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Volumn 56, Issue 6, 2014, Pages 301-310

MDC-Analyzer: A novel degenerate primer design tool for the construction of intelligent mutagenesis libraries with contiguous sites

Author keywords

Contiguous sites; Data driven protein engineering; Intelligent library design; Partial randomization

Indexed keywords

CONTIG; CODON; PRIMER DNA; PROTEIN;

EID: 84902332122     PISSN: 07366205     EISSN: 19409818     Source Type: Journal    
DOI: 10.2144/000114177     Document Type: Article
Times cited : (16)

References (39)
  • 1
    • 0027205210 scopus 로고
    • Tuning the activity of an enzyme for unusual environments: Sequential random mutagenesis of subtilisin E for catalysis in dimethylformamide
    • Chen, K. and F. H. Arnold. 1993. 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: 5618-5622.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 5618-5622
    • Chen, K.1    Arnold, F.H.2
  • 2
    • 0342367772 scopus 로고
    • Isolation of a thermostable enzyme variant by cloning and selection in a thermophile
    • Liao, H., T. McKenzie, and R. Hageman. 1986. Isolation of a thermostable enzyme variant by cloning and selection in a thermophile. Proc. Natl. Acad. Sci. USA 83: 576-580.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 576-580
    • Liao, H.1    McKenzie, T.2    Hageman, R.3
  • 4
    • 68049106179 scopus 로고    scopus 로고
    • Directed evolution drives the next generation of biocatalysts
    • Turner, N. J. 2009. Directed evolution drives the next generation of biocatalysts. Nat. Chem. Biol. 5: 567-573.
    • (2009) Nat. Chem. Biol , vol.5 , pp. 567-573
    • Turner, N.J.1
  • 5
    • 78349313517 scopus 로고    scopus 로고
    • Beyond directed evolution-semi-rational protein engineering and design
    • Lutz, S. 2010. Beyond directed evolution-semi-rational protein engineering and design. Curr. Opin. Biotechnol. 21: 734-743.
    • (2010) Curr. Opin. Biotechnol , vol.21 , pp. 734-743
    • Lutz, S.1
  • 6
    • 23444450226 scopus 로고    scopus 로고
    • Semi-rational approaches to engineering enzyme activity: Combining the benefits of directed evolution and rational design
    • Chica, R. A., N. Doucet, and J. N. Pelletier. 2005. Semi-rational approaches to engineering enzyme activity: combining the benefits of directed evolution and rational design. Curr. Opin. Biotechnol. 16: 378-384.
    • (2005) Curr. Opin. Biotechnol , vol.16 , pp. 378-384
    • Chica, R.A.1    Doucet, N.2    Pelletier, J.N.3
  • 7
    • 39149125127 scopus 로고    scopus 로고
    • Enzyme optimization: Moving from blind evolution to statistical exploration of sequence-function space
    • Fox, R. J. and G. W. Huisman. 2008. Enzyme optimization: moving from blind evolution to statistical exploration of sequence-function space. Trends Biotechnol. 26: 132-138.
    • (2008) Trends Biotechnol , vol.26 , pp. 132-138
    • Fox, R.J.1    Huisman, G.W.2
  • 8
    • 33744475011 scopus 로고    scopus 로고
    • Directed evolution of enantioselective enzymes: Iterative cycles of CASTing for probing protein-sequence space
    • Reetz, M. T., L. W. Wang, and M. Bocola. 2006. Directed evolution of enantioselective enzymes: iterative cycles of CASTing for probing protein-sequence space. Angew. Chem. Int. Ed. Engl. 45: 1236-1241.
    • (2006) Angew. Chem. Int. Ed. Engl , vol.45 , pp. 1236-1241
    • Reetz, M.T.1    Wang, L.W.2    Bocola, M.3
  • 9
    • 34248567845 scopus 로고    scopus 로고
    • Iterative saturation mutagenesis (ISM) for rapid directed evolution of functional enzymes
    • Reetz, M. T. and J. D. Carballeira. 2007. Iterative saturation mutagenesis (ISM) for rapid directed evolution of functional enzymes. Nat. Protoc. 2: 891-903.
    • (2007) Nat. Protoc , vol.2 , pp. 891-903
    • Reetz, M.T.1    Carballeira, J.D.2
  • 10
    • 67650547522 scopus 로고    scopus 로고
