메뉴 건너뛰기




Volumn 21, Issue 4, 2011, Pages 473-480

Strategy and success for the directed evolution of enzymes

Author keywords

[No Author keywords available]

Indexed keywords

BETA LACTAMASE TEM 1; ESTERASE; TRIACYLGLYCEROL LIPASE;

EID: 80052102623     PISSN: 0959440X     EISSN: 1879033X     Source Type: Journal    
DOI: 10.1016/j.sbi.2011.05.003     Document Type: Review
Times cited : (171)

References (65)
  • 1
    • 0033982936 scopus 로고    scopus 로고
    • KEGG: kyoto encyclopedia of genes and genomes
    • Kanehisa M., Goto S. KEGG: kyoto encyclopedia of genes and genomes. Nucleic Acids Res 2000, 28:27-30.
    • (2000) Nucleic Acids Res , vol.28 , pp. 27-30
    • Kanehisa, M.1    Goto, S.2
  • 2
    • 1842531448 scopus 로고    scopus 로고
    • Recent progress in biocatalyst discovery and optimization
    • Robertson D.E., Steer B.A. Recent progress in biocatalyst discovery and optimization. Curr Opin Chem Biol 2004, 8:141-149.
    • (2004) Curr Opin Chem Biol , vol.8 , pp. 141-149
    • Robertson, D.E.1    Steer, B.A.2
  • 3
    • 33748525883 scopus 로고    scopus 로고
    • Enzyme promiscuity: evolutionary and mechanistic aspects
    • Khersonsky O., Roodveldt C., Tawfik D.S. Enzyme promiscuity: evolutionary and mechanistic aspects. Curr Opin Chem Biol 2006, 10:498-508.
    • (2006) Curr Opin Chem Biol , vol.10 , pp. 498-508
    • Khersonsky, O.1    Roodveldt, C.2    Tawfik, D.S.3
  • 5
    • 68049106179 scopus 로고    scopus 로고
    • Directed evolution drives the next generation of biocatalysts
    • Turner N.J. Directed evolution drives the next generation of biocatalysts. Nat Chem Biol 2009, 5:568-574.
    • (2009) Nat Chem Biol , vol.5 , pp. 568-574
    • Turner, N.J.1
  • 6
    • 0019874718 scopus 로고
    • Changes in the substrate specificities of an enzyme during directed evolution of new functions
    • Hall B.G. Changes in the substrate specificities of an enzyme during directed evolution of new functions. Biochemistry 1981, 20:4042-4049.
    • (1981) Biochemistry , vol.20 , pp. 4042-4049
    • Hall, B.G.1
  • 7
    • 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 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
  • 8
    • 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 1994, 370:389-391.
    • (1994) Nature , vol.370 , pp. 389-391
    • Stemmer, W.P.1
  • 9
    • 0031909113 scopus 로고    scopus 로고
    • Molecular evolution by staggered extension process (StEP) in vitro recombination
    • Zhao H., Giver L., Shao Z., Affholter J.A., Arnold F.H. Molecular evolution by staggered extension process (StEP) in vitro recombination. 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
    • 0033280672 scopus 로고    scopus 로고
    • Exploring nonnatural evolutionary pathways by saturation mutagenesis: rapid improvement of protein function
    • Miyazaki K., Arnold F.H. Exploring nonnatural evolutionary pathways by saturation mutagenesis: rapid improvement of protein function. J Mol Evol 1999, 49:716-720.
    • (1999) J Mol Evol , vol.49 , pp. 716-720
    • Miyazaki, K.1    Arnold, F.H.2
  • 11
    • 0022479114 scopus 로고
    • Cloning of random-sequence oligodeoxynucleotides
    • Oliphant A.R., Nussbaum A.L., Struhl K. Cloning of random-sequence oligodeoxynucleotides. Gene 1986, 44:177-183.
