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Volumn 40, Issue 3, 2007, Pages 419-425

Directed evolution of beta-galactosidase from Escherichia coli into beta-glucuronidase

Author keywords

Directed evolution; DNA shuffling; Enzyme properties; Structure function analysis; galactosidase; glucuronidase

Indexed keywords

ESCHERICHIA COLI;

EID: 34249737018     PISSN: 12258687     EISSN: 02191024     Source Type: Journal    
DOI: 10.5483/bmbrep.2007.40.3.419     Document Type: Article
Times cited : (9)

References (34)
  • 1
    • 0038521054 scopus 로고    scopus 로고
    • Significantly enhanced stability of glucose dehydrogenase by directed evolution
    • Baik, S. H., Ide, T., Yoshida, H., Kagami, O. and Harayama, S. (2003) Significantly enhanced stability of glucose dehydrogenase by directed evolution. Appl. Microbiol. Biotechnol. 61, 329-335.
    • (2003) Appl. Microbiol. Biotechnol , vol.61 , pp. 329-335
    • Baik, S.H.1    Ide, T.2    Yoshida, H.3    Kagami, O.4    Harayama, S.5
  • 3
    • 0034798044 scopus 로고    scopus 로고
    • Improving the quality of industrially important enzymes by directed evolution
    • Chirumamilla, R. R., Muralidhar, R., Marchant, R. and Nigam, P. (2001) Improving the quality of industrially important enzymes by directed evolution. Mol. Cell Biochem. 224, 159-168.
    • (2001) Mol. Cell Biochem , vol.224 , pp. 159-168
    • Chirumamilla, R.R.1    Muralidhar, R.2    Marchant, R.3    Nigam, P.4
  • 4
    • 0029670330 scopus 로고    scopus 로고
    • Improved green fluorescent protein by molecular evolution using DNA shuffling
    • Crameri, A., Whitehorn, E. A., Tate, E. and Stemmer, W. P. (1996) Improved green fluorescent protein by molecular evolution using DNA shuffling. Nat. Biotechnol. 14, 315-319.
    • (1996) Nat. Biotechnol , vol.14 , pp. 315-319
    • Crameri, A.1    Whitehorn, E.A.2    Tate, E.3    Stemmer, W.P.4
  • 5
    • 0038606300 scopus 로고    scopus 로고
    • Forced evolution of a herbicide detoxifying glutathione transferase
    • Dixon, D. P., McEwen, A. G., Lapthorn, A. J. and Edwards, R. (2003) Forced evolution of a herbicide detoxifying glutathione transferase. J. Biol. Chem. 278, 23930-23935.
    • (2003) J. Biol. Chem , vol.278 , pp. 23930-23935
    • Dixon, D.P.1    McEwen, A.G.2    Lapthorn, A.J.3    Edwards, R.4
  • 6
    • 0036303387 scopus 로고    scopus 로고
    • Increasing the thermal stability of an oligomeric protein, beta-glucuronidase
    • Flores, H. and Ellington, A. D. (2002) Increasing the thermal stability of an oligomeric protein, beta-glucuronidase. J. Mol. Biol. 315, 325-337.
    • (2002) J. Mol. Biol , vol.315 , pp. 325-337
    • Flores, H.1    Ellington, A.D.2
  • 7
    • 0034683125 scopus 로고    scopus 로고
    • Novel fluorescent protein from Discosoma coral and its mutants possesses a unique far-red fluorescence
    • Fradkov, A. F., Chen, Y., Ding, L., Barsova, E. V., Matz, M. V. and Lukyanov, S. A. (2000) Novel fluorescent protein from Discosoma coral and its mutants possesses a unique far-red fluorescence. FEBS Lett. 479, 127-130.
    • (2000) FEBS Lett , vol.479 , pp. 127-130
    • Fradkov, A.F.1    Chen, Y.2    Ding, L.3    Barsova, E.V.4    Matz, M.V.5    Lukyanov, S.A.6
