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Volumn 4, Issue , 2005, Pages

Directed evolution strategies for improved enzymatic performance

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL ENZYME;

EID: 33645781503     PISSN: 14752859     EISSN: 14752859     Source Type: Journal    
DOI: 10.1186/1475-2859-4-29     Document Type: Review
Times cited : (88)

References (48)
  • 1
  • 2
    • 0037436563 scopus 로고    scopus 로고
    • Dispelling the myths - Biocatalysis in industrial synthesis
    • Schoemaker HE, Mink D, Wubbolts MG: Dispelling the myths--biocatalysis in industrial synthesis. Science 2003, 299:1694-1697.
    • (2003) Science , vol.299 , pp. 1694-1697
    • Schoemaker, H.E.1    Mink, D.2    Wubbolts, M.G.3
  • 3
    • 0036900263 scopus 로고    scopus 로고
    • The production of fine chemicals by biotransformations
    • Straathof AJ, Panke S, Schmid A: The production of fine chemicals by biotransformations. Curr Opin Biotechnol 2002, 13:548-556.
    • (2002) Curr Opin Biotechnol , vol.13 , pp. 548-556
    • Straathof, A.J.1    Panke, S.2    Schmid, A.3
  • 4
    • 0042430535 scopus 로고    scopus 로고
    • Optimising enzyme function by directed evolution
    • Dalby PA: Optimising enzyme function by directed evolution. Curr Opin Struct Biol 2003, 13:500-505.
    • (2003) Curr Opin Struct Biol , vol.13 , pp. 500-505
    • Dalby, P.A.1
  • 6
    • 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 FH: Tuning the activity of an enzyme for unusual environments: sequential random mutagenesis of subtilisin E for catalysis in dimethylformamide. Proc Natl Acad Sci U S A 1993, 90:5618-5622.
    • (1993) Proc Natl Acad Sci U S A , vol.90 , pp. 5618-5622
    • Chen, K.1    Arnold, F.H.2
  • 7
    • 0028050350 scopus 로고
    • Rapid evolution of a protein in vitro by DNA shuffling
    • Stemmer WPC: Rapid evolution of a protein in vitro by DNA shuffling. Nature 1994, 370:389-391.
    • (1994) Nature , vol.370 , pp. 389-391
    • Stemmer, W.P.C.1
  • 8
    • 0031909113 scopus 로고    scopus 로고
    • Molecular evolution by staggered extension process (StEP) in vitro recombination
    • [see comments]
    • Zhao H, Giver L, Shao Z, Affholter JA, Arnold FH: Molecular evolution by staggered extension process (StEP) in vitro recombination [see comments]. Nat Biotechnol 1998, 16:258-261.
    • (1998) Nat Biotechnol , vol.16 , pp. 258-261
    • Zhao, H.1    Giver, L.2    Shao, Z.3    Affholter, J.A.4    Arnold, F.H.5
  • 10
    • 17444363724 scopus 로고    scopus 로고
    • A combinatorial approach to hybrid enzymes independent of DNA homology
    • Ostermeier M, Shim JH, Benkovic SJ: A combinatorial approach to hybrid enzymes independent of DNA homology. Nat Biotechnol 1999, 17:1205-1209.
    • (1999) Nat Biotechnol , vol.17 , pp. 1205-1209
    • Ostermeier, M.1    Shim, J.H.2    Benkovic, S.J.3
  • 11
    • 1842842876 scopus 로고    scopus 로고
    • Creating random mutagenesis libraries using megaprimer PCR of whole plasmid
    • Miyazaki K, Takenouchi M: Creating random mutagenesis libraries using megaprimer PCR of whole plasmid. Biotechniques 2002, 33:1033-1038.
