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Volumn 579, Issue 5, 2005, Pages 1177-1182

A generic system for the Escherichia coli cell-surface display of lipolytic enzymes

Author keywords

Autotransporter; Bacterial surface display; Cutinase; EstA; Lipase; Type V a secretion

Indexed keywords

BACTERIAL ENZYME; CELL SURFACE PROTEIN; CUTINASE; ENZYME VARIANT; ESTERASE; OUTER MEMBRANE PROTEIN; PROTEIN ESTA; TRIACYLGLYCEROL LIPASE; UNCLASSIFIED DRUG;

EID: 13844257519     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2004.12.087     Document Type: Article
Times cited : (68)

References (28)
  • 1
    • 0031023666 scopus 로고    scopus 로고
    • 'Interfacial activation' of lipases, facts and artifacts
    • R. Verger 'Interfacial activation' of lipases, facts and artifacts Trends Biotechnol. 15 1997 32 38
    • (1997) Trends Biotechnol. , vol.15 , pp. 32-38
    • Verger, R.1
  • 2
    • 0032167489 scopus 로고    scopus 로고
    • Microbial lipases form versatile tools for biotechnology
    • K.E. Jaeger, and M.T. Reetz Microbial lipases form versatile tools for biotechnology Trends Biotechnol. 16 1998 396 403
    • (1998) Trends Biotechnol. , vol.16 , pp. 396-403
    • Jaeger, K.E.1    Reetz, M.T.2
  • 5
    • 0036234420 scopus 로고    scopus 로고
    • Microbial carboxyl esterases: Classification, properties and application in biocatalysis
    • U.T. Bornscheuer Microbial carboxyl esterases: classification, properties and application in biocatalysis FEMS Microbiol. Rev. 26 2002 73 81
    • (2002) FEMS Microbiol. Rev. , vol.26 , pp. 73-81
    • Bornscheuer, U.T.1
  • 6
    • 3543076929 scopus 로고    scopus 로고
    • Enantioselective biocatalysis optimized by directed evolution
    • K.E. Jaeger, and T. Eggert Enantioselective biocatalysis optimized by directed evolution Curr. Opin. Biotechnol. 15 2004 305 313
    • (2004) Curr. Opin. Biotechnol. , vol.15 , pp. 305-313
    • Jaeger, K.E.1    Eggert, T.2
  • 9
    • 0029808395 scopus 로고    scopus 로고
    • In vivo immobilization of enzymatically active polypeptides on the cell surface of Staphylococcus carnosus
    • A. Strauss, and F. Götz In vivo immobilization of enzymatically active polypeptides on the cell surface of Staphylococcus carnosus Mol. Microbiol. 21 1996 491 500
    • (1996) Mol. Microbiol. , vol.21 , pp. 491-500
    • Strauss, A.1    Götz, F.2
  • 10
    • 4644247440 scopus 로고    scopus 로고
    • Display of bacterial lipase on the Escherichia coli cell surface by using FadL as an anchoring motif and use of the enzyme in enantioselective biocatalysis
    • S.H. Lee, J.I. Choi, S.J. Park, S.Y. Lee, and B.C. Park Display of bacterial lipase on the Escherichia coli cell surface by using FadL as an anchoring motif and use of the enzyme in enantioselective biocatalysis Appl. Environ. Microbiol. 70 2004 5074 5080
    • (2004) Appl. Environ. Microbiol. , vol.70 , pp. 5074-5080
    • Lee, S.H.1    Choi, J.I.2    Park, S.J.3    Lee, S.Y.4    Park, B.C.5
  • 11
    • 0036727246 scopus 로고    scopus 로고
    • Construction of yeast strains with high cell surface lipase activity by using novel display systems based on the Flo1p flocculation functional domain
    • T. Matsumoto, H. Fukuda, M. Ueda, A. Tanaka, and A. Kondo Construction of yeast strains with high cell surface lipase activity by using novel display systems based on the Flo1p flocculation functional domain Appl. Environ. Microbiol. 68 2002 4517 4522
    • (2002) Appl. Environ. Microbiol. , vol.68 , pp. 4517-4522
    • Matsumoto, T.1    Fukuda, H.2    Ueda, M.3    Tanaka, A.4    Kondo, A.5
  • 12
