메뉴 건너뛰기




Volumn 14, Issue 4, 1996, Pages 458-467

Directed Evolution of a Para-Nitrobenzyl Esterase for Aqueous-Organic Solvents

Author keywords

Antibiotic synthesis; Enzymatic deprotection; Random mutagenesis

Indexed keywords

ANTIBIOTIC AGENT; ESTERASE; LORACARBEF; ORGANIC SOLVENT;

EID: 0029670577     PISSN: 10870156     EISSN: 15461696     Source Type: Journal    
DOI: 10.1038/nbt0496-458     Document Type: Article
Times cited : (378)

References (30)
  • 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 Arnold, F. 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.2
  • 2
    • 0029969577 scopus 로고
    • Directed evolution of Subtilisin E in Bacillus subtilis to enhance total activity in aqueous dimethylformamide
    • You, L. and Arnold, F. H. 1995. Directed evolution of Subtilisin E in Bacillus subtilis to enhance total activity in aqueous dimethylformamide. Protein Eng. 9:77-83.
    • (1995) Protein Eng , vol.9 , pp. 77-83
    • You, L.1    Arnold, F.H.2
  • 3
    • 0017289905 scopus 로고
    • De-esterification of cephalosporin para-nitrobenzyl esters by microbial enzymes
    • Brannon, D. R., Mabe, J. A., and Fukuda, D. S. 1976. De-esterification of cephalosporin para-nitrobenzyl esters by microbial enzymes. J. Antibiotics 29:121-124.
    • (1976) J. Antibiotics , vol.29 , pp. 121-124
    • Brannon, D.R.1    Mabe, J.A.2    Fukuda, D.S.3
  • 4
    • 84984770399 scopus 로고
    • U. S. Patent 3, 725, 359
    • U. S. Patent 3, 725, 359 [1975].
    • (1975)
  • 5
    • 0028567726 scopus 로고
    • The Bacillus subtilis pnbA gene encoding p-nitrobenzyl esterase—cloning, sequence and high-level expression in Escherichia coli
    • Zock, J., Cantwell, C, Swartling, J., Hodges, R., Pohl, T., Sutton, K., Rosteck, P. Jr., McGilvray, D., and Queener, S. 1994. The Bacillus subtilis pnbA gene encoding p-nitrobenzyl esterase—cloning, sequence and high-level expression in Escherichia coli. Gene 151:37-43.
    • (1994) Gene , vol.151 , pp. 37-43
    • Zock, J.1    Cantwell, C.2    Swartling, J.3    Hodges, R.4    Pohl, T.5    Sutton, K.6    Rosteck, P.7    McGilvray, D.8    Queener, S.9
  • 6
    • 0026668441 scopus 로고
    • The carbacephems: A new beta-lactam antibiotic class
    • Cooper, R. D. G. 1992. The carbacephems: a new beta-lactam antibiotic class. Am. J. Med. 92 Supplement 6A:S2-S6.
    • (1992) Am. J. Med , vol.92 , pp. S2-S6
    • Cooper, R.D.G.1
  • 7
    • 0030483509 scopus 로고    scopus 로고
    • Directed evolution: Creating biocatalysts for the future
    • In press
    • Arnold, F. H. 1996. Directed evolution: creating biocatalysts for the future. Chem. Eng. Science. In press.
    • (1996) Chem. Eng. Science
    • Arnold, F.H.1
  • 8
    • 0028110130 scopus 로고
    • DNA shuffling by random fragmentation and reassembly: In vitro recombination for molecular evolution
    • Stemmer, W. P. C. 1994. DNA shuffling by random fragmentation and reassembly: in vitro recombination for molecular evolution. Proc. Natl. Acad. Sci. USA 91:10747-10751.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 10747-10751
    • Stemmer, W.P.C.1
  • 9
    • 0028050350 scopus 로고
    • Rapid evolution of a protein in vitro by DNA shuffling
    • Stemmer, W. P. C. 1994. Rapid evolution of a protein in vitro by DNA shuffling. Nature 370:389-391.
    • (1994) Nature , vol.370 , pp. 389-391
    • Stemmer, W.P.C.1
  • 10
    • 0029670330 scopus 로고    scopus 로고
    • Improved green fluorescent protein by molecular evolution using DNA shuffling
    • Crameri, A., Whitehorn, E., Tate, E., and Stemmer, W. P. C. Improved green fluorescent protein by molecular evolution using DNA shuffling. Nature Biotechnology 14:315-319.
    • Nature Biotechnology , vol.14 , pp. 315-319
