메뉴 건너뛰기




Volumn 25, Issue 3, 2007, Pages 338-344

Improving catalytic function by ProSAR-driven enzyme evolution

Author keywords

[No Author keywords available]

Indexed keywords

CATALYST ACTIVITY; CHOLESTEROL; DRUG PRODUCTS; MUTAGENESIS;

EID: 33947095042     PISSN: 10870156     EISSN: 15461696     Source Type: Journal    
DOI: 10.1038/nbt1286     Document Type: Article
Times cited : (474)

References (34)
  • 1
    • 0035843170 scopus 로고    scopus 로고
    • Industrial biocatalysis today and tomorrow
    • Schmid, A. et al. Industrial biocatalysis today and tomorrow. Nature 409, 258-268 (2001).
    • (2001) Nature , vol.409 , pp. 258-268
    • Schmid, A.1
  • 2
    • 0037436563 scopus 로고    scopus 로고
    • Dispelling the myths - biocatalysis in industrial synthesis
    • Schoemaker, H.E., Mink, D. & Wubbolts, M.G. Dispelling the myths - biocatalysis in industrial synthesis. Science 299, 1694-1697 (2003).
    • (2003) Science , vol.299 , pp. 1694-1697
    • Schoemaker, H.E.1    Mink, D.2    Wubbolts, M.G.3
  • 3
    • 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. Microb. Cell Fact. 4, 29 (2005).
    • (2005) Microb. Cell Fact , vol.4 , pp. 29
    • Hibbert, E.G.1    Dalby, P.A.2
  • 4
    • 31544483652 scopus 로고    scopus 로고
    • Tawfik, D.S. Biochemistry. Loop grafting and the origins of enzyme species. Science 311, 475-476 (2006).
    • Tawfik, D.S. Biochemistry. Loop grafting and the origins of enzyme species. Science 311, 475-476 (2006).
  • 5
    • 2442668927 scopus 로고    scopus 로고
    • Discovery and directed evolution of a glyphosate tolerance gene
    • Castle, L.A. et al. Discovery and directed evolution of a glyphosate tolerance gene. Science 304, 1151-1154 (2004).
    • (2004) Science , vol.304 , pp. 1151-1154
    • Castle, L.A.1
  • 6
    • 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. & Stemmer, W.P. DNA shuffling of a family of genes from diverse species accelerates directed evolution. Nature 391, 288-291 (1998).
    • (1998) Nature , vol.391 , pp. 288-291
    • Crameri, A.1    Raillard, S.A.2    Bermudez, E.3    Stemmer, W.P.4
  • 7
    • 0036901312 scopus 로고    scopus 로고
    • Synthetic shuffling expands functional protein diversity by allowing amino acids to recombine independently
    • Ness, J.E. et al. Synthetic shuffling expands functional protein diversity by allowing amino acids to recombine independently. Nat. Biotechnol. 20, 1251-1255 (2002).
    • (2002) Nat. Biotechnol , vol.20 , pp. 1251-1255
    • Ness, J.E.1
  • 8
    • 0032885231 scopus 로고    scopus 로고
    • DNA shuffling of subgenomic sequences of subtilisin
    • Ness, J.E. et al. DNA shuffling of subgenomic sequences of subtilisin. Nat. Biotechnol. 17, 893-896 (1999).
    • (1999) Nat. Biotechnol , vol.17 , pp. 893-896
    • Ness, J.E.1
  • 9
    • 0028050350 scopus 로고
    • Rapid evolution of a protein in vitro by DNA shuffling
    • Stemmer, W.P.C. Rapid evolution of a protein in vitro by DNA shuffling. Nature 370, 389-391 (1994).
    • (1994) Nature , vol.370 , pp. 389-391
    • Stemmer, W.P.C.1
  • 11
    • 0030771347 scopus 로고    scopus 로고
    • QSAR and 3D QSAR in drug design Part1: Methodology
    • Kubinyi, H. QSAR and 3D QSAR in drug design Part1: methodology. Drug Disc. Today 2, 457-467 (1997).
    • (1997) Drug Disc. Today , vol.2 , pp. 457-467
    • Kubinyi, H.1
  • 12
    • 0022636036 scopus 로고
    • The prediction of bradykinin potentiating potency of pentapeptides. An example of a peptide quantitative structure-activity relationship
    • Hellberg, S., Sjostrom, M. & Wold, S. The prediction of bradykinin potentiating potency of pentapeptides. An example of a peptide quantitative structure-activity relationship. Acta Chem. Scand. B 40, 135-140 (1986).
    • (1986) Acta Chem. Scand. B , vol.40 , pp. 135-140
    • Hellberg, S.1    Sjostrom, M.2    Wold, S.3
  • 13
    • 0028923454 scopus 로고
    • PROANAL version 2: Multifunctional program for analysis of multiple protein sequence alignments and studying structure-activity relationships in protein families
