cahhon, E.B.1    Lindqvist, Y.2    Schneider, G.3
  • 24
    • 0029956966 scopus 로고    scopus 로고
    • Identifying functional domains within terpene cyclases using a domain-swapping strategy
    • Back, K., Chappell, J., Identifying functional domains within terpene cyclases using a domain-swapping strategy, Proc. Natl. Acad. Sci. USA., 1996, 93: 6841.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 6841
    • Back, K.1    Chappell, J.2
  • 25
    • 0028948295 scopus 로고
    • Substrate specificity differences between two catechl 2,3-dioxygenses encoded by the TOL and NAH plasmids from Psendomonas putida
    • Cerdan, P., Rekik, M., Harayama, S., Substrate specificity differences between two catechl 2,3-dioxygenses encoded by the TOL and NAH plasmids from Psendomonas putida, Eur. J. Biochem., 1995, 229: 113.
    • (1995) Eur. J. Biochem. , vol.229 , pp. 113
    • Cerdan, P.1    Rekik, M.2    Harayama, S.3
  • 26
    • 0032518181 scopus 로고    scopus 로고
    • Random-priming in vitro recombination: An effective tool for directed evolution
    • Shao, Z., Zhao, H., Giver, L. et al., Random-priming in vitro recombination: an effective tool for directed evolution, Nucl. Acids Res., 1998, 26: 681.
    • (1998) Nucl. Acids Res. , vol.26 , pp. 681
    • Shao, Z.1    Zhao, H.2    Giver, L.3
  • 27
    • 0031909113 scopus 로고    scopus 로고
    • Molecular evolution by staggered extension process (StEP) in vitro recombination
    • Zhao, H., Giver, L., Shao, Z. et al., Molecular evolution by staggered extension process (StEP) in vitro recombination, Nature Biotech, 1998, 16: 258.
    • (1998) Nature Biotech , vol.16 , pp. 258
    • Zhao, H.1    Giver, L.2    Shao, Z.3
  • 28
    • 0030848174 scopus 로고    scopus 로고
    • Homologous recombination occurs in a distinct retroviral subpopulation and exhibits high negative interference
    • Hu, W. S., Bowman, E. H., Delviks, K. A., Homologous recombination occurs in a distinct retroviral subpopulation and exhibits high negative interference, J. Virol., 1997, 71: 6028.
    • (1997) J. Virol. , vol.71 , pp. 6028
    • Hu, W.S.1    Bowman, E.H.2    Delviks, K.A.3
  • 29
    • 5644271662 scopus 로고
    • An enzymatic method for random-(site-specific) mutagenesis of ginseng peptide gene in vitro
    • Zhang, J., Li, Z. Q., Zhang, H. Y., An enzymatic method for random-(site-specific) mutagenesis of ginseng peptide gene in vitro, Chinese Biochem. J. (in Chinese), 1992, 8(1): 115.
    • (1992) Chinese Biochem. J. (in Chinese) , vol.8 , Issue.1 , pp. 115
    • Zhang, J.1    Li, Z.Q.2    Zhang, H.Y.3
  • 30
    • 0003468238 scopus 로고
    • Enzymatic generation of libraries in vitro for random mutagenesis of the aspartase gene
    • Zhang, H. Y., Li, Z. Q., Zhang, J. et al., Enzymatic generation of libraries in vitro for random mutagenesis of the aspartase gene, Chinese Science Buletin, 1992, 37: 598
    • (1992) Chinese Science Buletin , vol.37 , pp. 598
    • Zhang, H.Y.1    Li, Z.Q.2    Zhang, J.3
  • 31
    • 0027177736 scopus 로고
    • Enhancement of the stability and activity of aspartase by random and site-directed mutagenesis
    • Zhang, H. Y., Zhang, J., Lin, L. et al., Enhancement of the stability and activity of aspartase by random and site-directed mutagenesis, BBRC, 1993, 192(1): 15.
    • (1993) BBRC , vol.192 , Issue.1 , pp. 15
    • Zhang, H.Y.1    Zhang, J.2    Lin, L.3
  • 33
    • 0030858562 scopus 로고    scopus 로고
    • Functional and nonfunctional mutations distinguished by random recombination of homologous genes
    • Zhao, H., Arnold, F. H., Functional and nonfunctional mutations distinguished by random recombination of homologous genes, Proc. Natl. Acad. Sci. USA, 1997, 94: 7997.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 7997
    • Zhao, H.1    Arnold, F.H.2
  • 34
    • 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., 1997, 7: 480.