    • Crameri, A.1    Whitehorn, E.2    Tate, E.3    Stemmer, W.P.C.4
  • 11
    • 0002694056 scopus 로고
    • A method for random mutagenesis of a defined DNA segment using a modified polymerase chain reaction
    • Leung, D. W., Chen, E., and Goeddel, D. V. 1989. A method for random mutagenesis of a defined DNA segment using a modified polymerase chain reaction. Technique 1:11-15.
    • (1989) Technique , vol.1 , pp. 11-15
    • Leung, D.W.1    Chen, E.2    Goeddel, D.V.3
  • 12
    • 0026207466 scopus 로고
    • DNA polymerase fidelity and the polymerase chain reaction
    • Eckert, K. A. and Kunkel, T. A. 1991. DNA polymerase fidelity and the polymerase chain reaction. PCR Methods Applic. 1:17-24.
    • (1991) PCR Methods Applic , vol.1 , pp. 17-24
    • Eckert, K.A.1    Kunkel, T.A.2
  • 13
    • 85045502002 scopus 로고
    • Randomization of genes by PCR mutagenesis
    • Cadwell, R. C. and Joyce, G. F. 1992. Randomization of genes by PCR mutagenesis. PCR Methods Applic. 2:28-33.
    • (1992) PCR Methods Applic , vol.2 , pp. 28-33
    • Cadwell, R.C.1    Joyce, G.F.2
  • 14
    • 0026334373 scopus 로고
    • Enzyme engineering for nonaqueous solvents: Random mutagenesis to enhance activity of subtilisin E in polar organic media
    • Chen, K. and Arnold, F. 1991. Enzyme engineering for nonaqueous solvents: random mutagenesis to enhance activity of subtilisin E in polar organic media. Bio/Technology 9:1073-1077.
    • (1991) Bio/Technology , vol.9 , pp. 1073-1077
    • Chen, K.1    Arnold, F.2
  • 16
    • 0026744156 scopus 로고
    • Purification and properties of an arthrobacter-oxydans p52 carbamate hydrolase specific for the herbicide phenmedipham and nucleotide-sequence of the corresponding gene
    • Pohlenz, H. D., Boldol, W., Schuttke, I., and Streber, W. R. 1992. Purification and properties of an arthrobacter-oxydans p52 carbamate hydrolase specific for the herbicide phenmedipham and nucleotide-sequence of the corresponding gene. J. Bacteriol. 174:6600-6607.
    • (1992) J. Bacteriol , vol.174 , pp. 6600-6607
    • Pohlenz, H.D.1    Boldol, W.2    Schuttke, I.3    Streber, W.R.4
  • 17
    • 0025778840 scopus 로고
    • Atomic structure of acetylcholinesterase from Torpedo californica: A prototypic acetylcholine-binding protein
    • Sussman, J. L, Harel, M., Frolow, F., Oefner, C, Goldman, A., Toker, L, and Siliman, I. 1991. Atomic structure of acetylcholinesterase from Torpedo californica: a prototypic acetylcholine-binding protein. Science 253:872-879.
    • (1991) Science , vol.253 , pp. 872-879
    • Sussman, J.L.1    Harel, M.2    Frolow, F.3    Oefner, C.4    Goldman, A.5    Toker, L.6    Siliman, I.7
  • 18
    • 0027336654 scopus 로고
    • 1.8 angstroms refined structure of the lipase from Geotrichum candidum
    • Schrag, J. D. and Cygler, M. 1993. 1.8 angstroms refined structure of the lipase from Geotrichum candidum. J. Mol. Biol. 230:575-591.
    • (1993) J. Mol. Biol , vol.230 , pp. 575-591
    • Schrag, J.D.1    Cygler, M.2
  • 19
    • 0027136282 scopus 로고
    • Comparative modelling by satisfaction of spatial restraints
    • Sali, A. and Blundell, T. L. 1993. Comparative modelling by satisfaction of spatial restraints. J. Mol. Biol. 234:779-815.
    • (1993) J. Mol. Biol , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 20
    • 0028051828 scopus 로고
    • Derivation of rules for comparative modeling from a database of protein structure alignments
    • Sali, A. and Overington, J. P. 1994. Derivation of rules for comparative modeling from a database of protein structure alignments. Prot. Sci. 3:1582-1596.
    • (1994) Prot. Sci , vol.3 , pp. 1582-1596
    • Sali, A.1    Overington, J.P.2
  • 21
    • 84984778883 scopus 로고    scopus 로고