    • Directed evolution of an enantioselective epoxide hydrolase: Uncovering the source of enantioselectivity at each evolutionary stage
    • Reetz, M. T., M. Bocola, L. W. Wang, J. Sanchis, A. Cronin, M. Arand, J. Zou, A. Archelas, et al. 2009. Directed evolution of an enantioselective epoxide hydrolase: uncovering the source of enantioselectivity at each evolutionary stage. J. Am. Chem. Soc. 131: 7334-7343.
    • (2009) J. Am. Chem. Soc , vol.131 , pp. 7334-7343
    • Reetz, M.T.1    Bocola, M.2    Wang, L.W.3    Sanchis, J.4    Cronin, A.5    Arand, M.6    Zou, J.7    Archelas, A.8
  • 11
    • 0032030286 scopus 로고    scopus 로고
    • Codon-based mutagenesis using dimer-phosphoramidites
    • Neuner, P., R. Cortese, and P. Monaci. 1998. Codon-based mutagenesis using dimer-phosphoramidites. Nucleic Acids Res. 26: 1223-1227.
    • (1998) Nucleic Acids Res , vol.26 , pp. 1223-1227
    • Neuner, P.1    Cortese, R.2    Monaci, P.3
  • 12
    • 0028559783 scopus 로고
    • Trinucleotide phosphoramidites: Ideal reagents for the synthesis of mixed oligonucleotides for random mutagenesis
    • Virnekäs, B., L. Ge, A. Plückthun, K. C. Schneider, G. Wellnhofer, and S. E. Moroney. 1994. Trinucleotide phosphoramidites: ideal reagents for the synthesis of mixed oligonucleotides for random mutagenesis. Nucleic Acids Res. 22: 5600-5607.
    • (1994) Nucleic Acids Res , vol.22 , pp. 5600-5607
    • Virnekäs, B.1    Ge, L.2    Plückthun, A.3    Schneider, K.C.4    Wellnhofer, G.5    Moroney, S.E.6
  • 13
    • 84863280525 scopus 로고    scopus 로고
    • Construction of "small-intelligent" focused mutagenesis libraries using well-designed combinatorial degenerate primers
    • Tang, L., H. Gao, X. Zhu, X. Wang, M. Zhou, and R. Jiang. 2012. Construction of "small-intelligent" focused mutagenesis libraries using well-designed combinatorial degenerate primers. Biotechniques 52: 149-158.
    • (2012) Biotechniques , vol.52 , pp. 149-158
    • Tang, L.1    Gao, H.2    Zhu, X.3    Wang, X.4    Zhou, M.5    Jiang, R.6
  • 14
    • 84874034041 scopus 로고    scopus 로고
    • Reducing codon redundancy and screening effort of combinatorial protein libraries created by saturation mutagenesis
    • Kille, S., C. G. Acevedo-Rocha, L. P. Parra, Z. G. Zhang, D. J. Opperman, M. T. Reetz, and J. P. Acevedo. 2013. Reducing codon redundancy and screening effort of combinatorial protein libraries created by saturation mutagenesis. ACS Synth Biol 2: 83-92.
    • (2013) ACS Synth Biol , vol.2 , pp. 83-92
    • Kille, S.1    Acevedo-Rocha, C.G.2    Parra, L.P.3    Zhang, Z.G.4    Opperman, D.J.5    Reetz, M.T.6    Acevedo, J.P.7
  • 15
    • 84861163924 scopus 로고    scopus 로고
    • Key residues for controlling enantioselectivity of Halohydrin dehalogenase from Arthrobacter sp strain AD2, revealed by structure-guided directed evolution
    • Tang, L., X. Zhu, H. Zheng, R. Jiang., and M. Majeric Elenkov. 2012. Key residues for controlling enantioselectivity of Halohydrin dehalogenase from Arthrobacter sp. strain AD2, revealed by structure-guided directed evolution. Appl. Environ. Microbiol. 78: 2631-2637.
    • (2012) Appl. Environ. Microbiol , vol.78 , pp. 2631-2637
    • Tang, L.1    Zhu, X.2    Zheng, H.3    Jiang, R.4    Elenkov, M.M.5
  • 17
    • 84876732154 scopus 로고    scopus 로고
    • Strategies for the discovery and engineering of enzymes for biocatalysis
    • Davids, T., M. Schmidt, D. Böttcher, and U. T. Bornscheuer. 2013. Strategies for the discovery and engineering of enzymes for biocatalysis. Curr. Opin. Chem. Biol. 17: 215-220.
    • (2013) Curr. Opin. Chem. Biol , vol.17 , pp. 215-220
    • Davids, T.1    Schmidt, M.2    Böttcher, D.3    Bornscheuer, U.T.4
  • 20
    • 33845624902 scopus 로고    scopus 로고
    • Structure-guided SCHEMA recombination of distantly related b-lactamases
