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Volumn 2, Issue 3, 1999, Pages 241-245

Novel approaches for discovering industrial enzymes

Author keywords

[No Author keywords available]

Indexed keywords

BIODIVERSITY; BIOTECHNOLOGY; CATALYSIS; CHEMICAL MODIFICATION; ENZYME PURIFICATION; PHAGE DISPLAY; REVIEW; STEREOSPECIFICITY;

EID: 0033153175     PISSN: 13695274     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1369-5274(99)80042-3     Document Type: Article
Times cited : (69)

References (40)
  • 2
    • 0032424429 scopus 로고    scopus 로고
    • Bringing biological solutions to chemical problems
    • Schultz PG: Bringing biological solutions to chemical problems. Proc Natl Acad Sci USA 1998, 95:14590-14591.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 14590-14591
    • Schultz, P.G.1
  • 4
    • 0002284639 scopus 로고    scopus 로고
    • Specialty enzymes from marine organisms
    • Haard NF: Specialty enzymes from marine organisms. Food Technol 1998, 52:64-67.
    • (1998) Food Technol , vol.52 , pp. 64-67
    • Haard, N.F.1
  • 6
    • 0031300142 scopus 로고    scopus 로고
    • Recombinant approaches for accessing biodiversity
    • Short JM: Recombinant approaches for accessing biodiversity. Nat Biotechnol 1997, 15:1322-1323.
    • (1997) Nat Biotechnol , vol.15 , pp. 1322-1323
    • Short, J.M.1
  • 7
    • 0030865449 scopus 로고    scopus 로고
    • Characterization of a DNA polymerase from the uncultivated psychrophilic archeon Crenarchaeum symbiosum
    • Schleper C, Swanson RV, Mathur EJ, DeLong EF: Characterization of a DNA polymerase from the uncultivated psychrophilic archeon Crenarchaeum symbiosum. J Bacteriol 1997, 179:7803-7811.
    • (1997) J Bacteriol , vol.179 , pp. 7803-7811
    • Schleper, C.1    Swanson, R.V.2    Mathur, E.J.3    DeLong, E.F.4
  • 8
    • 0030803307 scopus 로고    scopus 로고
    • Cloning, sequencing and expression of the gene encoding extracellular alpha-amylase from Pyrococcus furiosus biochemical characterization of the recombinant enzyme
    • Dong G, Vieille C, Savchenko A, Zeikus JG: Cloning, sequencing and expression of the gene encoding extracellular alpha-amylase from Pyrococcus furiosus biochemical characterization of the recombinant enzyme. Appl Environ Microbiol 1997, 63:3577-3584. A very nice example of the isolation and characterization of a novel industrial enzyme via heterologous expression of an extremophile gene in an easy to handle host.
    • (1997) Appl Environ Microbiol , vol.63 , pp. 3577-3584
    • Dong, G.1    Vieille, C.2    Savchenko, A.3    Zeikus, J.G.4
  • 9
    • 0030803307 scopus 로고    scopus 로고
    • Cloning, sequencing and expression of the gene encoding Pyrococcus furiosus amylopullulanase and enzyme biochemical characterization
    • Dong G, Vieille C, Zeikus G: Cloning, sequencing and expression of the gene encoding Pyrococcus furiosus amylopullulanase and enzyme biochemical characterization. Appl Environ Microbiol 1997, 63:3577-3584.
    • (1997) Appl Environ Microbiol , vol.63 , pp. 3577-3584
    • Dong, G.1    Vieille, C.2    Zeikus, G.3
  • 10
    • 0032142867 scopus 로고    scopus 로고
    • Thermozymes: Biotechnology and structure-function relationships
    • Zeikus G, Vieille C, Savchenko A: Thermozymes: Biotechnology and structure-function relationships. Extremophiles 1998, 2:179-183. A review worth reading for its focus on industrial enzymes.
    • (1998) Extremophiles , vol.2 , pp. 179-183
    • Zeikus, G.1    Vieille, C.2    Savchenko, A.3
  • 11
    • 0032404525 scopus 로고    scopus 로고
    • Finding and using hyperthermophilic enzymes
    • Adams MWW, Kelly RM: Finding and using hyperthermophilic enzymes. Tibtech 1998, 16:329-332.
    • (1998) Tibtech , vol.16 , pp. 329-332
    • Adams, M.W.W.1    Kelly, R.M.2
  • 12
    • 0031865608 scopus 로고    scopus 로고
    • Novel evolutionary histories and adaptive features of proteins from hyperthermophiles
    • Robb FT, Maeder DL: Novel evolutionary histories and adaptive features of proteins from hyperthermophiles. Curr Opin Biotechnol 1998, 9:288-291.
    • (1998) Curr Opin Biotechnol , vol.9 , pp. 288-291
    • Robb, F.T.1    Maeder, D.L.2
  • 13
    • 0031811930 scopus 로고    scopus 로고
    • Deep ocean environmental biotechnology
    • Deming JW: Deep ocean environmental biotechnology. Curr Opin Biotechnol 1998, 9:283-287.
    • (1998) Curr Opin Biotechnol , vol.9 , pp. 283-287
    • Deming, J.W.1
  • 14
    • 0030749081 scopus 로고    scopus 로고
    • Cold-adapted enzymes