    • (1986) Gene , vol.44 , pp. 177-183
    • Oliphant, A.R.1    Nussbaum, A.L.2    Struhl, K.3
  • 12
    • 2342535792 scopus 로고    scopus 로고
    • Sequence saturation mutagenesis (SeSaM): a novel method for directed evolution
    • Wong T.S., Tee K.L., Hauer B., Schwaneberg U. Sequence saturation mutagenesis (SeSaM): a novel method for directed evolution. Nucleic Acids Res 2004, 32:e26.
    • (2004) Nucleic Acids Res , vol.32
    • Wong, T.S.1    Tee, K.L.2    Hauer, B.3    Schwaneberg, U.4
  • 13
    • 73849104591 scopus 로고    scopus 로고
    • USER friendly DNA recombination (USERec): a simple and flexible near homology-independent method for gene library construction
    • Villiers B.R., Stein V., Hollfelder F. USER friendly DNA recombination (USERec): a simple and flexible near homology-independent method for gene library construction. Protein Eng Des Sel 2010, 23:1-8.
    • (2010) Protein Eng Des Sel , vol.23 , pp. 1-8
    • Villiers, B.R.1    Stein, V.2    Hollfelder, F.3
  • 14
    • 0035025314 scopus 로고    scopus 로고
    • Libraries of hybrid proteins from distantly related sequences
    • Sieber V., Martinez C.A., Arnold F.H. Libraries of hybrid proteins from distantly related sequences. Nat Biotechnol 2001, 19:456-460.
    • (2001) Nat Biotechnol , vol.19 , pp. 456-460
    • Sieber, V.1    Martinez, C.A.2    Arnold, F.H.3
  • 15
    • 33644852766 scopus 로고    scopus 로고
    • RAISE: a simple and novel method of generating random insertion and deletion mutations
    • Fujii R., Kitaoka M., Hayashi K. RAISE: a simple and novel method of generating random insertion and deletion mutations. Nucleic Acids Res 2006, 34:e30.
    • (2006) Nucleic Acids Res , vol.34
    • Fujii, R.1    Kitaoka, M.2    Hayashi, K.3
  • 16
    • 0035014185 scopus 로고    scopus 로고
    • Directed evolution of proteins by exon shuffling
    • Kolkman J.A., Stemmer W.P. Directed evolution of proteins by exon shuffling. Nat Biotechnol 2001, 19:423-428.
    • (2001) Nat Biotechnol , vol.19 , pp. 423-428
    • Kolkman, J.A.1    Stemmer, W.P.2
  • 17
    • 48749101428 scopus 로고    scopus 로고
    • Picomolar affinity fibronectin domains engineered utilizing loop length diversity, recursive mutagenesis, and loop shuffling
    • Hackel B.J., Kapila A., Wittrup K.D. Picomolar affinity fibronectin domains engineered utilizing loop length diversity, recursive mutagenesis, and loop shuffling. J Mol Biol 2008, 381:1238-1252.
    • (2008) J Mol Biol , vol.381 , pp. 1238-1252
    • Hackel, B.J.1    Kapila, A.2    Wittrup, K.D.3
  • 19
    • 70450242805 scopus 로고    scopus 로고
    • Exploring protein fitness landscapes by directed evolution
    • Romero P.A., Arnold F.H. Exploring protein fitness landscapes by directed evolution. Nat Rev Mol Cell Biol 2009, 10:866-876.
    • (2009) Nat Rev Mol Cell Biol , vol.10 , pp. 866-876
    • Romero, P.A.1    Arnold, F.H.2
  • 20
    • 33645781503 scopus 로고    scopus 로고
    • Directed evolution strategies for improved enzymatic performance
    • Hibbert E.G., Dalby P.A. Directed evolution strategies for improved enzymatic performance. Microbial Cell Fact 2005, 4:29.
    • (2005) Microbial Cell Fact , vol.4 , pp. 29
    • Hibbert, E.G.1    Dalby, P.A.2
  • 21
    • 0014935646 scopus 로고
    • Natural selection and the concept of a protein space
    • Smith J.M. Natural selection and the concept of a protein space. Nature 1970, 225:563-564.
    • (1970) Nature , vol.225 , pp. 563-564
    • Smith, J.M.1
  • 22
    • 18044364063 scopus 로고    scopus 로고
    • Rapid creation of a novel protein function by in vitro coevolution
    • Chen Z., Zhao H. Rapid creation of a novel protein function by in vitro coevolution. J Mol Biol 2005, 348:1273-1282.
