메뉴 건너뛰기




Volumn 1, Issue C, 2008, Pages 29-47

Enzyme Engineering

Author keywords

Directed evolution; Enzyme engineering; Enzyme evolution; Fitness landscape; Gene shuffling; Rational design; Sequence space; Variant enzyme

Indexed keywords


EID: 65249159180     PISSN: 17550408     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S1755-0408(07)01002-8     Document Type: Review
Times cited : (4)

References (59)
  • 1
    • 0345071423 scopus 로고    scopus 로고
    • Genes duplicated by polyploidy show unequal contributions to the transcriptome and organ-specific reciprocal silencing
    • Adams K.L., Cronn R., Percifield R., and Wendel J.F. Genes duplicated by polyploidy show unequal contributions to the transcriptome and organ-specific reciprocal silencing. Proc. Natl. Acad. Sci. USA 100 (2003) 4649-4654
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 4649-4654
    • Adams, K.L.1    Cronn, R.2    Percifield, R.3    Wendel, J.F.4
  • 2
    • 1542323289 scopus 로고    scopus 로고
    • Staggered extension process (StEP) in vitro recombination
    • Aguinaldo A.M., and Arnold F.H. Staggered extension process (StEP) in vitro recombination. Methods Mol. Biol. 231 (2003) 105-110
    • (2003) Methods Mol. Biol. , vol.231 , pp. 105-110
    • Aguinaldo, A.M.1    Arnold, F.H.2
  • 3
    • 0034628501 scopus 로고    scopus 로고
    • Directed evolution of new catalytic activity using the alpha/beta-barrel scaffold
    • Altamirano M.M., Blackburn J.M., Aguayo C., and Fersht A.R. Directed evolution of new catalytic activity using the alpha/beta-barrel scaffold. Nature 403 (2000) 617-622
    • (2000) Nature , vol.403 , pp. 617-622
    • Altamirano, M.M.1    Blackburn, J.M.2    Aguayo, C.3    Fersht, A.R.4
  • 4
    • 0031855459 scopus 로고    scopus 로고
    • When blind is better: Protein design by evolution
    • Arnold F.H. When blind is better: Protein design by evolution. Nat. Biotechnol. 16 (1998) 617-618
    • (1998) Nat. Biotechnol. , vol.16 , pp. 617-618
    • Arnold, F.H.1
  • 5
    • 0035843136 scopus 로고    scopus 로고
    • Combinatorial and computational challenges for biocatalyst design
    • Arnold F.H. Combinatorial and computational challenges for biocatalyst design. Nature 409 (2001) 253-257
    • (2001) Nature , vol.409 , pp. 253-257
    • Arnold, F.H.1
  • 6
    • 0038653402 scopus 로고    scopus 로고
    • ADP-glucose pyrophosphorylase, a regulatory enzyme for bacterial glycogen synthesis
    • table of contents
    • Ballicora M.A., Iglesias A.A., and Preiss J. ADP-glucose pyrophosphorylase, a regulatory enzyme for bacterial glycogen synthesis. Microbiol. Mol. Biol. Rev. 67 (2003) 213-225 table of contents
    • (2003) Microbiol. Mol. Biol. Rev. , vol.67 , pp. 213-225
    • Ballicora, M.A.1    Iglesias, A.A.2    Preiss, J.3
  • 7
    • 0037013191 scopus 로고    scopus 로고
    • Desaturation and hydroxylation. Residues 148 and 324 of Arabidopsis FAD2, in addition to substrate chain length, exert a major influence in partitioning of catalytic specificity
    • Broadwater J.A., Whittle E., and Shanklin J. Desaturation and hydroxylation. Residues 148 and 324 of Arabidopsis FAD2, in addition to substrate chain length, exert a major influence in partitioning of catalytic specificity. J. Biol. Chem. 277 (2002) 15613-15620
    • (2002) J. Biol. Chem. , vol.277 , pp. 15613-15620
    • Broadwater, J.A.1    Whittle, E.2    Shanklin, J.3
  • 8
    • 0031883086 scopus 로고    scopus 로고
    • A bifunctional oleate 12-hydroxylase: Desaturase from Lesquerella fendleri
    • Broun P., Boddupalli S., and Somerville C. A bifunctional oleate 12-hydroxylase: Desaturase from Lesquerella fendleri. Plant J. 13 (1998) 201-210
    • (1998) Plant J. , vol.13 , pp. 201-210
    • Broun, P.1    Boddupalli, S.2    Somerville, C.3
  • 9
    • 85045502002 scopus 로고
    • Randomization of genes by PCR mutagenesis
    • Cadwell R.C., and Joyce G.F. Randomization of genes by PCR mutagenesis. PCR Methods Appl. 2 (1992) 28-33