  • 8
    • 2942739036 scopus 로고    scopus 로고
    • Rapid evolution of beta-glucuronidase specificity by saturation mutagenesis of an active site loop
    • Geddie, M. L. and Matsumura, I. (2004) Rapid evolution of beta-glucuronidase specificity by saturation mutagenesis of an active site loop. J. Biol. Chem. 279, 26462-26468.
    • (2004) J. Biol. Chem , vol.279 , pp. 26462-26468
    • Geddie, M.L.1    Matsumura, I.2
  • 9
    • 0026055308 scopus 로고
    • A classification of glycosyl hydrolases based on amino acid sequence similarities
    • Henrissat, B. (1991) A classification of glycosyl hydrolases based on amino acid sequence similarities. Biochem. J. 280, 309-316.
    • (1991) Biochem. J , vol.280 , pp. 309-316
    • Henrissat, B.1
  • 10
    • 0028175669 scopus 로고
    • The active site and mechanism of the beta-galactosidase from Escherichia coli
    • Huber, R. E., Gupta, M. N. and Khare, S. K. (1994) The active site and mechanism of the beta-galactosidase from Escherichia coli. Int. J. Biochem. 26, 309-318.
    • (1994) Int. J. Biochem , vol.26 , pp. 309-318
    • Huber, R.E.1    Gupta, M.N.2    Khare, S.K.3
  • 11
    • 0028178377 scopus 로고
    • Three-dimensional structure of beta-galactosidase from E. coli
    • Jacobson, R. H., Zhang, X. J., DuBose, R. F. and Matthews, B. W. (1994) Three-dimensional structure of beta-galactosidase from E. coli. Nature 369, 761-766.
    • (1994) Nature , vol.369 , pp. 761-766
    • Jacobson, R.H.1    Zhang, X.J.2    DuBose, R.F.3    Matthews, B.W.4
  • 12
    • 0342444416 scopus 로고
    • GUS fusions: β-glucuronidase as a sensitive and versatile gene fusion marker for higher plants
    • Jefferson, R. A., Kavanaugh, T. A. and Bevan, M. W. (1987) GUS fusions: β-glucuronidase as a sensitive and versatile gene fusion marker for higher plants. EMBO J. 6, 3901-3907.
    • (1987) EMBO J , vol.6 , pp. 3901-3907
    • Jefferson, R.A.1    Kavanaugh, T.A.2    Bevan, M.W.3
  • 13
    • 0032923813 scopus 로고    scopus 로고
    • Structural comparisons of TIM barrel proteins suggest functional and evolutionary relationships between β-galactosidase and other glycohydrolases
    • Juers, D. H., Huber, R. E. and Matthews, B. W. (1999) Structural comparisons of TIM barrel proteins suggest functional and evolutionary relationships between β-galactosidase and other glycohydrolases. Protein Sci. 8, 122-136.
    • (1999) Protein Sci , vol.8 , pp. 122-136
    • Juers, D.H.1    Huber, R.E.2    Matthews, B.W.3
  • 14
    • 0035118386 scopus 로고    scopus 로고
    • Directed molecular evolution in plant improvement
    • Lassner, M. and Bedbrook, J. (2001) Directed molecular evolution in plant improvement. Curr. Opin. Plant Biol. 4, 152-156.
    • (2001) Curr. Opin. Plant Biol , vol.4 , pp. 152-156
    • Lassner, M.1    Bedbrook, J.2
  • 15
    • 0030000625 scopus 로고    scopus 로고
    • DNA shuffling brightens prospects for GFP
    • Matsumura, I. and Ellington, A. D. (1996) DNA shuffling brightens prospects for GFP. Nat. Biotechnol. 14, 366.
    • (1996) Nat. Biotechnol , vol.14 , pp. 366
    • Matsumura, I.1    Ellington, A.D.2
  • 16
    • 0035846958 scopus 로고    scopus 로고