    • Marshall CJ: Cold-adapted enzymes. Tends Biotechnol 1997, 15:359-364.
    • (1997) Tends Biotechnol , vol.15 , pp. 359-364
    • Marshall, C.J.1
  • 15
    • 0013567048 scopus 로고    scopus 로고
    • Screening of novel enzymes for the production of useful compounds
    • Yamada H: Screening of novel enzymes for the production of useful compounds. Stud Organ Chem 1998, 53:13-17.
    • (1998) Stud Organ Chem , vol.53 , pp. 13-17
    • Yamada, H.1
  • 16
    • 0030624098 scopus 로고    scopus 로고
    • Screening of novel microbial enzymes for the production of biologically and chemically useful compounds
    • Shimizu S, Ogawa J, Kataoka M, Kobayashi M: Screening of novel microbial enzymes for the production of biologically and chemically useful compounds. Adv Biochem Engin/Biotechnol 1997, 58:45-88. An extensive review, focusing on the more recent enzyme discoveries to come out of this renowned laboratory. It defines the classic approach to discovery of novel industrial enzymes.
    • (1997) Adv Biochem Engin/Biotechnol , vol.58 , pp. 45-88
    • Shimizu, S.1    Ogawa, J.2    Kataoka, M.3    Kobayashi, M.4
  • 23
    • 0032568526 scopus 로고    scopus 로고
    • Highly specific protein sequence motifs for genome analysis
    • A good example of bioinformatics applied to the search for new enzymes distantly related to enzymes of known function
    • Nevill-Manning CG, Wu TD, Brutlag DL: Highly specific protein sequence motifs for genome analysis. Proc Natl Acad Sci USA 1998, 95:5865-5871. A good example of bioinformatics applied to the search for new enzymes distantly related to enzymes of known function.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 5865-5871
    • Nevill-Manning, C.G.1    Wu, T.D.2    Brutlag, D.L.3
  • 24
    • 0030784438 scopus 로고    scopus 로고
    • An artificial intelligence approach to motif discovery in protein sequences: Application to steriod dehydrogenases
    • Bailey TL, Baker ME, Elkan CP: An artificial intelligence approach to motif discovery in protein sequences: Application to steriod dehydrogenases. J Steroid Biochem Mol Biol 1997, 62:29-44.
    • (1997) J Steroid Biochem Mol Biol , vol.62 , pp. 29-44
    • Bailey, T.L.1    Baker, M.E.2    Elkan, C.P.3
  • 25
    • 0032952822 scopus 로고    scopus 로고
    • Using the Saccharomyces Genome Database (SGD) for analysis of protein similarities and structure
    • Chervitz SA, Hester ET, Ball CA, Dolinski K, Dwight SS, Harris MA, Juvik G, Malekian A, Roberts S, Roe T et al.: Using the Saccharomyces Genome Database (SGD) for analysis of protein similarities and structure. Nucleic Acids Res 1999, 27:74-78. One of the many databases discussed in a special issue of Nucleic Acids Research (see http://www.oup.co.uk/nar/Volume_27/Issue_01/), a description of new tools used to link protein structures to genomic information is given.
    • (1999) Nucleic Acids Res , vol.27 , pp. 74-78
    • Chervitz, S.A.1    Hester, E.T.2    Ball, C.A.3    Dolinski, K.4    Dwight, S.S.5    Harris, M.A.6    Juvik, G.7    Malekian, A.8    Roberts, S.9    Roe, T.10
  • 26
    • 0001270261 scopus 로고    scopus 로고
    • Design by directed evolution
    • Arnold FH: Design by directed evolution. Acc Chem Res 1998, 31:125-131.
    • (1998) Acc Chem Res , vol.31 , pp. 125-131
    • Arnold, F.H.1
  • 27
    • 0033023419 scopus 로고    scopus 로고
    • Directed evolution of biocatalysts
    • Arnold FH, Volkov AA: Directed evolution of biocatalysts. Curr Opin Chem Biol, 1999, 3: 54-59. A review of applications of directed enzyme evolution including altering enantio-and chemo-selectivity of lipases; aminotransferases and dioxygenases; altering stability and expression of subtilisins, dehydrogenases, esterases, and catalytic and binding antibodies; and altering activity of recombinases and lipases. Also reviewed are advances in genetic and screening/selection methods, including Tawfik's water-oil emulsion method and pH based assays.
    • (1999) Curr Opin Chem Biol , vol.3 , pp. 54-59
    • Arnold, F.H.1    Volkov, A.A.2
  • 28
    • 0032007562 scopus 로고    scopus 로고
    • Artificial evolution by DNA shuffling
    • Harayama S: Artificial evolution by DNA shuffling. Tibtech 1998, 16:76-82.
    • (1998) Tibtech , vol.16 , pp. 76-82
    • Harayama, S.1
  • 29
    • 0028110130 scopus 로고
    • DNA shuffling by random fragmentation and reassembly: In vitro recombination for molecular evolution