    • (2002) Biotechniques , vol.33 , pp. 1033-1038
    • Miyazaki, K.1    Takenouchi, M.2
  • 14
    • 20544449855 scopus 로고    scopus 로고
    • Why high-error-rate random mutagenesis libraries are enriched in functional and improved proteins
    • Drummond DA, Iverson BL, Georgiou G, Arnold FH: Why high-error-rate random mutagenesis libraries are enriched in functional and improved proteins. J Mol Biol 2005, 350:806-816.
    • (2005) J Mol Biol , vol.350 , pp. 806-816
    • Drummond, D.A.1    Iverson, B.L.2    Georgiou, G.3    Arnold, F.H.4
  • 15
    • 12344337569 scopus 로고    scopus 로고
    • Focusing mutations into the P. fluorescens esterase binding site increases enantioselectivity more effectively than distant mutations
    • Park S, Morley KL, Horsman GP, Holmquist M, Hult K, Kazlauskas RJ: Focusing mutations into the P. fluorescens esterase binding site increases enantioselectivity more effectively than distant mutations. Chemistry & Biology 2005, 12:45-54.
    • (2005) Chemistry & Biology , vol.12 , pp. 45-54
    • Park, S.1    Morley, K.L.2    Horsman, G.P.3    Holmquist, M.4    Hult, K.5    Kazlauskas, R.J.6
  • 16
    • 14644433770 scopus 로고    scopus 로고
    • Combinatorial exploration of the catalytic site of a drug- resistant dihydrofolate reductase: Creating alternative functional configurations
    • Schmitzer AR, Lepine F, Pelletier JN: Combinatorial exploration of the catalytic site of a drug- resistant dihydrofolate reductase: creating alternative functional configurations. Protein Engineering Design & Selection 2004, 17:809-819.
    • (2004) Protein Engineering Design & Selection , vol.17 , pp. 809-819
    • Schmitzer, A.R.1    Lepine, F.2    Pelletier, J.N.3
  • 18
    • 24044554219 scopus 로고    scopus 로고
    • Site-saturation mutagenesis is more efficient than DNA shuffling for the directed evolution of b-fucosidase from b-galactosidase
    • Parikh MR, Matsumura I: Site-saturation mutagenesis is more efficient than DNA shuffling for the directed evolution of b-fucosidase from b-galactosidase. J Mol Biol 2005, 352:621-628.
    • (2005) J Mol Biol , vol.352 , pp. 621-628
    • Parikh, M.R.1    Matsumura, I.2
  • 19
    • 18144403554 scopus 로고    scopus 로고
    • Improving enzyme properties: When are closer mutations better?
    • Morley KL, Kazlauskas RJ: Improving enzyme properties: when are closer mutations better? Trends in Biotechnology 2005, 23:231-237.
    • (2005) Trends in Biotechnology , vol.23 , pp. 231-237
    • Morley, K.L.1    Kazlauskas, R.J.2
  • 23
    • 18044366809 scopus 로고    scopus 로고
    • A thermostable variant of fructose bisphosphate aldolase constructed by directed evolution also shows increased stability in organic solvents
    • Hao JJ, Berry A: A thermostable variant of fructose bisphosphate aldolase constructed by directed evolution also shows increased stability in organic solvents. Protein Engineering Design & Selection 2004, 17:689-697.
    • (2004) Protein Engineering Design & Selection , vol.17 , pp. 689-697
    • Hao, J.J.1    Berry, A.2
  • 26
    • 18744388856 scopus 로고    scopus 로고
    • Engineering of protease variants exhibiting high catalytic activity and exquisite substrate selectivity
    • Varadarajan N, Gam J, Olsen MJ, Georgiou G, Iverson BL: Engineering of protease variants exhibiting high catalytic activity and exquisite substrate selectivity. Proc Natl Acad Sci U S A 2005, 102:6855-6860.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 6855-6860
    • Varadarajan, N.1    Gam, J.2    Olsen, M.J.3    Georgiou, G.4    Iverson, B.L.5
  • 27
    • 0033178525 scopus 로고    scopus 로고
    • Beyond binding: Using phage display to select for structure, folding and enzymatic activity in proteins
    • Forrer P, Jung S, Pluckthun A: Beyond binding: using phage display to select for structure, folding and enzymatic activity in proteins. Curr Opin Struct Biol 1999, 9:514-520.