    • In vitro evolution of beta-glucuronidase into a beta-galactosidase proceeds through non-specific intermediates
    • Matsumura, I. and Ellington, A. D. (2001) In vitro evolution of beta-glucuronidase into a beta-galactosidase proceeds through non-specific intermediates. J. Mol. Biol. 305, 331-339.
    • (2001) J. Mol. Biol , vol.305 , pp. 331-339
    • Matsumura, I.1    Ellington, A.D.2
  • 17
    • 0033054580 scopus 로고    scopus 로고
    • Directed evolution of the surface chemistry of the reporter enzyme beta-glucuronidase
    • Matsumura, I., Wallingford, J. B., Surana, N. K., Vize, P. D. and Ellington, A. D. (1999) Directed evolution of the surface chemistry of the reporter enzyme beta-glucuronidase. Nat. Biotechnol. 17, 696-701.
    • (1999) Nat. Biotechnol , vol.17 , pp. 696-701
    • Matsumura, I.1    Wallingford, J.B.2    Surana, N.K.3    Vize, P.D.4    Ellington, A.D.5
  • 18
    • 20444373710 scopus 로고    scopus 로고
    • The structure of E. coli beta-galactosidase
    • Matthews, B. W. (2005) The structure of E. coli beta-galactosidase. C. R. Biol. 328, 549-556.
    • (2005) C. R. Biol , vol.328 , pp. 549-556
    • Matthews, B.W.1
  • 19
    • 0347089333 scopus 로고    scopus 로고
    • Selectable marker genes in transgenic plants: Applications, alternatives and biosafety
    • Miki, B. and McHugh, S. (2004) Selectable marker genes in transgenic plants: applications, alternatives and biosafety. J. Biotechnol. 107, 193-232.
    • (2004) J. Biotechnol , vol.107 , pp. 193-232
    • Miki, B.1    McHugh, S.2
  • 20
    • 1442359485 scopus 로고    scopus 로고
    • Functional tuning of a salvaged green fluorescent protein variant with a new sequence space by directed evolution
    • Nam, S. H., Oh, K. H., Kim, G. J. and Kim, H. S. (2003) Functional tuning of a salvaged green fluorescent protein variant with a new sequence space by directed evolution. Protein Eng. 16, 1099-1105.
    • (2003) Protein Eng , vol.16 , pp. 1099-1105
    • Nam, S.H.1    Oh, K.H.2    Kim, G.J.3    Kim, H.S.4
  • 21
    • 18044390504 scopus 로고    scopus 로고
    • Directed evolution: Selecting today's biocatalysts
    • Otten, L. G. and Quax, W. J. (2005) Directed evolution: selecting today's biocatalysts. Biomol. Eng. 22, 1-9.
    • (2005) Biomol. Eng , vol.22 , pp. 1-9
    • Otten, L.G.1    Quax, W.J.2
  • 22
    • 24044554219 scopus 로고    scopus 로고
    • Site-saturation mutagenesis is more efficient than DNA shuffling for the directed evolution of beta-fucosidase from beta-galactosidase
    • Parikh, M. R. and Matsumura, I. (2005) Site-saturation mutagenesis is more efficient than DNA shuffling for the directed evolution of beta-fucosidase from beta-galactosidase. J. Mol. Biol. 352, 621-628.
    • (2005) J. Mol. Biol , vol.352 , pp. 621-628
    • Parikh, M.R.1    Matsumura, I.2
  • 23
    • 33750329048 scopus 로고    scopus 로고
    • A direct and efficient PAGE-mediated overlap extension PCR method for gene multiple-site mutagenesis
    • Peng, R. H., Xiong, A. S. and Yao, Q. H. (2006) A direct and efficient PAGE-mediated overlap extension PCR method for gene multiple-site mutagenesis. Appl. Microbiol. Biotechnol. 73, 234-240.
    • (2006) Appl. Microbiol. Biotechnol , vol.73 , pp. 234-240
    • Peng, R.H.1    Xiong, A.S.2    Yao, Q.H.3