    • U.S. Patent Application No. 07, 739, 2801
    • U.S. Patent Application No. 07, 739, 2801.
  • 23
    • 0029099249 scopus 로고
    • Purification and properties of p-nitrobenzyl esterase from Bacillus subtilis
    • Chen, Y., Usui, S., Queener, S. W., and Yu, C. 1995. Purification and properties of p-nitrobenzyl esterase from Bacillus subtilis. J. Ind. Micro. 15:10-18.
    • (1995) J. Ind. Micro , vol.15 , pp. 10-18
    • Chen, Y.1    Usui, S.2    Queener, S.W.3    Yu, C.4
  • 24
    • 0028024897 scopus 로고
    • Acetylcholinesterase and butyrylcholinesterase expression in adult-rabbit tissues and during development
    • Jbilo, O., L’Hermite, Y, Talesa, V, Toutant, J. P., and Chatonnet, A. 1994. Acetylcholinesterase and butyrylcholinesterase expression in adult-rabbit tissues and during development. Eur. J. Biochem. 225:115-124.
    • (1994) Eur. J. Biochem , vol.225 , pp. 115-124
    • Jbilo, O.1    L’Hermite, Y.2    Talesa, V.3    Toutant, J.P.4    Chatonnet, A.5
  • 25
    • 0025297850 scopus 로고
    • Complete sequence of rabbit butyrylcholinesterase
    • Jbilo, O. and Chatonnet, A. 1990. Complete sequence of rabbit butyrylcholinesterase. Nucleic Acids Res. 18:3990.
    • (1990) Nucleic Acids Res , vol.18 , pp. 3990
    • Jbilo, O.1    Chatonnet, A.2
  • 26
    • 0024380746 scopus 로고
    • Isolation, properties, and the complete amino-acid sequence of a 2nd form of 60-kda glycoprotein esterase—orientation of the 60-kda proteins in the microsomal membrane
    • Ozols, J. 1989. Isolation, properties, and the complete amino-acid sequence of a 2nd form of 60-kda glycoprotein esterase—orientation of the 60-kda proteins in the microsomal membrane. J. Biol. Chem. 264:12533-12545.
    • (1989) J. Biol. Chem , vol.264 , pp. 12533-12545
    • Ozols, J.1
  • 27
    • 0025305481 scopus 로고
    • Membrane-enclosed crystals in Dictyostelium discoideum cells, consisting of developmentally regulated proteins with sequence similarities to known esterases
    • Bomblies, L., Blegelmann, E., Doering, V., Gerisch, G., Krafft-Czepa, H., Noegel, A. A., Schleicher, M., and Humbel B. M. 1990. Membrane-enclosed crystals in Dictyostelium discoideum cells, consisting of developmentally regulated proteins with sequence similarities to known esterases. J. Cell Biol. 110:669-679.
    • (1990) J. Cell Biol , vol.110 , pp. 669-679
    • Bomblies, L.1    Blegelmann, E.2    Doering, V.3    Gerisch, G.4    Krafft-Czepa, H.5    Noegel, A.A.6    Schleicher, M.7    Humbel, B.M.8
  • 28
    • 0027238559 scopus 로고
    • Molecular cloning and sequencing of thioesterase B cDNA and stimulation of expression of the thioesterase B gene associated with hormonal induction of peroxisomal proliferation
    • Hwang, C-S. and Kolattukudy, P. E. 1993. Molecular cloning and sequencing of thioesterase B cDNA and stimulation of expression of the thioesterase B gene associated with hormonal induction of peroxisomal proliferation. J. Biol. Chem. 268:14278-14284.
    • (1993) J. Biol. Chem , vol.268 , pp. 14278-14284
    • Hwang, C.-S.1    Kolattukudy, P.E.2
  • 30
    • 0027979972 scopus 로고
    • Monomeric and dimeric forms of cholesterol esterase from Candida cylindracea. Primary structure, identity in peptide patterns, and additional microheterogeneity
    • Kaiser, R., Erman, M., Duax, W. L., Ghosh, D., and Joernvall, H. 1994. Monomeric and dimeric forms of cholesterol esterase from Candida cylindracea. Primary structure, identity in peptide patterns, and additional microheterogeneity. FEBS Lett. 337:123-127.
    • (1994) FEBS Lett , vol.337 , pp. 123-127
    • Kaiser, R.1    Erman, M.2    Duax, W.L.3    Ghosh, D.4    Joernvall, H.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.