    • (1992) PCR Methods Appl. , vol.2 , pp. 28-33
    • Cadwell, R.C.1    Joyce, G.F.2
  • 10
    • 0034710903 scopus 로고    scopus 로고
    • Substrate-dependent mutant complementation to select fatty acid desaturase variants for metabolic engineering of plant seed oils
    • Cahoon E.B., and Shanklin J. Substrate-dependent mutant complementation to select fatty acid desaturase variants for metabolic engineering of plant seed oils. Proc. Natl. Acad. Sci. USA 97 (2000) 12350-12355
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 12350-12355
    • Cahoon, E.B.1    Shanklin, J.2
  • 11
    • 0033607294 scopus 로고    scopus 로고
    • Biosynthetic origin of conjugated double bonds: Production of fatty acid components of high-value drying oils in transgenic soybean embryos
    • Cahoon E.B., Carlson T.J., Ripp K.G., Schweiger B.J., Cook G.A., Hall S.E., and Kinney A.J. Biosynthetic origin of conjugated double bonds: Production of fatty acid components of high-value drying oils in transgenic soybean embryos. Proc. Natl. Acad. Sci. USA 96 (1999) 12935-12940
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 12935-12940
    • Cahoon, E.B.1    Carlson, T.J.2    Ripp, K.G.3    Schweiger, B.J.4    Cook, G.A.5    Hall, S.E.6    Kinney, A.J.7
  • 12
    • 0030138028 scopus 로고    scopus 로고
    • Functional expression of the extraplastidial Arabidopsis thaliana oleate desaturase gene (FAD2) in Saccharomyces cerevisiae
    • Covello P.S., and Reed D.W. Functional expression of the extraplastidial Arabidopsis thaliana oleate desaturase gene (FAD2) in Saccharomyces cerevisiae. Plant Physiol. 111 (1996) 223-236
    • (1996) Plant Physiol. , vol.111 , pp. 223-236
    • Covello, P.S.1    Reed, D.W.2
  • 13
    • 0021096466 scopus 로고
    • Beta-hydroxydecanoyl thio ester dehydrase does not catalyze a rate-limiting step in Escherichia coli unsaturated fatty acid synthesis
    • Clark D.P., Demendoza D., Polacco M.L., and Cronan Jr. J.E. Beta-hydroxydecanoyl thio ester dehydrase does not catalyze a rate-limiting step in Escherichia coli unsaturated fatty acid synthesis. Biochemistry 22 (1983) 5897-5902
    • (1983) Biochemistry , vol.22 , pp. 5897-5902
    • Clark, D.P.1    Demendoza, D.2    Polacco, M.L.3    Cronan Jr., J.E.4
  • 14
    • 0030048583 scopus 로고    scopus 로고
    • Construction and evolution of antibody-phage libraries by DNA shuffling
    • Crameri A., Cwirla S., and Stemmer W.P. Construction and evolution of antibody-phage libraries by DNA shuffling. Nat. Med. 2 (1996) 100-102
    • (1996) Nat. Med. , vol.2 , pp. 100-102
    • Crameri, A.1    Cwirla, S.2    Stemmer, W.P.3
  • 15
    • 0030951186 scopus 로고    scopus 로고
    • Molecular evolution of an arsenate detoxification pathway by DNA shuffling [see comments]
    • Crameri A., Dawes G., Rodriguez Jr. E., Silver S., and Stemmer W.P. Molecular evolution of an arsenate detoxification pathway by DNA shuffling [see comments]. Nat. Biotechnol. 15 (1997) 436-438
    • (1997) Nat. Biotechnol. , vol.15 , pp. 436-438
    • Crameri, A.1    Dawes, G.2    Rodriguez Jr., E.3    Silver, S.4    Stemmer, W.P.5
  • 16
    • 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., and Stemmer W.P. 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.4
  • 17
    • 0030793767 scopus 로고    scopus 로고
    • De novo protein design: Fully automated sequence selection
    • Dahiyat B.I., and Mayo S.L. De novo protein design: Fully automated sequence selection. Science 278 (1997) 82-87
    • (1997) Science , vol.278 , pp. 82-87
    • Dahiyat, B.I.1    Mayo, S.L.2
  • 19
    • 0036928370 scopus 로고    scopus 로고
    • Molecular analysis of a bifunctional fatty acid conjugase/desaturase from tung. Implications for the evolution of plant fatty acid diversity
    • Dyer J.M., Chapital D.C., Kuan J.C., Mullen R.T., Turner C., Mckeon T.A., and Pepperman A.B. Molecular analysis of a bifunctional fatty acid conjugase/desaturase from tung. Implications for the evolution of plant fatty acid diversity. Plant Physiol. 130 (2002) 2027-2038