    • (1997) Curr. Opin. Struct. Biol. , vol.7 , pp. 480
    • Zhao, H.1    Arnold, F.H.2
  • 35
    • 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., 1997, 7: 470.
    • (1997) Curr. Opin. Struct. Biol. , vol.7 , pp. 470
    • Kast, P.1    Hilvert, D.2
  • 36
    • 0029996325 scopus 로고    scopus 로고
    • A rapid and effective procedure for screening protease mutants
    • Venekei, I., Hedstrom, L., Rutter, W. J., A rapid and effective procedure for screening protease mutants, Protein Eng., 1996, 9: 85.
    • (1996) Protein Eng. , vol.9 , pp. 85
    • Venekei, I.1    Hedstrom, L.2    Rutter, W.J.3
  • 37
    • 0029102175 scopus 로고
    • Phage display: Protein engineering by directed evolution
    • O'Neil, K. T., Hoess, R. H., Phage display: protein engineering by directed evolution, Curr. Opin. Struct. Biol., 1995, 5: 443.
    • (1995) Curr. Opin. Struct. Biol. , vol.5 , pp. 443
    • O'Neil, K.T.1    Hoess, R.H.2
  • 38
    • 0026568164 scopus 로고
    • Directed evolution of a protein: Selection of potent neutrophil elastase inhibitors displayed on M13 fusion phage
    • Roberts, B. L., Markland, W., Arthur, C. et al., Directed evolution of a protein: selection of potent neutrophil elastase inhibitors displayed on M13 fusion phage, Proc. Natl. Acad. Sci. USA, 1992, 89: 2429.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 2429
    • Roberts, B.L.1    Markland, W.2    Arthur, C.3
  • 39
    • 0030974119 scopus 로고    scopus 로고
    • In vitro selection and evolution of functional proteins by using ribosome display
    • Manes, J., Pluckthun, A., In vitro selection and evolution of functional proteins by using ribosome display, Proc. Natl. Acad. Sci. USA, 1997, 94: 4937.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 4937
    • Manes, J.1    Pluckthun, A.2
  • 40
    • 0030016226 scopus 로고    scopus 로고
    • A rapid screen of active site mutants in glycinamide ribonucleotide
    • Warren, M. S., Marolewski, A. E., Beukovic, S. J., A rapid screen of active site mutants in glycinamide ribonucleotide, Biochem., 1996, 35: 8855.
    • (1996) Biochem. , vol.35 , pp. 8855
    • Warren, M.S.1    Marolewski, A.E.2    Beukovic, S.J.3
  • 41
    • 0029670330 scopus 로고    scopus 로고
    • Improved green fluorescent protein by molecular evolution using DNA shuffling
    • Crameri, A., Whitehorn, E. A., Tale, E. et al., Improved green fluorescent protein by molecular evolution using DNA shuffling, Nature Biotechnol, 1996, 14: 315.
    • (1996) Nature Biotechnol , vol.14 , pp. 315
    • Crameri, A.1    Whitehorn, E.A.2    Tale, E.3
  • 42
    • 0032007562 scopus 로고    scopus 로고
    • Artificial evolution by DNA shuffling
    • Harayama, S., Artificial evolution by DNA shuffling, Trends Biotech., 1998, 16: 76.
    • (1998) Trends Biotech. , vol.16 , pp. 76
    • Harayama, S.1
  • 43
    • 0030220851 scopus 로고    scopus 로고
    • Engineering new function and altering existing functions
    • Shao, Z., Arnold, F. H., Engineering new function and altering existing functions, Curr. Opin. Struct. Biol., 1996, 6: 513.
    • (1996) Curr. Opin. Struct. Biol. , vol.6 , pp. 513
    • Shao, Z.1    Arnold, F.H.2
  • 44
    • 0031543435 scopus 로고    scopus 로고
    • Directed evolution of enzyme catalysts
    • Kuchner, O., Arnold, F. H., Directed evolution of enzyme catalysts, Trends Biotech., 1997, 15: 523.