    • (2005) J Mol Biol , vol.348 , pp. 1273-1282
    • Chen, Z.1    Zhao, H.2
  • 24
    • 66649132872 scopus 로고    scopus 로고
    • Chaperonin overexpression promotes genetic variation and enzyme evolution
    • This paper has significant implications for understanding the evolutionary mechanisms that allow new functions to evolve in nature. Chaperones provide a natural buffer for the intrinsic loss of protein stability and correct folding which allows greater diversification of gene pools through the accumulation of non-deleterious mutations. The authors show how co-expression with a chaperone in E. coli
    • Tokuriki N., Tawfik D.S. Chaperonin overexpression promotes genetic variation and enzyme evolution. Nature 2009, 459:668-673. This paper has significant implications for understanding the evolutionary mechanisms that allow new functions to evolve in nature. Chaperones provide a natural buffer for the intrinsic loss of protein stability and correct folding which allows greater diversification of gene pools through the accumulation of non-deleterious mutations. The authors show how co-expression with a chaperone in E. coli relaxes the selective pressure on stability and folding, and then allows enzymes with much higher activities to be evolved than in the absence of chaperone.
    • (2009) Nature , vol.459 , pp. 668-673
    • Tokuriki, N.1    Tawfik, D.S.2
  • 25
    • 0033555718 scopus 로고    scopus 로고
    • The effect of high-frequency random mutagenesis on in vitro protein evolution: a study on TEM-1 beta-lactamase
    • Zaccolo M., Gherardi E. The effect of high-frequency random mutagenesis on in vitro protein evolution: a study on TEM-1 beta-lactamase. J Mol Biol 1999, 285:775-783.
    • (1999) J Mol Biol , vol.285 , pp. 775-783
    • Zaccolo, M.1    Gherardi, E.2
  • 26
    • 18144403554 scopus 로고    scopus 로고
    • Improving enzyme properties: when are closer mutations better?
    • Morley K.L., Kazlauskas R.J. Improving enzyme properties: when are closer mutations better?. Trends Biotechnol 2005, 23:231-237.
    • (2005) Trends Biotechnol , vol.23 , pp. 231-237
    • Morley, K.L.1    Kazlauskas, R.J.2
  • 27
    • 12344337569 scopus 로고    scopus 로고
    • Focusing mutations into the P. fluorescens esterase binding site increases enantioselectivity more effectively than distant mutations
    • Park S., Morley K.L., Horsman G.P., Holmquist M., Hult K., Kazlauskas R.J. Focusing mutations into the P. fluorescens esterase binding site increases enantioselectivity more effectively than distant mutations. Chem Biol 2005, 12:45-54.
    • (2005) Chem Biol , 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
  • 28
    • 67651171257 scopus 로고    scopus 로고
    • Distributions of enzyme residues yielding mutants with improved substrate specificities from two different directed evolution strategies
    • The potency and efficiency of random mutagenesis and saturation mutagenesis methods are compared by analyzing examples in the literature in which substrate preference is improved. Saturation mutagenesis is found to access more residues that are in direct contact with catalytic residues, cofactors or substrate than random mutagenesis by error-prone PCR. Furthermore, saturation mutagenesis is more l
    • Paramesvaran J., Hibbert E.G., Russell A.J., Dalby P.A. Distributions of enzyme residues yielding mutants with improved substrate specificities from two different directed evolution strategies. Protein Eng Des Sel 2009, 22:401-411. The potency and efficiency of random mutagenesis and saturation mutagenesis methods are compared by analyzing examples in the literature in which substrate preference is improved. Saturation mutagenesis is found to access more residues that are in direct contact with catalytic residues, cofactors or substrate than random mutagenesis by error-prone PCR. Furthermore, saturation mutagenesis is more likely to find beneficial variants at conserved residues than for epPCR.