    • 0032721432 scopus 로고    scopus 로고
    • A novel lipolytic enzyme located in the outer membrane of Pseudomonas aeruginosa
    • S. Wilhelm, J. Tommassen, and K.E. Jaeger A novel lipolytic enzyme located in the outer membrane of Pseudomonas aeruginosa J. Bacteriol. 181 1999 6977 6986
    • (1999) J. Bacteriol. , vol.181 , pp. 6977-6986
    • Wilhelm, S.1    Tommassen, J.2    Jaeger, K.E.3
  • 13
    • 0029007122 scopus 로고
    • A new family of lipolytic enzymes
    • C. Upton, and J.T. Buckley A new family of lipolytic enzymes Trends Biochem. Sci. 20 1995 178 179
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 178-179
    • Upton, C.1    Buckley, J.T.2
  • 14
    • 0027382306 scopus 로고
    • Growth-phase-dependent expression of the lipolytic system of Acinetobacter calcoaceticus BD413: Cloning of a gene encoding one of the esterases
    • R.G. Kok, V.M. Christoffels, B. Vosman, and K.J. Hellingwerf Growth-phase-dependent expression of the lipolytic system of Acinetobacter calcoaceticus BD413: cloning of a gene encoding one of the esterases J. Gen. Microbiol. 139 Pt 10 1993 2329 2342
    • (1993) J. Gen. Microbiol. , vol.139 , Issue.10 PART , pp. 2329-2342
    • Kok, R.G.1    Christoffels, V.M.2    Vosman, B.3    Hellingwerf, K.J.4
  • 15
    • 0024344169 scopus 로고
    • Efficient oligonucleotide-directed construction of mutations in expression vectors by the gapped duplex DNA method using alternating selectable markers
    • P. Stanssens, C. Opsomer, Y.M. McKeown, W. Kramer, M. Zabeau, and H.J. Fritz Efficient oligonucleotide-directed construction of mutations in expression vectors by the gapped duplex DNA method using alternating selectable markers Nucleic Acids Res. 17 1989 4441 4454
    • (1989) Nucleic Acids Res. , vol.17 , pp. 4441-4454
    • Stanssens, P.1    Opsomer, C.2    McKeown, Y.M.3    Kramer, W.4    Zabeau, M.5    Fritz, H.J.6
  • 16
    • 11844260767 scopus 로고    scopus 로고
    • Intimin-mediated export of passenger proteins requires maintenance of a translocation-competent conformation
    • T.M. Adams, A. Wentzel, and H. Kolmar Intimin-mediated export of passenger proteins requires maintenance of a translocation-competent conformation J. Bacteriol. 187 2005 522 533
    • (2005) J. Bacteriol. , vol.187 , pp. 522-533
    • Adams, T.M.1    Wentzel, A.2    Kolmar, H.3
  • 18
    • 0022913002 scopus 로고
    • Purification of extracellular lipase from Pseudomonas aeruginosa
    • W. Stuer, K.E. Jaeger, and U.K. Winkler Purification of extracellular lipase from Pseudomonas aeruginosa J. Bacteriol. 168 1986 1070 1074
    • (1986) J. Bacteriol. , vol.168 , pp. 1070-1074
    • Stuer, W.1    Jaeger, K.E.2    Winkler, U.K.3
  • 19
    • 0035212525 scopus 로고    scopus 로고
    • Display of passenger proteins on the surface of Escherichia coli K-12 by the enterohemorrhagic E. coli intimin EaeA
    • A. Wentzel, A. Christmann, T. Adams, and H. Kolmar Display of passenger proteins on the surface of Escherichia coli K-12 by the enterohemorrhagic E. coli intimin EaeA J. Bacteriol. 183 2001 7273 7284
    • (2001) J. Bacteriol. , vol.183 , pp. 7273-7284
    • Wentzel, A.1    Christmann, A.2    Adams, T.3    Kolmar, H.4
  • 20
    • 0026638399 scopus 로고
    • Cloning, nucleotide sequence and expression in Escherichia coli of a lipase gene from Bacillus subtilis 168
    • V. Dartois, A. Baulard, K. Schanck, and C. Colson Cloning, nucleotide sequence and expression in Escherichia coli of a lipase gene from Bacillus subtilis 168 Biochim. Biophys. Acta 1131 1992 253 260
    • (1992) Biochim. Biophys. Acta , vol.1131 , pp. 253-260