    • (1997) Trends Biotech. , vol.15 , pp. 523
    • Kuchner, O.1    Arnold, F.H.2
  • 45
    • 0030951186 scopus 로고    scopus 로고
    • Molecular evolution of an arsenate detoxification pathway by DNA shuffling
    • Crameri, A., Dawes, G., Rodrigues, E. J. et al., Molecular evolution of an arsenate detoxification pathway by DNA shuffling, Nature Biotechnol., 1997, 15: 436.
    • (1997) Nature Biotechnol. , vol.15 , pp. 436
    • Crameri, A.1    Dawes, G.2    Rodrigues, E.J.3
  • 46
    • 0028877429 scopus 로고
    • The directed evolution of radiation resistance in E. coli
    • Ewing, D., The directed evolution of radiation resistance in E. coli, Biochem. Biophys. Res. Commun., 1995, 216: 549.
    • (1995) Biochem. Biophys. Res. Commun. , vol.216 , pp. 549
    • Ewing, D.1
  • 47
  • 48
    • 0347770044 scopus 로고    scopus 로고
    • Biocatalysis for chiral intermediates: Meeting commercial and technical challenges
    • Matcham, G. W., Bowen, A. R. S., Biocatalysis for chiral intermediates: meeting commercial and technical challenges, Chem. Today, 1996, 14: 20.
    • (1996) Chem. Today , vol.14 , pp. 20
    • Matcham, G.W.1    Bowen, A.R.S.2
  • 49
    • 0030048583 scopus 로고    scopus 로고
    • Construction and evolution of antibody-phage libraries by DNA shuffling
    • Crameri, A., Cwirla, S., Stemmer, W. P. C., Construction and evolution of antibody-phage libraries by DNA shuffling, Nature Med., 1996, 2: 100.
    • (1996) Nature Med. , vol.2 , pp. 100
    • Crameri, A.1    Cwirla, S.2    Stemmer, W.P.C.3
  • 50
    • 0029862991 scopus 로고    scopus 로고
    • In vitro evolution of the DNA binding site of Escherichia coli methionine repressor
    • He, Y. Y., Stockley, P. G., Gold, L. In vitro evolution of the DNA binding site of Escherichia coli methionine repressor, Met. J. J. Mol. Biol., 1996, 255: 55.
    • (1996) Met. J. J. Mol. Biol. , vol.255 , pp. 55
    • He, Y.Y.1    Stockley, P.G.2    Gold, L.3
  • 51
    • 0029000018 scopus 로고
    • Directed evolution of subtilisin with calcium-independent stability
    • Strausberg, S. L., Alexander, P. A., Gallagher, D. T. et al., Directed evolution of subtilisin with calcium-independent stability, Biotechnology, 1995, 13: 669.
    • (1995) Biotechnology , vol.13 , pp. 669
    • Strausberg, S.L.1    Alexander, P.A.2    Gallagher, D.T.3
  • 52
    • 0029883624 scopus 로고    scopus 로고
    • Creation of drug specific HSV-1 thymidine kinase mutants for gene therapy
    • Black, M. E., Newcomb, T. G., Wilson, H. M. P. et al., Creation of drug specific HSV-1 thymidine kinase mutants for gene therapy, Proc. Natl. Acad. Sci. USA, 1996, 93: 3525.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 3525
    • Black, M.E.1    Newcomb, T.G.2    Wilson, H.M.P.3
  • 53
    • 0026649231 scopus 로고
    • Directed evolution of an RNA enzyme
    • Beaudry, A. A., Joyce, G. F., Directed evolution of an RNA enzyme, Science, 1992, 257: 635641.
    • (1992) Science , vol.257 , pp. 635641
    • Beaudry, A.A.1    Joyce, G.F.2
  • 54
    • 0030722164 scopus 로고    scopus 로고
    • Application of DNA shuffling to pharmaceuticals and vaccines
    • Patten, P. A., Howard, R. J., Stemmer, W. P. C., Application of DNA shuffling to pharmaceuticals and vaccines, Curr. Opin. Biotech., 1997 8: 724.
    • (1997) Curr. Opin. Biotech. , vol.8 , pp. 724
    • Patten, P.A.1    Howard, R.J.2    Stemmer, W.P.C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.