    • Stemmer WP: DNA shuffling by random fragmentation and reassembly: In vitro recombination for molecular evolution. Proc Natl Acad Sci USA 1994, 91:10747-10751.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 10747-10751
    • Stemmer, W.P.1
  • 30
    • 0028050350 scopus 로고
    • Rapid evolution of a protein in vitro by DNA shuffling
    • Stemmer WP: 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
  • 31
    • 0032518266 scopus 로고    scopus 로고
    • DNA shuffling of a family of genes from diverse species accelerates directed evolution
    • Crameri A, Raillard SA, Bermudez E, Stemmer WP: DNA shuffling of a family of genes from diverse species accelerates directed evolution. Nature 1998, 391:288-291. A significant advance is shuffling methodology, this technique allows access to recombination between species that is not available by traditional, whole organism, breeding methods.
    • (1998) Nature , vol.391 , pp. 288-291
    • Crameri, A.1    Raillard, S.A.2    Bermudez, E.3    Stemmer, W.P.4
  • 33
    • 0030858562 scopus 로고    scopus 로고
    • Functional and nonfunctional mutations distinguished by random recombination of homologous genes
    • Zhao H, Arnold FH: Functional and nonfunctional mutations distinguished by random recombination of homologous genes. Proc Natl Acad Sci USA 1997, 94:7997-8000.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 7997-8000
    • Zhao, H.1    Arnold, F.H.2
  • 34
    • 0031587291 scopus 로고    scopus 로고
    • Strategies for the in vitro evolution of protein function: Enzyme evolution by random recombination of improved sequences
    • Kuchner O, Arnold FH: Strategies for the in vitro evolution of protein function: Enzyme evolution by random recombination of improved sequences. J Mol Biol 1997, 272:336-347. Required reading for in vitro evolution via DNA shuffling.
    • (1997) J Mol Biol , vol.272 , pp. 336-347
    • Kuchner, O.1    Arnold, F.H.2
  • 35
    • 0032518181 scopus 로고    scopus 로고
    • Random-priming in vitro recombination: An effective tool for directed evolution. Description of RPR for DNA shuffling
    • Shao Z, Zhao H, Giver L, Arnold FH: Random-priming in vitro recombination: An effective tool for directed evolution. Description of RPR for DNA shuffling. Nucleic Acids Res 1998, 26:681-683. A description of RPR for DNA shuffling. This technique differs from Stemmer's [29,30] because the generation of oligomers occurs by synthesis (i.e. polymerization) of duplex DNA rather than fragmentation of existing duplex DNA. It differs from StEP [36••] in that the primers are random oligomers.
    • (1998) Nucleic Acids Res , vol.26 , pp. 681-683
    • Shao, Z.1    Zhao, H.2    Giver, L.3    Arnold, F.H.4
  • 36
    • 0031909113 scopus 로고    scopus 로고
    • Molecular evolution by staggered extension process (StEP) in vitro recombination
    • Zhao H, Giver L, Shao Z, Affholter JA, Arnold FH: Molecular evolution by staggered extension process (StEP) in vitro recombination. Nat Biotechnol 1998, 16:258-261. Description of StEP for DNA shuffling. This technique differs from Stemmer's [29,30] because the generation of oligomers occurs by synthesis (i.e. polymerization) of duplex DNA rather than fragmentation of existing of duplex DNA. It differs from RPR [35••] in that only one pair of primers is used.
    • (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
  • 38
    • 0032168985 scopus 로고    scopus 로고
    • A method for directed evolution and functional cloning of enzymes
    • Pedersen H, Holder S, Sutherlin DP, Schwitter U, King DS, Schultz PG: A method for directed evolution and functional cloning of enzymes. Proc Natl Acad Sci USA 1998, 95:10523-10528. The system described in this article is complex but is one of the first successful application of phage display to the selection of catalysts from a complex mixture.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 10523-10528
    • Pedersen, H.1    Holder, S.2    Sutherlin, D.P.3    Schwitter, U.4    King, D.S.5    Schultz, P.G.6
  • 39
    • 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
  • 40
    • 0030924508 scopus 로고    scopus 로고
    • Phage display of a catalytic antibody to optimize affinity for transition-state analog binding
    • Baca M, Scanlan TS, Stephenson RC, Wells JA: Phage display of a catalytic antibody to optimize affinity for transition-state analog binding. Proc Natl Acad Sci USA 1997, 94:10063-10068.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 10063-10068
    • Baca, M.1    Scanlan, T.S.2    Stephenson, R.C.3    Wells, J.A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.