    • (2002) Plant Physiol. , vol.130 , pp. 2027-2038
    • Dyer, J.M.1    Chapital, D.C.2    Kuan, J.C.3    Mullen, R.T.4    Turner, C.5    Mckeon, T.A.6    Pepperman, A.B.7
  • 20
    • 0033028744 scopus 로고    scopus 로고
    • Improved stearate phenotype in transgenic canola expressing a modified acyl-acyl carrier protein thioesterase
    • Facciotti M.T., Bertain P.B., and Yuan L. Improved stearate phenotype in transgenic canola expressing a modified acyl-acyl carrier protein thioesterase. Nat. Biotechnol. 17 (1999) 593-597
    • (1999) Nat. Biotechnol. , vol.17 , pp. 593-597
    • Facciotti, M.T.1    Bertain, P.B.2    Yuan, L.3
  • 22
    • 0032893932 scopus 로고    scopus 로고
    • Preservation of duplicate genes by complementary, degenerative mutations
    • Force A., Lynch M., Pickett F.B., Amores A., Yan Y.L., and Postlethwait J. Preservation of duplicate genes by complementary, degenerative mutations. Genetics 151 (1999) 1531-1545
    • (1999) Genetics , vol.151 , pp. 1531-1545
    • Force, A.1    Lynch, M.2    Pickett, F.B.3    Amores, A.4    Yan, Y.L.5    Postlethwait, J.6
  • 25
    • 0034923923 scopus 로고    scopus 로고
    • Divergent evolution of enzymatic function: Mechanistically diverse superfamilies and functionally distinct suprafamilies
    • Gerlt J.A., and Babbitt P.C. Divergent evolution of enzymatic function: Mechanistically diverse superfamilies and functionally distinct suprafamilies. Annu. Rev. Biochem. 70 (2001) 209-246
    • (2001) Annu. Rev. Biochem. , vol.70 , pp. 209-246
    • Gerlt, J.A.1    Babbitt, P.C.2
  • 26
    • 0036865360 scopus 로고    scopus 로고
    • Acyl-CoA measurements in plants suggest a role in regulating various cellular processes
    • Graham I.A., Li Y., and Larson T.R. Acyl-CoA measurements in plants suggest a role in regulating various cellular processes. Biochem. Soc. Trans. 30 (2002) 1095-1099
    • (2002) Biochem. Soc. Trans. , vol.30 , pp. 1095-1099
    • Graham, I.A.1    Li, Y.2    Larson, T.R.3
  • 28
    • 0029115481 scopus 로고
    • A sequence property approach to searching protein databases
    • Hobohm U., and Sander C. A sequence property approach to searching protein databases. J. Mol. Biol. 251 (1995) 390-399
    • (1995) J. Mol. Biol. , vol.251 , pp. 390-399
    • Hobohm, U.1    Sander, C.2
  • 29
    • 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., and 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
  • 30
    • 0028956983 scopus 로고
    • Molecular basis of the cauliflower phenotype in Arabidopsis
    • Kempin S.A., Savidge B., and Yanofsky M.F. Molecular basis of the cauliflower phenotype in Arabidopsis. Science 267 (1995) 522-525
    • (1995) Science , vol.267 , pp. 522-525
    • Kempin, S.A.1    Savidge, B.2    Yanofsky, M.F.3
  • 33
    • 0029670577 scopus 로고    scopus 로고
    • Directed evolution of a para-nitrobenzyl esterase for aqueous-organic solvents
    • Moore J.C., and Arnold F.H. Directed evolution of a para-nitrobenzyl esterase for aqueous-organic solvents. Nat. Biotechnol. 14 (1996) 458-467
    • (1996) Nat. Biotechnol. , vol.14 , pp. 458-467
    • Moore, J.C.1    Arnold, F.H.2
  • 34
    • 0031921553 scopus 로고    scopus 로고
    • Selection of a subtillisin-hyperproducing Bacillus in a highly structured environment
    • Naki D., Paech C., Granshaw G., and Schellenberger V. Selection of a subtillisin-hyperproducing Bacillus in a highly structured environment. Appl. Microbiol. Biotechnol. 49 (1998) 290-294
    • (1998) Appl. Microbiol. Biotechnol. , vol.49 , pp. 290-294
    • Naki, D.1    Paech, C.2    Granshaw, G.3    Schellenberger, V.4
  • 36
    • 0035749216 scopus 로고    scopus 로고
    • Effect of nuclear matrix attachment regions on transgene expression in tobacco plants
    • Nowak W., Gawlowska M., Jarmolowski A., and Augustyniak J. Effect of nuclear matrix attachment regions on transgene expression in tobacco plants. Acta Biochim. Pol. 48 (2001) 637-646