    • Meyer, M. M., L. Hochrein, and F. H. Arnold. 2006. Structure-guided SCHEMA recombination of distantly related b-lactamases. Protein Eng. Des. Sel. 19: 563-570.
    • (2006) Protein Eng. Des. Sel , vol.19 , pp. 563-570
    • Meyer, M.M.1    Hochrein, L.2    Arnold, F.H.3
  • 21
    • 77958179580 scopus 로고    scopus 로고
    • Efficient screening of fungal cellobiohydrolase class I enzymes for thermostabilizing sequence blocks by SCHEMA structure-guided recombination
    • Heinzelman, P., R. Komor, A. Kanaan, P. Romero, X. Yu, S. Mohler, C. Snow, and F. H. Arnold. 2010. Efficient screening of fungal cellobiohydrolase class I enzymes for thermostabilizing sequence blocks by SCHEMA structure-guided recombination. Protein Eng. Des. Sel. 23: 871-880.
    • (2010) Protein Eng. Des. Sel , vol.23 , pp. 871-880
    • Heinzelman, P.1    Komor, R.2    Kanaan, A.3    Romero, P.4    Yu, X.5    Mohler, S.6    Snow, C.7    Arnold, F.H.8
  • 22
    • 84868117425 scopus 로고    scopus 로고
    • SCHEMA-designed variants of human Arginase I and II reveal sequence elements important to stability and catalysis
    • Romero, P. A., E. Stone, C. Lamb, L. Chantranupong, A. Krause, A. E. Miklos, R. A. Hughes, B. Fechtel, et al. 2012. SCHEMA-designed variants of human Arginase I and II reveal sequence elements important to stability and catalysis. ACS Synth Biol 1: 221-228.
    • (2012) ACS Synth Biol , vol.1 , pp. 221-228
    • Romero, P.A.1    Stone, E.2    Lamb, C.3    Chantranupong, L.4    Krause, A.5    Miklos, A.E.6    Hughes, R.A.7    Fechtel, B.8
  • 23
    • 67849130559 scopus 로고    scopus 로고
    • HotSpot Wizard: A web server for identification of hot spots in protein engineering
    • Pavelka, A., E. Chovancova, and J. Damborsky. 2009. HotSpot Wizard: a web server for identification of hot spots in protein engineering. Nucleic Acids Res. 37: W376-W383.
    • (2009) Nucleic Acids Res , vol.37
    • Pavelka, A.1    Chovancova, E.2    Damborsky, J.3
  • 24
    • 12944257228 scopus 로고    scopus 로고
    • The ConSurf-HSSP database: The mapping of evolutionary conservation among homologs onto PDB structures
    • Glaser, F., Y. Rosenberg, A. Kessel, T. Pupko, and N. Ben-Tal. 2005. The ConSurf-HSSP database: the mapping of evolutionary conservation among homologs onto PDB structures. Proteins 58: 610-617.
    • (2005) Proteins , vol.58 , pp. 610-617
    • Glaser, F.1    Rosenberg, Y.2    Kessel, A.3    Pupko, T.4    Ben-Tal, N.5
  • 25
    • 77956234144 scopus 로고    scopus 로고
    • Natural diversity to guide focused directed evolution
    • Jochens, H. and U. T. Bornscheuer. 2010. Natural diversity to guide focused directed evolution. ChemBioChem 11: 1861-1866.
    • (2010) ChemBioChem , vol.11 , pp. 1861-1866
    • Jochens, H.1    Bornscheuer, U.T.2
  • 26
    • 78649277331 scopus 로고    scopus 로고
    • Thermostabilization of an esterase by alignment-guided focussed directed evolution
    • Jochens, H., D. Aerts, and U. T. Bornscheuer. 2010. Thermostabilization of an esterase by alignment-guided focussed directed evolution. Protein Eng. Des. Sel. 23: 903-909.
    • (2010) Protein Eng. Des. Sel , vol.23 , pp. 903-909
    • Jochens, H.1    Aerts, D.2    Bornscheuer, U.T.3
  • 27
    • 84879196613 scopus 로고    scopus 로고
    • Use of 'small but smart' libraries to enhance the enantioselectivity of an esterase from Bacillus stearothermophilus towards tetrahydrofuran-3-yl acetate
    • Nobili, A., M. G. Gall, I. V. Pavlidis, M. L. Thompson, M. Schmidt, and U. T. Bornscheuer. 2013. Use of 'small but smart' libraries to enhance the enantioselectivity of an esterase from Bacillus stearothermophilus towards tetrahydrofuran-3-yl acetate. FEBS J. 280: 3084-3093.
    • (2013) FEBS J , vol.280 , pp. 3084-3093
    • Nobili, A.1    Gall, M.G.2    Pavlidis, I.V.3    Thompson, M.L.4    Schmidt, M.5    Bornscheuer, U.T.6
  • 28
    • 84880635582 scopus 로고    scopus 로고