    • (2009) Protein Eng Des Sel , vol.22 , pp. 401-411
    • Paramesvaran, J.1    Hibbert, E.G.2    Russell, A.J.3    Dalby, P.A.4
  • 29
    • 68749107059 scopus 로고    scopus 로고
    • Protein sectors: evolutionary units of three-dimensional structure
    • Statistical analysis of multiple sequence alignments is used to determine networks of residues that co-evolve. Several networks are found in many proteins that correspond to distinct functional roles or 'sectors'. Understanding these sectors and the networks of residues that create them plays a critical role in understanding the natural evolution of proteins a
    • Halabi N., Rivoire O., Leibler S., Ranganathan R. Protein sectors: evolutionary units of three-dimensional structure. Cell 2009, 138:774-786. Statistical analysis of multiple sequence alignments is used to determine networks of residues that co-evolve. Several networks are found in many proteins that correspond to distinct functional roles or 'sectors'. Understanding these sectors and the networks of residues that create them plays a critical role in understanding the natural evolution of proteins and will also inform directed evolution strategies to either avoid or exploit them.
    • (2009) Cell , vol.138 , pp. 774-786
    • Halabi, N.1    Rivoire, O.2    Leibler, S.3    Ranganathan, R.4
  • 30
    • 0036384211 scopus 로고    scopus 로고
    • Structural bases of stability-function tradeoffs in enzymes
    • Beadle B.M., Shoichet B.K. Structural bases of stability-function tradeoffs in enzymes. J Mol Biol 2002, 321:285-296.
    • (2002) J Mol Biol , vol.321 , pp. 285-296
    • Beadle, B.M.1    Shoichet, B.K.2
  • 32
    • 0036295508 scopus 로고    scopus 로고
    • Evolution of an antibiotic resistance enzyme constrained by stability and activity trade-offs
    • Wang X., Minasov G., Shoichet B.K. Evolution of an antibiotic resistance enzyme constrained by stability and activity trade-offs. J Mol Biol 2002, 320:85-95.
    • (2002) J Mol Biol , vol.320 , pp. 85-95
    • Wang, X.1    Minasov, G.2    Shoichet, B.K.3
  • 33
    • 77954274719 scopus 로고    scopus 로고
    • Iterative saturation mutagenesis accelerates laboratory evolution of enzyme stereoselectivity: rigorous comparison with traditional methods
    • Reetz M.T., Prasad S., Carballeira J.D., Gumulya Y., Bocola M. Iterative saturation mutagenesis accelerates laboratory evolution of enzyme stereoselectivity: rigorous comparison with traditional methods. J Am Chem Soc 2010, 132:9144-9152.
    • (2010) J Am Chem Soc , vol.132 , pp. 9144-9152
    • Reetz, M.T.1    Prasad, S.2    Carballeira, J.D.3    Gumulya, Y.4    Bocola, M.5
  • 34
    • 77956234144 scopus 로고    scopus 로고
    • Natural diversity to guide focused directed evolution
    • Jochens H., Bornscheuer U.T. Natural diversity to guide focused directed evolution. Chembiochem 2010, 11:1861-1866.
    • (2010) Chembiochem , vol.11 , pp. 1861-1866
    • Jochens, H.1    Bornscheuer, U.T.2
  • 35
    • 33748053033 scopus 로고    scopus 로고
    • Improving nature's enzyme active site with genetically encoded unnatural amino acids
    • Jackson J.C., Duffy S.P., Hess K.R., Mehl R.A. Improving nature's enzyme active site with genetically encoded unnatural amino acids. J Am Chem Soc 2006, 128:11124-11127.
    • (2006) J Am Chem Soc , vol.128 , pp. 11124-11127
    • Jackson, J.C.1    Duffy, S.P.2    Hess, K.R.3    Mehl, R.A.4
  • 36
    • 27544497498 scopus 로고    scopus 로고
    • Combination of computational prescreening and experimental library construction can accelerate enzyme optimization by directed evolution
    • Funke S.A., Otte N., Eggert T., Bocola M., Jaeger K.E., Thiel W. Combination of computational prescreening and experimental library construction can accelerate enzyme optimization by directed evolution. Protein Eng Des Sel 2005, 18:509-514.