    • Eroshkin, A.M., Fomin, V.I., Zhilkin, P.A., Ivanisenko, V.A. & Kondrakhin, Y.V. PROANAL version 2: multifunctional program for analysis of multiple protein sequence alignments and studying structure-activity relationships in protein families. Comp. Appl. Biosci. 11, 39-44 (1995).
    • (1995) Comp. Appl. Biosci , vol.11 , pp. 39-44
    • Eroshkin, A.M.1    Fomin, V.I.2    Zhilkin, P.A.3    Ivanisenko, V.A.4    Kondrakhin, Y.V.5
  • 14
    • 0027373440 scopus 로고
    • Algorithm and computer program Pro__Anal for analysis of relationship between structure and activity in a family of proteins or peptides
    • Eroshkin, A.M., Zhilkin, P.A. & Fomin, V.I. Algorithm and computer program Pro__Anal for analysis of relationship between structure and activity in a family of proteins or peptides. Comput. Appl. Biosci. 9, 491-497 (1993).
    • (1993) Comput. Appl. Biosci , vol.9 , pp. 491-497
    • Eroshkin, A.M.1    Zhilkin, P.A.2    Fomin, V.I.3
  • 15
    • 14844335718 scopus 로고    scopus 로고
    • Directed molecular evolution by machine learning and the influence of nonlinear interactions
    • Fox, R. Directed molecular evolution by machine learning and the influence of nonlinear interactions. J. Theor. Biol. 234, 187-199 (2005).
    • (2005) J. Theor. Biol , vol.234 , pp. 187-199
    • Fox, R.1
  • 16
    • 0141705742 scopus 로고    scopus 로고
    • Optimizing the search algorithm for protein engineering by directed evolution
    • Fox, R. et al. Optimizing the search algorithm for protein engineering by directed evolution. Protein Eng. 16, 589-597 (2003).
    • (2003) Protein Eng , vol.16 , pp. 589-597
    • Fox, R.1
  • 17
    • 0025998074 scopus 로고
    • A new catalytic function of halohydrin hydrogen-halide-lyase, synthesis of beta-hydroxynitriles from epoxides and cyanide
    • Nakamura, T., Nagasawa, T., Yu, F., Watanabe, I. & Yamada, H. A new catalytic function of halohydrin hydrogen-halide-lyase, synthesis of beta-hydroxynitriles from epoxides and cyanide. Biochem. Biophys. Res. Commun. 180, 124-130 (1991).
    • (1991) Biochem. Biophys. Res. Commun , vol.180 , pp. 124-130
    • Nakamura, T.1    Nagasawa, T.2    Yu, F.3    Watanabe, I.4    Yamada, H.5
  • 18
    • 0026004141 scopus 로고
    • Purification and characterization of haloalcohol dehalogenase from Arthrobacter sp. strain AD2
    • van den Wijngaard, A.J., Reuvekamp, P.T. & Janssen, D.B. Purification and characterization of haloalcohol dehalogenase from Arthrobacter sp. strain AD2. J. Bacteriol. 173, 124-129 (1991).
    • (1991) J. Bacteriol , vol.173 , pp. 124-129
    • van den Wijngaard, A.J.1    Reuvekamp, P.T.2    Janssen, D.B.3
  • 19
    • 33947142990 scopus 로고    scopus 로고
    • Matsuda, H, Shibata, T, Hashimoto, H. & Kitai, M. Method for producing (R)-4-cyano-3-hydroxybutyric acid lower alkyl ester. US patent 5,908,953 1999
    • Matsuda, H., Shibata, T., Hashimoto, H. & Kitai, M. Method for producing (R)-4-cyano-3-hydroxybutyric acid lower alkyl ester. US patent 5,908,953 (1999).
  • 20
    • 0028110130 scopus 로고
    • in vitro shuffling by random fragmentation and reassembly in vitro recombination for molecular evolution
    • Stemmer, W.P. DNA in vitro shuffling by random fragmentation and reassembly in vitro recombination for molecular evolution. Proc. Natl. Acad. Sci. USA 91, 10747-10751 (1994).
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 10747-10751
    • Stemmer, W.P.D.1
  • 21
    • 0025082684 scopus 로고
    • Additivity of mutational effects in proteins
    • Wells, J.A. Additivity of mutational effects in proteins. Biochemistry 29, 8509-8517 (1990).
    • (1990) Biochemistry , vol.29 , pp. 8509-8517
    • Wells, J.A.1
  • 22
    • 0027248706 scopus 로고
    • Engineering multiple properties of a protein by combinatorial mutagenesis
    • Sandberg, W.S. & Terwilliger, T.C. Engineering multiple properties of a protein by combinatorial mutagenesis. Proc. Natl. Acad. Sci. USA 90, 8367-8371 (1993).
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 8367-8371
    • Sandberg, W.S.1    Terwilliger, T.C.2
  • 23
    • 0027530250 scopus 로고