    • (1999) Curr Opin Struct Biol , vol.9 , pp. 514-520
    • Forrer, P.1    Jung, S.2    Pluckthun, A.3
  • 28
  • 29
    • 0025187838 scopus 로고
    • Substrate specificity of trypsin investigated by using a genetic selection
    • Evnin LB, Vasquez JR, Craik CS: Substrate specificity of trypsin investigated by using a genetic selection. Proc Natl Acad Sci U S A 1990, 87:6659-6663.
    • (1990) Proc Natl Acad Sci U S A , vol.87 , pp. 6659-6663
    • Evnin, L.B.1    Vasquez, J.R.2    Craik, C.S.3
  • 31
    • 0033582608 scopus 로고    scopus 로고
    • A strategy for the isolation of catalytic activities from repertoires of enzymes displayed on phage
    • Demartis S, Huber A, Viti F, Lozzi L, Giovannoni L, Neri P, Winter G, Neri D: A strategy for the isolation of catalytic activities from repertoires of enzymes displayed on phage. J Mol Biol 1999, 286:617-633.
    • (1999) J Mol Biol , vol.286 , pp. 617-633
    • Demartis, S.1    Huber, A.2    Viti, F.3    Lozzi, L.4    Giovannoni, L.5    Neri, P.6    Winter, G.7    Neri, D.8
  • 32
    • 0032509131 scopus 로고    scopus 로고
    • Probing the importance of second sphere residues in an esterolytic antibody by phage display
    • Arkin MR, Wells JA. Probing the importance of second sphere residues in an esterolytic antibody by phage display. J Mol Biol 1998, 284:1083-1094.
    • (1998) J Mol Biol , vol.284 , pp. 1083-1094
    • Arkin, M.R.1    Wells, J.A.2
  • 33
    • 0035121685 scopus 로고    scopus 로고
    • Specific glycosidase activity isolated from a random phage display antibody library
    • Goud GN, Artsaenko O, Bols M, Sierks M: Specific glycosidase activity isolated from a random phage display antibody library. Biotechnol Prog 2001, 17:197-202.
    • (2001) Biotechnol Prog , vol.17 , pp. 197-202
    • Goud, G.N.1    Artsaenko, O.2    Bols, M.3    Sierks, M.4
  • 34
    • 0029008514 scopus 로고
    • Glutathione Transferases with Novel Active-Sites Isolated by Phage Display from A Library of Random Mutants
    • Widersten M, Mannervik B: Glutathione Transferases with Novel Active-Sites Isolated by Phage Display from A Library of Random Mutants. Journal of Molecular Biology 1995, 250:115-122.
    • (1995) Journal of Molecular Biology , vol.250 , pp. 115-122
    • Widersten, M.1    Mannervik, B.2
  • 37
    • 0035807809 scopus 로고    scopus 로고
    • Enzyme-like proteins by computational design
    • Bolon DN, Mayo SL: Enzyme-like proteins by computational design. Proc Natl Acad Sci U S A 2001, 98:14274-14279.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 14274-14279
    • Bolon, D.N.1    Mayo, S.L.2
  • 38
    • 3042655537 scopus 로고    scopus 로고
    • Computational design of a biologically active enzyme
    • Dwyer MA, Looger LL, Hellinga HW: Computational design of a biologically active enzyme. Science 2004, 304:1967-1971.
    • (2004) Science , vol.304 , pp. 1967-1971
    • Dwyer, M.A.1    Looger, L.L.2    Hellinga, H.W.3
  • 40
    • 18844410540 scopus 로고    scopus 로고
    • Computationally designed variants of Escherichia coli chorismate mutase show altered catalytic activity
    • Lassila JK, Keeffe JR, Oelschlaeger P, Mayo SL: Computationally designed variants of Escherichia coli chorismate mutase show altered catalytic activity. Protein Engineering Design & Selection 2005, 18:161-163.