    • (2005) Protein Eng Des Sel , vol.18 , pp. 509-514
    • Funke, S.A.1    Otte, N.2    Eggert, T.3    Bocola, M.4    Jaeger, K.E.5    Thiel, W.6
  • 37
    • 33846102955 scopus 로고    scopus 로고
    • Computationally designed libraries of fluorescent proteins evaluated by preservation and diversity of function
    • Treynor T.P., Vizcarra C.L., Nedelcu D., Mayo S.L. Computationally designed libraries of fluorescent proteins evaluated by preservation and diversity of function. Proc Natl Acad Sci U S A 2007, 104:48-53.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 48-53
    • Treynor, T.P.1    Vizcarra, C.L.2    Nedelcu, D.3    Mayo, S.L.4
  • 38
    • 0035424955 scopus 로고    scopus 로고
    • Engineering proteins for thermostability: the use of sequence alignments versus rational design and directed evolution
    • Lehmann M., Wyss M. Engineering proteins for thermostability: the use of sequence alignments versus rational design and directed evolution. Curr Opin Biotechnol 2001, 12:371-375.
    • (2001) Curr Opin Biotechnol , vol.12 , pp. 371-375
    • Lehmann, M.1    Wyss, M.2
  • 40
    • 78149450306 scopus 로고    scopus 로고
    • Increasing the stability of an enzyme toward hostile organic solvents by directed evolution based on iterative saturation mutagenesis using the B-FIT method
    • While the consensus method creates a more stable protein sequence on the assumption that most residues are selected for stability on average, the B-FIT method uses structural data from crystallography to identify target residues that are the most mobile. Thermostable enzymes are known to be more rigid, and so randomly mutating the more mobile residues in a structure was an insightful strategy that
    • Reetz M.T., Soni P., Fernandez L., Gumulya Y., Carballeira J.D. Increasing the stability of an enzyme toward hostile organic solvents by directed evolution based on iterative saturation mutagenesis using the B-FIT method. Chem Commun (Camb) 2010, 46:8657-8658. While the consensus method creates a more stable protein sequence on the assumption that most residues are selected for stability on average, the B-FIT method uses structural data from crystallography to identify target residues that are the most mobile. Thermostable enzymes are known to be more rigid, and so randomly mutating the more mobile residues in a structure was an insightful strategy that successfully identified mutants with improved thermostability.
    • (2010) Chem Commun (Camb) , vol.46 , pp. 8657-8658
    • Reetz, M.T.1    Soni, P.2    Fernandez, L.3    Gumulya, Y.4    Carballeira, J.D.5
  • 41
    • 78649277331 scopus 로고    scopus 로고
    • Thermostabilization of an esterase by alignment-guided focussed directed evolution
    • Jochens H., Aerts D., Bornscheuer U.T. Thermostabilization of an esterase by alignment-guided focussed directed evolution. Protein Eng Des Sel 2010, 23:903-909.
    • (2010) Protein Eng Des Sel , vol.23 , pp. 903-909
    • Jochens, H.1    Aerts, D.2    Bornscheuer, U.T.3
  • 42
    • 79955534060 scopus 로고    scopus 로고
    • A system for the continuous directed evolution of biomolecules
    • Esvelt K.M., Carlson J.C., Liu D.R. A system for the continuous directed evolution of biomolecules. Nature 2011, 472:499-503.
    • (2011) Nature , vol.472 , pp. 499-503
    • Esvelt, K.M.1    Carlson, J.C.2    Liu, D.R.3
  • 45
    • 78649529303 scopus 로고    scopus 로고
    • Multiple global suppressors of protein stability defects facilitate the evolution of extended-spectrum TEM beta-lactamases
    • Brown N.G., Pennington J.M., Huang W., Ayvaz T., Palzkill T. Multiple global suppressors of protein stability defects facilitate the evolution of extended-spectrum TEM beta-lactamases. J Mol Biol 2010, 404:832-846.