    • SIMPLS: An alternative approach to partial least squares regression
    • de Jong, S. SIMPLS: an alternative approach to partial least squares regression. Chemomet. and Intell. Lab. Sys. 18, 251-263 (1993).
    • (1993) Chemomet. and Intell. Lab. Sys , vol.18 , pp. 251-263
    • de Jong, S.1
  • 24
    • 0030914367 scopus 로고    scopus 로고
    • Design of active analogues of a 15-residue peptide using D-optimal design, QSAR and a combinatorial search algorithm
    • Mee, R.P., Auton, T.R. & Morgan, P.J. Design of active analogues of a 15-residue peptide using D-optimal design, QSAR and a combinatorial search algorithm. J. Pept. Res. 49, 89-102 (1997).
    • (1997) J. Pept. Res , vol.49 , pp. 89-102
    • Mee, R.P.1    Auton, T.R.2    Morgan, P.J.3
  • 26
    • 0141865521 scopus 로고    scopus 로고
    • Structure and mechanism of a bacterial haloalcohol dehalogenase: A new variation of the short-chain dehydrogenase/reductase fold without an NAD(P)H binding site
    • de Jong, R.M. et al. Structure and mechanism of a bacterial haloalcohol dehalogenase: a new variation of the short-chain dehydrogenase/reductase fold without an NAD(P)H binding site. EMBO J. 22, 4933-4944 (2003).
    • (2003) EMBO J , vol.22 , pp. 4933-4944
    • de Jong, R.M.1
  • 27
    • 0021710490 scopus 로고
    • Nonrandomness of point mutation as reflected in nucleotide substitutions in pseudogenes and its evolutionary implications
    • Li, W.H., Wu, C.I. & Luo, C.C. Nonrandomness of point mutation as reflected in nucleotide substitutions in pseudogenes and its evolutionary implications. J. Mol. Evol. 21, 58-71 (1984).
    • (1984) J. Mol. Evol , vol.21 , pp. 58-71
    • Li, W.H.1    Wu, C.I.2    Luo, C.C.3
  • 28
    • 7344229253 scopus 로고    scopus 로고
    • Towards a theory of evolutionary adaptation
    • Hartl, D.L. & Taubes, C.H. Towards a theory of evolutionary adaptation. Genetica 102-103, 525-533 (1998).
    • (1998) Genetica , vol.102-103 , pp. 525-533
    • Hartl, D.L.1    Taubes, C.H.2
  • 29
    • 0034891764 scopus 로고    scopus 로고
    • Halohydrin dehalogenases are structurally and mechanistically related to short-chain dehydrogenases/ reductases
    • Hylckama Vlieg, J.E.T. et al. Halohydrin dehalogenases are structurally and mechanistically related to short-chain dehydrogenases/ reductases. J. Bacteriol. 183, 5058-5066 (2001).
    • (2001) J. Bacteriol , vol.183 , pp. 5058-5066
    • Hylckama Vlieg, J.E.T.1
  • 31
    • 33748085677 scopus 로고    scopus 로고
    • Competitors want to get a piece of Lipitor
    • Thayer, A. Competitors want to get a piece of Lipitor. Chem. Eng. News 84, 26-27 (2006).
    • (2006) Chem. Eng. News , vol.84 , pp. 26-27
    • Thayer, A.1
  • 32
    • 0030989062 scopus 로고    scopus 로고
    • Directed evolution of a fucosidase from a galactosidase by DNA shuffling and screening
    • Zhang, J.H., Dawes, G. & Stemmer, W.P. Directed evolution of a fucosidase from a galactosidase by DNA shuffling and screening. Proc. Natl. Acad. Sci. USA 94, 4504-4509 (1997).
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 4504-4509
    • Zhang, J.H.1    Dawes, G.2    Stemmer, W.P.3
  • 33
    • 20844451538 scopus 로고    scopus 로고
    • Semi-synthetic DNA shuffling of aveC leads to improved industrial scale production of doramectin by Streptomyces avermitilis
    • Stutzman-Engwall, K. et al. Semi-synthetic DNA shuffling of aveC leads to improved industrial scale production of doramectin by Streptomyces avermitilis. Metab. Eng. 7, 27-37 (2005).
    • (2005) Metab. Eng , vol.7 , pp. 27-37
    • Stutzman-Engwall, K.1
  • 34
    • 33744475011 scopus 로고    scopus 로고
    • Directed evolution of enantioselective enzymes: Iterative cycles of CASTing for probing protein-sequence space
    • Reetz, M.T., Wang, L.W. & Bocola, M. Directed evolution of enantioselective enzymes: Iterative cycles of CASTing for probing protein-sequence space. Angew Chem. Int. Ed. Engl. 45, 1236-1241 (2006).
    • (2006) Angew Chem. Int. Ed. Engl , vol.45 , pp. 1236-1241
    • Reetz, M.T.1    Wang, L.W.2    Bocola, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.