    • (2005) Protein Engineering Design & Selection , vol.18 , pp. 161-163
    • Lassila, J.K.1    Keeffe, J.R.2    Oelschlaeger, P.3    Mayo, S.L.4
  • 41
    • 0035818409 scopus 로고    scopus 로고
    • Directed evolution of single proteins, metabolic pathways, and viruses
    • Schmidt-Dannert C: Directed evolution of single proteins, metabolic pathways, and viruses. Biochemistry 2001, 40:13125-13136.
    • (2001) Biochemistry , vol.40 , pp. 13125-13136
    • Schmidt-Dannert, C.1
  • 42
    • 0030951186 scopus 로고    scopus 로고
    • Molecular evolution of an arsenate detoxification pathway by DNA shuffling
    • [see comments]
    • Crameri A, Dawes G, Rodriguez EJ, Silver S, Stemmer WP: Molecular evolution of an arsenate detoxification pathway by DNA shuffling [see comments]. Nat Biotechnol 1997, 15:436-438.
    • (1997) Nat Biotechnol , vol.15 , pp. 436-438
    • Crameri, A.1    Dawes, G.2    Rodriguez, E.J.3    Silver, S.4    Stemmer, W.P.5
  • 43
    • 0034518317 scopus 로고    scopus 로고
    • Directed evolution of metabolically engineered Escherichia coli for carotenoid production
    • Wang CW, Oh MK, Liao JC: Directed evolution of metabolically engineered Escherichia coli for carotenoid production. Biotechnology Progress 2000, 16:922-926.
    • (2000) Biotechnology Progress , vol.16 , pp. 922-926
    • Wang, C.W.1    Oh, M.K.2    Liao, J.C.3
  • 44
    • 0035798705 scopus 로고    scopus 로고
    • Alteration of product specificity of Rhodobacter sphaeroides phytoene desaturase by directed evolution
    • Wang CW, Liao JC: Alteration of product specificity of Rhodobacter sphaeroides phytoene desaturase by directed evolution. Journal Of Biological Chemistry 2001, 276:41161-41164.
    • (2001) Journal of Biological Chemistry , vol.276 , pp. 41161-41164
    • Wang, C.W.1    Liao, J.C.2
  • 45
    • 0033941389 scopus 로고    scopus 로고
    • Molecular breeding of carotenoid biosynthetic pathways
    • Schmidt-Dannert C, Umeno D, Arnold FH: Molecular breeding of carotenoid biosynthetic pathways. Nat Biotechnol 2000, 18:750-753.
    • (2000) Nat Biotechnol , vol.18 , pp. 750-753
    • Schmidt-Dannert, C.1    Umeno, D.2    Arnold, F.H.3
  • 46
    • 1342304132 scopus 로고    scopus 로고
    • Evolution of a pathway to novel longchain carotenoids
    • Umeno D, Arnold FH: Evolution of a pathway to novel longchain carotenoids. Journal of Bacteriology 2004, 186:1531-1536.
    • (2004) Journal of Bacteriology , vol.186 , pp. 1531-1536
    • Umeno, D.1    Arnold, F.H.2
  • 47
    • 17844400062 scopus 로고    scopus 로고
    • Identification of a carotenoid oxygenase synthesizing acyclic xanthophylls: Combinatorial biosynthesis and directed evolution
    • Mijts BN, Lee PC, Schmidt-Dannert C: Identification of a carotenoid oxygenase synthesizing acyclic xanthophylls: Combinatorial biosynthesis and directed evolution. Chemistry & Biology 2005, 12:453-460.
    • (2005) Chemistry & Biology , vol.12 , pp. 453-460
    • Mijts, B.N.1    Lee, P.C.2    Schmidt-Dannert, C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.