    • (2010) J Mol Biol , vol.404 , pp. 832-846
    • Brown, N.G.1    Pennington, J.M.2    Huang, W.3    Ayvaz, T.4    Palzkill, T.5
  • 46
    • 44649102734 scopus 로고    scopus 로고
    • Improving activity and stability of cutinase towards the anionic detergent AOT by complete saturation mutagenesis
    • Brissos V., Eggert T., Cabral J.M.S., Jaeger K.E. Improving activity and stability of cutinase towards the anionic detergent AOT by complete saturation mutagenesis. Protein Eng Des Sel 2008, 21:387-393.
    • (2008) Protein Eng Des Sel , vol.21 , pp. 387-393
    • Brissos, V.1    Eggert, T.2    Cabral, J.M.S.3    Jaeger, K.E.4
  • 47
    • 33750353815 scopus 로고    scopus 로고
    • Directed evolution by accumulating tailored mutations: thermostabilization of lactate oxidase with less trade-off with catalytic activity
    • Hamamatsu N., Nomiya Y., Aita T., Nakajima M., Husimi Y., Shibanaka Y. Directed evolution by accumulating tailored mutations: thermostabilization of lactate oxidase with less trade-off with catalytic activity. Protein Eng Des Sel 2006, 19:483-489.
    • (2006) Protein Eng Des Sel , vol.19 , pp. 483-489
    • Hamamatsu, N.1    Nomiya, Y.2    Aita, T.3    Nakajima, M.4    Husimi, Y.5    Shibanaka, Y.6
  • 48
    • 56149121547 scopus 로고    scopus 로고
    • Directed enzyme evolution via small and effective neutral drift libraries
    • Gupta R.D., Tawfik D.S. Directed enzyme evolution via small and effective neutral drift libraries. Nat Methods 2008, 5:939-942.
    • (2008) Nat Methods , vol.5 , pp. 939-942
    • Gupta, R.D.1    Tawfik, D.S.2
  • 49
    • 70350110646 scopus 로고    scopus 로고
    • Creation of an amino acid network of structurally coupled residues in the directed evolution of a thermostable enzyme
    • Reetz M.T., Soni P., Acevedo J.P., Sanchis J. Creation of an amino acid network of structurally coupled residues in the directed evolution of a thermostable enzyme. Angew Chem-Int Ed 2009, 48:8268-8272.
    • (2009) Angew Chem-Int Ed , vol.48 , pp. 8268-8272
    • Reetz, M.T.1    Soni, P.2    Acevedo, J.P.3    Sanchis, J.4
  • 51
    • 77954797329 scopus 로고    scopus 로고
    • Biocatalytic asymmetric synthesis of chiral amines from ketones applied to sitagliptin manufacture
    • By far the most comprehensive, outstanding and practical example of directed evolution published to date. This paper combines many directed evolution techniques and strategies at various stages of development for an industrially useful transaminase. Multiple properties were evolved, some sequentially and some simultaneously, to obtain an enzyme that can operate on a completely novel substrate, at
    • Savile C.K., Janey J.M., Mundorff E.C., Moore J.C., Tam S., Jarvis W.R., Colbeck J.C., Krebber A., Fleitz F.J., Brands J., et al. Biocatalytic asymmetric synthesis of chiral amines from ketones applied to sitagliptin manufacture. Science 2010, 329:305-309. By far the most comprehensive, outstanding and practical example of directed evolution published to date. This paper combines many directed evolution techniques and strategies at various stages of development for an industrially useful transaminase. Multiple properties were evolved, some sequentially and some simultaneously, to obtain an enzyme that can operate on a completely novel substrate, at high substrate concentration, high temperature and in the presence of 50% cosolvent.
    • (2010) Science , vol.329 , pp. 305-309
    • Savile, C.K.1    Janey, J.M.2    Mundorff, E.C.3    Moore, J.C.4    Tam, S.5    Jarvis, W.R.6    Colbeck, J.C.7    Krebber, A.8    Fleitz, F.J.9    Brands, J.10
  • 52
    • 16844379112 scopus 로고    scopus 로고
    • Directed evolution of the promiscuous esterase activity of carbonic anhydrase II
    • Gould S.M., Tawfik D.S. Directed evolution of the promiscuous esterase activity of carbonic anhydrase II. Biochemistry 2005, 44:5444-5452.
