메뉴 건너뛰기




Volumn 7, Issue 6, 2012, Pages

Intramolecular epistasis and the evolution of a new enzymatic function

Author keywords

[No Author keywords available]

Indexed keywords

ATRAZINE CHLOROHYDROLASE; BACTERIAL ENZYME; ENZYME VARIANT; MELAMINE DEAMINASE; UNCLASSIFIED DRUG;

EID: 84863090430     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0039822     Document Type: Article
Times cited : (45)

References (29)
  • 1
    • 65249177164 scopus 로고    scopus 로고
    • Directed enzyme evolution: Climbing fitness peaks one amino acid at a time
    • Tracewell CA, Arnold FH, (2009) Directed enzyme evolution: Climbing fitness peaks one amino acid at a time. Current Opinion in Chemical Biology 13: 3-9.
    • (2009) Current Opinion in Chemical Biology , vol.13 , pp. 3-9
    • Tracewell, C.A.1    Arnold, F.H.2
  • 2
    • 36749020130 scopus 로고    scopus 로고
    • Protein engineers turned evolutionists
    • Peisajovich SG, Tawfik DS, (2007) Protein engineers turned evolutionists. Nature Methods 4: 991-994.
    • (2007) Nature Methods , vol.4 , pp. 991-994
    • Peisajovich, S.G.1    Tawfik, D.S.2
  • 3
    • 77953623874 scopus 로고    scopus 로고
    • Enzyme promiscuity: A mechanistic and evolutionary perspective
    • Khersonsky O, Tawfik DS, (2010) Enzyme promiscuity: A mechanistic and evolutionary perspective. Annual Review of Biochemistry 79: 471-505.
    • (2010) Annual Review of Biochemistry , vol.79 , pp. 471-505
    • Khersonsky, O.1    Tawfik, D.S.2
  • 4
    • 77954743785 scopus 로고    scopus 로고
    • Mutational effects and the evolution of new protein functions
    • Soskine M, Tawfik DS, (2010) Mutational effects and the evolution of new protein functions. Nature Reviews Genetics 11: 572-582.
    • (2010) Nature Reviews Genetics , vol.11 , pp. 572-582
    • Soskine, M.1    Tawfik, D.S.2
  • 5
    • 33645666942 scopus 로고    scopus 로고
    • Darwinian evolution can follow only very few mutational paths to fitter proteins
    • Weinreich DM, Delaney NF, DePristo MA, Hartl DL, (2006) Darwinian evolution can follow only very few mutational paths to fitter proteins. Science 312: 111-114.
    • (2006) Science , vol.312 , pp. 111-114
    • Weinreich, D.M.1    Delaney, N.F.2    DePristo, M.A.3    Hartl, D.L.4
  • 6
    • 80053133668 scopus 로고    scopus 로고
    • The evolutionary landscape of antifolate resistance in Plasmodium falciparum
    • Costanzo MS, Hartl DL, (2011) The evolutionary landscape of antifolate resistance in Plasmodium falciparum. Journal of Genetics 90: 187-190.
    • (2011) Journal of Genetics , vol.90 , pp. 187-190
    • Costanzo, M.S.1    Hartl, D.L.2
  • 7
    • 70349464621 scopus 로고    scopus 로고
    • An epistatic ratchet constrains the direction of glucocorticoid receptor evolution
    • Bridgham JT, Ortlund EA, Thornton JW, (2009) An epistatic ratchet constrains the direction of glucocorticoid receptor evolution. Nature 461: 515-578.
    • (2009) Nature , vol.461 , pp. 515-578
    • Bridgham, J.T.1    Ortlund, E.A.2    Thornton, J.W.3
  • 8
    • 66449099080 scopus 로고    scopus 로고
    • Questioning our perceptions about evolution of biodegradative enzymes
    • Wackett LP, (2009) Questioning our perceptions about evolution of biodegradative enzymes. Current Opinion in Microbiology 12: 244-251.