    • (2001) Acta Biochim. Pol. , vol.48 , pp. 637-646
    • Nowak, W.1    Gawlowska, M.2    Jarmolowski, A.3    Augustyniak, J.4
  • 37
    • 4043109994 scopus 로고    scopus 로고
    • Functional evolution and structural conservation in chimeric cytochromes p450: Calibrating a structure-guided approach
    • Otey C.R., Silberg J.J., Voigt C.A., Endelman J.B., Bandara G., and Arnold F.H. Functional evolution and structural conservation in chimeric cytochromes p450: Calibrating a structure-guided approach. Chem. Biol. 11 (2004) 309-318
    • (2004) Chem. Biol. , vol.11 , pp. 309-318
    • Otey, C.R.1    Silberg, J.J.2    Voigt, C.A.3    Endelman, J.B.4    Bandara, G.5    Arnold, F.H.6
  • 38
    • 0035220128 scopus 로고    scopus 로고
    • Production of polyesters in transgenic plants
    • Poirier Y. Production of polyesters in transgenic plants. Adv. Biochem. Eng. Biotechnol. 71 (2001) 209-240
    • (2001) Adv. Biochem. Eng. Biotechnol. , vol.71 , pp. 209-240
    • Poirier, Y.1
  • 40
    • 0030309983 scopus 로고    scopus 로고
    • ADPglucose pyrophosphorylase: Basic science and applications in biotechnology
    • Preiss J. ADPglucose pyrophosphorylase: Basic science and applications in biotechnology. Biotechnol. Annu. Rev. 2 (1996) 259-279
    • (1996) Biotechnol. Annu. Rev. , vol.2 , pp. 259-279
    • Preiss, J.1
  • 42
    • 10644266747 scopus 로고    scopus 로고
    • RuBisCO without the Calvin cycle improves the carbon efficiency of developing green seeds
    • Schwender J., Goffman F., Ohlrogge J.B., and Shachar-Hill Y. RuBisCO without the Calvin cycle improves the carbon efficiency of developing green seeds. Nature 432 (2004) 779-782
    • (2004) Nature , vol.432 , pp. 779-782
    • Schwender, J.1    Goffman, F.2    Ohlrogge, J.B.3    Shachar-Hill, Y.4
  • 44
    • 0030737949 scopus 로고    scopus 로고
    • Generation of large libraries of random mutants in Bacillus subtilis by PCR-based plasmid multimerization
    • Shafikhani S., Siegel R.A., Ferrari E., and Schellenberger V. Generation of large libraries of random mutants in Bacillus subtilis by PCR-based plasmid multimerization. Biotechniques 23 (1997) 304-310
    • (1997) Biotechniques , vol.23 , pp. 304-310
    • Shafikhani, S.1    Siegel, R.A.2    Ferrari, E.3    Schellenberger, V.4
  • 46
    • 0028110130 scopus 로고
    • DNA shuffling by random fragmentation and reassembly: In vitro recombination for molecular evolution
    • Stemmer W.P. DNA shuffling by random fragmentation and reassembly: In vitro recombination for molecular evolution. Proc. Natl. Acad. Sci. USA 91 (1994) 10747-10751
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 10747-10751
    • Stemmer, W.P.1
  • 47
    • 0028050350 scopus 로고
    • Rapid evolution of a protein in vitro by DNA shuffling
    • Stemmer W.P. 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.1
  • 48
    • 1542273451 scopus 로고    scopus 로고
    • Seed-expressed fluorescent proteins as versatile tools for easy (co)transformation and high-throughput functional genomics in Arabidopsis
    • Stuitje A.R., Verbree E.C., Van Der Linden K.H., Mietiewska E.M., Nap J.P., and Kneppers T.J.A. Seed-expressed fluorescent proteins as versatile tools for easy (co)transformation and high-throughput functional genomics in Arabidopsis. Plant Biotechnol. J. 1 (2003) 301-309
    • (2003) Plant Biotechnol. J. , vol.1 , pp. 301-309
    • Stuitje, A.R.1    Verbree, E.C.2    Van Der Linden, K.H.3    Mietiewska, E.M.4    Nap, J.P.5    Kneppers, T.J.A.6
  • 49
    • 32944461132 scopus 로고    scopus 로고
    • Regulation of metabolic networks: Understanding metabolic complexity in the systems biology era
    • Sweetlove L.J., and Fernie A.R. Regulation of metabolic networks: Understanding metabolic complexity in the systems biology era. New Phytol. 168 (2005) 9-24
    • (2005) New Phytol. , vol.168 , pp. 9-24
    • Sweetlove, L.J.1    Fernie, A.R.2
  • 50
    • 0036306115 scopus 로고    scopus 로고
    • Why are proteins so robust to site mutations?