    • (2005) Biochemistry , vol.44 , pp. 5444-5452
    • Gould, S.M.1    Tawfik, D.S.2
  • 55
    • 33750070283 scopus 로고    scopus 로고
    • Directed evolution of hybrid enzymes: evolving enantioselectivity of an achiral Rh-complex anchored to a protein
    • Reetz M.T., Peyralans J.J., Maichele A., Fu Y., Maywald M. Directed evolution of hybrid enzymes: evolving enantioselectivity of an achiral Rh-complex anchored to a protein. Chem Commun (Camb) 2006, 4318-4320.
    • (2006) Chem Commun (Camb) , pp. 4318-4320
    • Reetz, M.T.1    Peyralans, J.J.2    Maichele, A.3    Fu, Y.4    Maywald, M.5
  • 57
    • 77954811495 scopus 로고    scopus 로고
    • Computational design of an enzyme catalyst for a stereoselective bimolecular Diels-Alder reaction
    • Computational design is once again shown to be a fully viable approach for creating novel catalysis in a protein scaffold. The Diels-Alder reaction has not been conclusively demonstrated in natural enzymes, and those that appear to do so are often catalysing the reaction by a different mechanism. The authors computationally designed and optimized by directed evolution, an enzyme that catalyses a r
    • Siegel J.B., Zanghellini A., Lovick H.M., Kiss G., Lambert A.R., St Clair J.L., Gallaher J.L., Hilvert D., Gelb M.H., Stoddard B.L., et al. Computational design of an enzyme catalyst for a stereoselective bimolecular Diels-Alder reaction. Science 2010, 329:309-313. Computational design is once again shown to be a fully viable approach for creating novel catalysis in a protein scaffold. The Diels-Alder reaction has not been conclusively demonstrated in natural enzymes, and those that appear to do so are often catalysing the reaction by a different mechanism. The authors computationally designed and optimized by directed evolution, an enzyme that catalyses a reaction by a true Diels-Alder mechanism, thus achieving an unprecedented enzyme catalysed route.
    • (2010) Science , vol.329 , pp. 309-313
    • Siegel, J.B.1    Zanghellini, A.2    Lovick, H.M.3    Kiss, G.4    Lambert, A.R.5    St Clair, J.L.6    Gallaher, J.L.7    Hilvert, D.8    Gelb, M.H.9    Stoddard, B.L.10
  • 58
    • 0035807809 scopus 로고    scopus 로고
    • Enzyme-like proteins by computational design
    • Bolon D.N., Mayo S.L. 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
  • 60
    • 79953310914 scopus 로고    scopus 로고
    • Optimizing non-natural protein function with directed evolution
    • Brustad E.M., Arnold F.H. Optimizing non-natural protein function with directed evolution. Curr Opin Chem Biol 2011, 15:201-210.
    • (2011) Curr Opin Chem Biol , vol.15 , pp. 201-210
    • Brustad, E.M.1    Arnold, F.H.2
  • 61
    • 77649271939 scopus 로고    scopus 로고
    • Evolutionary optimization of computationally designed enzymes: Kemp eliminases of the KE07 series
    • Khersonsky O., Rothlisberger D., Dym O., Albeck S., Jackson C.J., Baker D., Tawfik D.S. Evolutionary optimization of computationally designed enzymes: Kemp eliminases of the KE07 series. J Mol Biol 2010, 396:1025-1042.
    • (2010) J Mol Biol , vol.396 , pp. 1025-1042
    • Khersonsky, O.1    Rothlisberger, D.2    Dym, O.3    Albeck, S.4    Jackson, C.J.5    Baker, D.6    Tawfik, D.S.7
  • 62
    • 34547958191 scopus 로고    scopus 로고
    • Selection and evolution of enzymes from a partially randomized non-catalytic scaffold
    • Seelig B., Szostak J.W. Selection and evolution of enzymes from a partially randomized non-catalytic scaffold. Nature 2007, 448:828-831.
    • (2007) Nature , vol.448 , pp. 828-831
    • Seelig, B.1    Szostak, J.W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.