    • (2009) Current Opinion in Microbiology , vol.12 , pp. 244-251
    • Wackett, L.P.1
  • 9
    • 68049085674 scopus 로고    scopus 로고
    • Evolution of efficient pathways for degradation of anthropogenic chemicals
    • Copley SD, (2009) Evolution of efficient pathways for degradation of anthropogenic chemicals. Nature Chemical Biology 5: 560-567.
    • (2009) Nature Chemical Biology , vol.5 , pp. 560-567
    • Copley, S.D.1
  • 10
    • 79951633115 scopus 로고    scopus 로고
    • The evolution of new enzyme function: Lessons from xenobiotic metabolizing bacteria versus insecticide-resistant insects
    • Russell RJ, Scott C, Jackson CJ, Pandey R, Pandey G, et al. (2011) The evolution of new enzyme function: Lessons from xenobiotic metabolizing bacteria versus insecticide-resistant insects. Evolutionary Applications 4: 225-248.
    • (2011) Evolutionary Applications , vol.4 , pp. 225-248
    • Russell, R.J.1    Scott, C.2    Jackson, C.J.3    Pandey, R.4    Pandey, G.5
  • 11
    • 0028922453 scopus 로고
    • Isolation and characterization of a Pseudomonas sp that mineralizes the s-triazine herbicide atrazine
    • Mandelbaum RT, Allan DL, Wackett LP, (1995) Isolation and characterization of a Pseudomonas sp that mineralizes the s-triazine herbicide atrazine. Applied and Environmental Microbiology 61: 1451-1457.
    • (1995) Applied and Environmental Microbiology , vol.61 , pp. 1451-1457
    • Mandelbaum, R.T.1    Allan, D.L.2    Wackett, L.P.3
  • 12
    • 0029784331 scopus 로고    scopus 로고
    • Atrazine chlorohydrolase from Pseudomonas sp strain ADP: Gene sequence, enzyme purification, and protein characterization
    • de Souza ML, Sadowsky MJ, Wackett LP, (1996) Atrazine chlorohydrolase from Pseudomonas sp strain ADP: Gene sequence, enzyme purification, and protein characterization. Journal of Bacteriology 178: 4894-4900.
    • (1996) Journal of Bacteriology , vol.178 , pp. 4894-4900
    • de Souza, M.L.1    Sadowsky, M.J.2    Wackett, L.P.3
  • 13
    • 0026089423 scopus 로고
    • Cloning and alanlysis of the s-triazine catabolic genes from Pseudomonas sp. strain NRRLB-12227
    • Eaton RW, Karns JS, (1991) Cloning and alanlysis of the s-triazine catabolic genes from Pseudomonas sp. strain NRRLB-12227. Journal of Bacteriology 173: 1215-1222.
    • (1991) Journal of Bacteriology , vol.173 , pp. 1215-1222
    • Eaton, R.W.1    Karns, J.S.2
  • 15
    • 0035980264 scopus 로고    scopus 로고
    • Rapid evolution of bacterial catabolic enzymes: A case study with atrazine chlorohydrolase
    • Seffernick JL, Wackett LP, (2001) Rapid evolution of bacterial catabolic enzymes: A case study with atrazine chlorohydrolase. Biochemistry 40: 12747-12753.
    • (2001) Biochemistry , vol.40 , pp. 12747-12753
    • Seffernick, J.L.1    Wackett, L.P.2
  • 16
    • 0034833072 scopus 로고    scopus 로고
    • Novel enzyme activities and functional plasticity revealed by recombining highly homologous enzymes
    • Raillard S, Krebber A, Chen YC, Ness JE, Bermudez E, et al. (2001) Novel enzyme activities and functional plasticity revealed by recombining highly homologous enzymes. Chemistry & Biology 8: 891-898.
    • (2001) Chemistry & Biology , vol.8 , pp. 891-898
    • Raillard, S.1    Krebber, A.2    Chen, Y.C.3    Ness, J.E.4    Bermudez, E.5
  • 17
    • 0035091008 scopus 로고    scopus 로고