    • Optimal codon randomization via mathematical programming
    • Nov, Y. and D. Segev. 2013. Optimal codon randomization via mathematical programming. J. Theor. Biol. 335: 147-152.
    • (2013) J. Theor. Biol , vol.335 , pp. 147-152
    • Nov, Y.1    Segev, D.2
  • 31
    • 55849148481 scopus 로고    scopus 로고
    • Greatly reduced amino acid alphabets in directed evolution: Making the right choice for saturation mutagenesis at homologous enzyme positions
    • Reetz, M. T. and S. Wu. 2008. Greatly reduced amino acid alphabets in directed evolution: making the right choice for saturation mutagenesis at homologous enzyme positions. Chem. Commun. (Camb.) 43: 5499-5501.
    • (2008) Chem. Commun. (Camb.) , vol.43 , pp. 5499-5501
    • Reetz, M.T.1    Wu, S.2
  • 32
    • 0036841628 scopus 로고    scopus 로고
    • Creating randomized amino acid libraries with the QuikChange™ multi site-directed mutagenesis kit
    • Hogrefe, H. H., J. Cline, G. L. Youngblood, and R. M. Allen. 2002. Creating randomized amino acid libraries with the QuikChange™ multi site-directed mutagenesis kit. Biotechniques 33: 1158-1160.
    • (2002) Biotechniques , vol.33 , pp. 1158-1160
    • Hogrefe, H.H.1    Cline, J.2    Youngblood, G.L.3    Allen, R.M.4
  • 33
    • 1842842876 scopus 로고    scopus 로고
    • Creating random mutagenesis libraries using megaprimer PCR of whole plasmid
    • Miyazaki, K. and M. Takenouchi. 2002. Creating random mutagenesis libraries using megaprimer PCR of whole plasmid. Biotechniques 33: 1033-1034.
    • (2002) Biotechniques , vol.33 , pp. 1033-1034
    • Miyazaki, K.1    Takenouchi, M.2
  • 34
    • 0041765676 scopus 로고    scopus 로고
    • User friendly algorithms for estimating completeness and diversity in randomized protein-encoding libraries
    • Patrick, W. M., A. E. Firth, and J. M. Blackburn. 2003. User friendly algorithms for estimating completeness and diversity in randomized protein-encoding libraries. Protein Eng. 16: 451-457.
    • (2003) Protein Eng , vol.16 , pp. 451-457
    • Patrick, W.M.1    Firth, A.E.2    Blackburn, J.M.3
  • 35
    • 27944437517 scopus 로고    scopus 로고
    • Automated design of degenerate codon libraries
    • Mena, M. A. and P. S. Daugherty. 2005. Automated design of degenerate codon libraries. Protein Eng. Des. Sel. 18: 559-561.
    • (2005) Protein Eng. Des. Sel , vol.18 , pp. 559-561
    • Mena, M.A.1    Daugherty, P.S.2
  • 36
    • 40649107834 scopus 로고    scopus 로고
    • A novel megaprimed and ligase-free, PCR-based, site-directed mutagenesis method
    • Tseng, W. C., J. W. Lin, T. Y. Wei, and T. Y. Fang. 2008. A novel megaprimed and ligase-free, PCR-based, site-directed mutagenesis method. Anal. Biochem. 375: 376-378.
    • (2008) Anal. Biochem , vol.375 , pp. 376-378
    • Tseng, W.C.1    Lin, J.W.2    Wei, T.Y.3    Fang, T.Y.4
  • 37
  • 38
    • 84859707637 scopus 로고    scopus 로고
    • Restriction enzyme-free construction of random gene mutagenesis libraries in Escherichia coli
    • Pai, J. C., K. C. Entzminger, and J. A. Maynard. 2012. Restriction enzyme-free construction of random gene mutagenesis libraries in Escherichia coli. Anal. Biochem. 421: 640-648.
    • (2012) Anal. Biochem , vol.421 , pp. 640-648
    • Pai, J.C.1    Entzminger, K.C.2    Maynard, J.A.3
  • 39
    • 84876471612 scopus 로고    scopus 로고
    • Exploring the potential of megaprimer PCR in coupling with orthogonal array design for mutagenesis library
    • Tang, L., K. Zheng, Y. Liu, Z. Zheng, H. Wang, C. Song, and H. Zhou. 2013. Exploring the potential of megaprimer PCR in coupling with orthogonal array design for mutagenesis library. Biotechnol. Appl. Biochem. 60: 190-195.
    • (2013) Biotechnol. Appl. Biochem , vol.60 , pp. 190-195
    • Tang, L.1    Zheng, K.2    Liu, Y.3    Zheng, Z.4    Wang, H.5    Song, C.6    Zhou, H.7


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