  • 24
    • 0041324888 scopus 로고    scopus 로고
    • A comparison of directed evolution approaches using the beta-glucuronidase model system
    • Rowe, L. A., Geddie, M. L., Alexander, O. B. and Matsumura, I. (2003) A comparison of directed evolution approaches using the beta-glucuronidase model system. J. Mol. Biol. 332, 851-860.
    • (2003) J. Mol. Biol , vol.332 , pp. 851-860
    • Rowe, L.A.1    Geddie, M.L.2    Alexander, O.B.3    Matsumura, I.4
  • 26
    • 0028050350 scopus 로고
    • Rapid evolution of a protein in vitro by DNA shuffling
    • Stemmer, W. P. (1994) Rapid evolution of a protein in vitro by DNA shuffling. Nature 370, 389-391.
    • (1994) Nature , vol.370 , pp. 389-391
    • Stemmer, W.P.1
  • 28
    • 1842846524 scopus 로고    scopus 로고
    • Molecular evolution of beta-glucuronidase in vitro: Obtaining thermotolerant GUS gene
    • Xiong, A. S., Yao, Q. H., Peng, R. H., Chen, J. M., Li, X. and Fan, H. Q. (2002) Molecular evolution of beta-glucuronidase in vitro: obtaining thermotolerant GUS gene. Yi Chuan Xue Bao 29, 1034-1040.
    • (2002) Yi Chuan Xue Bao , vol.29 , pp. 1034-1040
    • Xiong, A.S.1    Yao, Q.H.2    Peng, R.H.3    Chen, J.M.4    Li, X.5    Fan, H.Q.6
  • 29
    • 3142666033 scopus 로고    scopus 로고
    • Isolation, characterization, molecular cloning of the cDNA encoding a novel phytase from Aspergillus niger 113 and high expression in Pichia pastoris
    • Xiong, A. S., Yao, Q. H., Peng, R. H., Li, X., Fan, H. Q., Guo, M. J. and Zhang, S. L. (2004a) Isolation, characterization, molecular cloning of the cDNA encoding a novel phytase from Aspergillus niger 113 and high expression in Pichia pastoris. J. Biochem. Mol. Biol. 37, 282-291.
    • (2004) J. Biochem. Mol. Biol , vol.37 , pp. 282-291
    • Xiong, A.S.1    Yao, Q.H.2    Peng, R.H.3    Li, X.4    Fan, H.Q.5    Guo, M.J.6    Zhang, S.L.7
  • 30
    • 3042820410 scopus 로고    scopus 로고
    • A simple, rapid, high-fidelity and cost-effective PCR-based two-step DNA synthesis method for long gene sequences
    • Xiong, A. S., Yao, Q. H., Peng, R. H., Li, X., Fan, H. Q., Cheng, Z. M. and Li, Y. (2004b) A simple, rapid, high-fidelity and cost-effective PCR-based two-step DNA synthesis method for long gene sequences. Nucleic Acids Res. 32, 98.
    • (2004) Nucleic Acids Res , vol.32 , pp. 98
    • Xiong, A.S.1    Yao, Q.H.2    Peng, R.H.3    Li, X.4    Fan, H.Q.5    Cheng, Z.M.6    Li, Y.7
  • 33
    • 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. (1997) Directed evolution of a fucosidase from a galactosidase by DNA shuffling and screening. Proc. Natl. Acad. Sci. USA 94, 4504-4509.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 4504-4509
    • Zhang, J.H.1    Dawes, G.2    Stemmer, W.P.3
  • 34
    • 0036536478 scopus 로고    scopus 로고
    • Directed evolution of enzymes and pathways for industrial biocatalysis
    • Zhao, H., Chockalingam, K. and Chen, Z. (2002) Directed evolution of enzymes and pathways for industrial biocatalysis. Curr. Opin. Biotechnol. 13, 104-110.
    • (2002) Curr. Opin. Biotechnol , vol.13 , pp. 104-110
    • Zhao, H.1    Chockalingam, K.2    Chen, Z.3


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