    • Melamine deaminase and atrazine chlorohydrolase: 98 percent identical but functionally different
    • Seffernick JL, de Souza ML, Sadowsky MJ, Wackett LP, (2001) Melamine deaminase and atrazine chlorohydrolase: 98 percent identical but functionally different. Journal of Bacteriology 183: 2405-2410.
    • (2001) Journal of Bacteriology , vol.183 , pp. 2405-2410
    • Seffernick, J.L.1    de Souza, M.L.2    Sadowsky, M.J.3    Wackett, L.P.4
  • 18
    • 4744339316 scopus 로고    scopus 로고
    • Evolution of enzymes for the metabolism of new chemical inputs into the environment
    • Wackett LP, (2004) Evolution of enzymes for the metabolism of new chemical inputs into the environment. Journal of Biological Chemistry 279: 41259-41262.
    • (2004) Journal of Biological Chemistry , vol.279 , pp. 41259-41262
    • Wackett, L.P.1
  • 19
    • 79956356758 scopus 로고    scopus 로고
    • Fitness Trade-Offs in the Evolution of Dihydrofolate Reductase and Drug Resistance in Plasmodium falciparum
    • Costanzo MS, Brown KM, Hartl DL, (2011) Fitness Trade-Offs in the Evolution of Dihydrofolate Reductase and Drug Resistance in Plasmodium falciparum. PLoS One 6: e19636.
    • (2011) PLoS One , vol.6
    • Costanzo, M.S.1    Brown, K.M.2    Hartl, D.L.3
  • 23
    • 79956356758 scopus 로고    scopus 로고
    • Fitness Trade-Offs in the Evolution of Dihydrofolate Reductase and Drug Resistance in Plasmodium falciparum
    • Costanzo MS, Brown KM, Hartl DL, (2011) Fitness Trade-Offs in the Evolution of Dihydrofolate Reductase and Drug Resistance in Plasmodium falciparum. Plos One 6.
    • (2011) Plos One 6
    • Costanzo, M.S.1    Brown, K.M.2    Hartl, D.L.3
  • 26
    • 34548018528 scopus 로고    scopus 로고
    • Mechanistic approaches to the study of evolution: the functional synthesis
    • Dean AM, Thornton JW, (2007) Mechanistic approaches to the study of evolution: the functional synthesis. Nature Reviews Genetics 8: 675-688.
    • (2007) Nature Reviews Genetics , vol.8 , pp. 675-688
    • Dean, A.M.1    Thornton, J.W.2
  • 27
    • 50449147866 scopus 로고
    • Transduction of linked genetic characters of the host by bacteriophage P1
    • Lennox ES, (1955) Transduction of linked genetic characters of the host by bacteriophage P1. Virology 1: 190-206.
    • (1955) Virology , vol.1 , pp. 190-206
    • Lennox, E.S.1
  • 28
    • 0024520745 scopus 로고
    • Site-directed mutagenesis by overlap extension using the polymerase chain-reaction
    • Ho SN, Hunt HD, Horton RM, Pullen JK, Pease LR, (1989) Site-directed mutagenesis by overlap extension using the polymerase chain-reaction. Gene 77: 51-59.
    • (1989) Gene , vol.77 , pp. 51-59
    • Ho, S.N.1    Hunt, H.D.2    Horton, R.M.3    Pullen, J.K.4    Pease, L.R.5
  • 29
    • 27144505097 scopus 로고    scopus 로고
    • Protein identification and analysis tools on the ExPASy server
    • In: Walker JM, editors, editor
    • Gasteiger E, Hoogland C, Gattiker A, Duvaud S, Wilkins MR, et al. (2005) Protein identification and analysis tools on the ExPASy server. In: Walker JM, editors. pp. 571-607 editor. The Proteomics Protocols Handbook. New York: Humana Press.
    • (2005) , pp. 571-607
    • Gasteiger, E.1    Hoogland, C.2    Gattiker, A.3    Duvaud, S.4    Wilkins, M.R.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.