    • Taverna D.M., and Goldstein R.A. Why are proteins so robust to site mutations?. J. Mol. Biol. 315 (2002) 479-484
    • (2002) J. Mol. Biol. , vol.315 , pp. 479-484
    • Taverna, D.M.1    Goldstein, R.A.2
  • 51
    • 0036139093 scopus 로고    scopus 로고
    • Why are proteins marginally stable?
    • Taverna D.M., and Goldstein R.A. Why are proteins marginally stable?. Proteins 46 (2002) 105-109
    • (2002) Proteins , vol.46 , pp. 105-109
    • Taverna, D.M.1    Goldstein, R.A.2
  • 52
    • 0036338519 scopus 로고    scopus 로고
    • Metabolic engineering of fatty acid biosynthesis in plants
    • Thelen J.J., and Ohlrogge J.B. Metabolic engineering of fatty acid biosynthesis in plants. Metab. Eng. 4 (2002) 12-21
    • (2002) Metab. Eng. , vol.4 , pp. 12-21
    • Thelen, J.J.1    Ohlrogge, J.B.2
  • 54
    • 0035877632 scopus 로고    scopus 로고
    • Engineering delta 9-16:0-acyl carrier protein (ACP) desaturase specificity based on combinatorial saturation mutagenesis and logical redesign of the castor delta 9-18:0-ACP desaturase
    • Whittle E., Cahoon E.B., and Shanklin J. Engineering delta 9-16:0-acyl carrier protein (ACP) desaturase specificity based on combinatorial saturation mutagenesis and logical redesign of the castor delta 9-18:0-ACP desaturase. J. Biol. Chem. 276 (2001) 21500-21505
    • (2001) J. Biol. Chem. , vol.276 , pp. 21500-21505
    • Whittle, E.1    Cahoon, E.B.2    Shanklin, J.3
  • 55
    • 0029969577 scopus 로고    scopus 로고
    • Directed evolution of subtilisin E in Bacillus subtilis to enhance total activity in aqueous dimethylformamide
    • You L., and Arnold F.H. Directed evolution of subtilisin E in Bacillus subtilis to enhance total activity in aqueous dimethylformamide. Protein Eng. 9 (1996) 77-83
    • (1996) Protein Eng. , vol.9 , pp. 77-83
    • You, L.1    Arnold, F.H.2
  • 56
    • 0032545151 scopus 로고    scopus 로고
    • Estimating the number of protein folds
    • Zhang C., and Delisi C. Estimating the number of protein folds. J. Mol. Biol. 284 (1998) 1301-1305
    • (1998) J. Mol. Biol. , vol.284 , pp. 1301-1305
    • Zhang, C.1    Delisi, C.2
  • 57
    • 0030989062 scopus 로고    scopus 로고
    • Directed evolution of a fucosidase from a galactosidase by DNA shuffling and screening
    • Zhang J.H., Dawes G., and Stemmer W.P. Directed evolution of a fucosidase from a galactosidase by DNA shuffling and screening. Proc. Natl. Acad. Sci. USA 94 (1997) 4504-4509
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 4504-4509
    • Zhang, J.H.1    Dawes, G.2    Stemmer, W.P.3
  • 59
    • 0032973026 scopus 로고    scopus 로고
    • Directed evolution converts subtilisin E into a functional equivalent of thermitase
    • Zhao H., and Arnold F.H. Directed evolution converts subtilisin E into a functional equivalent of thermitase. Protein Eng. 12 (1999) 47-53
    • (1999) Protein Eng. , vol.12 , pp. 47-53
    • Zhao, H.1    Arnold, F.H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.