    • Dartois, V.1    Baulard, A.2    Schanck, K.3    Colson, C.4
  • 21
    • 0029032314 scopus 로고
    • Gene cloning, sequence analysis, purification, and secretion by Escherichia coli of an extracellular lipase from Serratia marcescens
    • X. Li, S. Tetling, U.K. Winkler, K.E. Jaeger, and M.J. Benedik Gene cloning, sequence analysis, purification, and secretion by Escherichia coli of an extracellular lipase from Serratia marcescens Appl. Environ. Microbiol. 61 1995 2674 2680
    • (1995) Appl. Environ. Microbiol. , vol.61 , pp. 2674-2680
    • Li, X.1    Tetling, S.2    Winkler, U.K.3    Jaeger, K.E.4    Benedik, M.J.5
  • 22
    • 0024598450 scopus 로고
    • Structure of the cutinase gene and detection of promoter activity in the 5'-flanking region by fungal transformation
    • C.L. Soliday, M.B. Dickman, and P.E. Kolattukudy Structure of the cutinase gene and detection of promoter activity in the 5'-flanking region by fungal transformation J. Bacteriol. 171 1989 1942 1951
    • (1989) J. Bacteriol. , vol.171 , pp. 1942-1951
    • Soliday, C.L.1    Dickman, M.B.2    Kolattukudy, P.E.3
  • 24
    • 0030608368 scopus 로고    scopus 로고
    • Absence of periplasmic DsbA oxidoreductase facilitates export of cysteine-containing passenger proteins to the Escherichia coli cell surface via the Iga β autotransporter pathway
    • J. Jose, J. Kramer, T. Klauser, J. Pohlner, and T.F. Meyer Absence of periplasmic DsbA oxidoreductase facilitates export of cysteine-containing passenger proteins to the Escherichia coli cell surface via the Iga β autotransporter pathway Gene 178 1996 107 110
    • (1996) Gene , vol.178 , pp. 107-110
    • Jose, J.1    Kramer, J.2    Klauser, T.3    Pohlner, J.4    Meyer, T.F.5
  • 25
    • 0032824531 scopus 로고    scopus 로고
    • The cystine knot of a squash-type protease inhibitor as a structural scaffold for Escherichia coli cell surface display of conformationally constrained peptides
    • A. Christmann, K. Walter, A. Wentzel, R. Krätzner, and H. Kolmar The cystine knot of a squash-type protease inhibitor as a structural scaffold for Escherichia coli cell surface display of conformationally constrained peptides Protein Eng. 12 1999 797 806
    • (1999) Protein Eng. , vol.12 , pp. 797-806
    • Christmann, A.1    Walter, K.2    Wentzel, A.3    Krätzner, R.4    Kolmar, H.5
  • 26
    • 3242687055 scopus 로고    scopus 로고
    • Autodisplay of active sorbitol dehydrogenase (SDH) yields a whole cell biocatalyst for the synthesis of rare sugars
    • J. Jose, and S. von Schwichow Autodisplay of active sorbitol dehydrogenase (SDH) yields a whole cell biocatalyst for the synthesis of rare sugars Chembiochemistry 5 2004 491 499
    • (2004) Chembiochemistry , vol.5 , pp. 491-499
    • Jose, J.1    Von Schwichow, S.2
  • 27
    • 0023128808 scopus 로고
    • Gene structure and extracellular secretion of Neisseria gonorrhoeae IgA protease
    • J. Pohlner, R. Halter, K. Beyreuther, and T.F. Meyer Gene structure and extracellular secretion of Neisseria gonorrhoeae IgA protease Nature 325 1987 458 462
    • (1987) Nature , vol.325 , pp. 458-462
    • Pohlner, J.1    Halter, R.2    Beyreuther, K.3    Meyer, T.F.4
  • 28
    • 0041813141 scopus 로고    scopus 로고
    • Directed evolution of an enantioselective Bacillus subtilis lipase
    • S.A. Funke Directed evolution of an enantioselective Bacillus subtilis lipase Biocatal. Biotransform. 21 2003 67 73
    • (2003) Biocatal. Biotransform. , vol.21 , pp. 67-73
    • Funke, S.A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.