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Volumn 74, Issue 4, 2008, Pages 1167-1175

Relevant double mutations in bioengineered Streptomyces clavuligerus deacetoxycephalosporin C synthase result in higher binding specificities which improve penicillin bioconversion

Author keywords

[No Author keywords available]

Indexed keywords

AMPICILLIN CONVERSION; CEPHALOSPORIN SYNTHESIS; ENZYME CATALYSIS; SUBSTRATE BINDING AFFINITY;

EID: 39649095868     PISSN: 00992240     EISSN: None     Source Type: Journal    
DOI: 10.1128/AEM.02230-07     Document Type: Article
Times cited : (18)

References (28)
  • 1
    • 0037010875 scopus 로고    scopus 로고
    • Construction of hybrid bacterial deacetoxycephalosporin C synthases (expandases) by in vivo homeologous recombination
    • Adrio, J. L., G. A. Hintermann, A. L. Demain, and J. M. Piret. 2002. Construction of hybrid bacterial deacetoxycephalosporin C synthases (expandases) by in vivo homeologous recombination. Enzyme Microb. Technol. 31:932-940.
    • (2002) Enzyme Microb. Technol , vol.31 , pp. 932-940
    • Adrio, J.L.1    Hintermann, G.A.2    Demain, A.L.3    Piret, J.M.4
  • 2
    • 0036305290 scopus 로고    scopus 로고
    • C-terminus modification of Streptomyces clavuligerus deacetoxycephalosporin C synthase improves catalysis with an expanded substrate specificity
    • Chin, H. S., and T. S. Sim. 2002. C-terminus modification of Streptomyces clavuligerus deacetoxycephalosporin C synthase improves catalysis with an expanded substrate specificity. Biochem. Biophys. Res. Commun. 295:55-61.
    • (2002) Biochem. Biophys. Res. Commun , vol.295 , pp. 55-61
    • Chin, H.S.1    Sim, T.S.2
  • 3
    • 0035929372 scopus 로고    scopus 로고
    • Mutation of N304 to leucine in Streptomyces clavuligerus deacetoxycephalosporin C synthase creates an enzyme with increased penicillin analogue conversion
    • Chin, H. S., J. Sim, and T. S. Sim. 2001. Mutation of N304 to leucine in Streptomyces clavuligerus deacetoxycephalosporin C synthase creates an enzyme with increased penicillin analogue conversion. Biochem. Biophys. Res. Commun. 287:507-513.
    • (2001) Biochem. Biophys. Res. Commun , vol.287 , pp. 507-513
    • Chin, H.S.1    Sim, J.2    Sim, T.S.3
  • 4
    • 0345868794 scopus 로고    scopus 로고
    • A complete library of amino acid alterations at N304 in Streptomyces clavuligerus deacetoxycephalosporin C synthase elucidates the basis for enhanced penicillin analogue conversion
    • Chin, H. S., K. S. Goo, and T. S. Sim. 2004. A complete library of amino acid alterations at N304 in Streptomyces clavuligerus deacetoxycephalosporin C synthase elucidates the basis for enhanced penicillin analogue conversion. Appl. Environ. Microbiol. 70:607-609.
    • (2004) Appl. Environ. Microbiol , vol.70 , pp. 607-609
    • Chin, H.S.1    Goo, K.S.2    Sim, T.S.3
  • 5
    • 0033051211 scopus 로고    scopus 로고
    • The beta-lactam antibiotics: Past, present, and future
    • Demain, A. L., and R. P. Elander. 1999. The beta-lactam antibiotics: past, present, and future. Antonie van Leeuwenhoek 75:5-19.
    • (1999) Antonie van Leeuwenhoek , vol.75 , pp. 5-19
    • Demain, A.L.1    Elander, R.P.2
  • 6
    • 0034968454 scopus 로고    scopus 로고
    • Probing the penicillin sidechain selectivity of recombinant deacetoxycephalosporin C synthase
    • Dubus, A., M. D. Lloyd, H. J. Lee, C. J. Schofield, J. E. Baldwin, and J. M. Frere. 2001. Probing the penicillin sidechain selectivity of recombinant deacetoxycephalosporin C synthase. Cell. Mol. Life Sci. 58:835-843.
    • (2001) Cell. Mol. Life Sci , vol.58 , pp. 835-843
    • Dubus, A.1    Lloyd, M.D.2    Lee, H.J.3    Schofield, C.J.4    Baldwin, J.E.5    Frere, J.M.6
  • 7
    • 0038236925 scopus 로고    scopus 로고
    • Industrial production of β-lactam antibiotics
    • Elander, R. P. 2003. Industrial production of β-lactam antibiotics. Appl. Microbiol. Biotechnol. 61:385-392.
    • (2003) Appl. Microbiol. Biotechnol , vol.61 , pp. 385-392
    • Elander, R.P.1
  • 8
    • 0037568271 scopus 로고    scopus 로고
    • Performance of a recombinant strain of Streptomyces lividans for bioconversion of penicillin G to deacetoxycephalosporin G
    • Gao, Q., J. M. Piret, J. L. Adrio, and A. L. Demain. 2003. Performance of a recombinant strain of Streptomyces lividans for bioconversion of penicillin G to deacetoxycephalosporin G. J. Ind. Microbiol. Biotechnol. 30:190-194.
    • (2003) J. Ind. Microbiol. Biotechnol , vol.30 , pp. 190-194
    • Gao, Q.1    Piret, J.M.2    Adrio, J.L.3    Demain, A.L.4
  • 9
    • 38549098629 scopus 로고    scopus 로고
    • Goo, K. S., C. S. Chua, and T. S. Sim. 29 August 2007, posting date. A complete library of amino acid alterations at R306 in Streptomyces clavuligerus deacetoxycephalosporin C synthase demonstrates its structural role in the ring-expansion activity. Proteins. doi:10.1002/prot.21549.
    • Goo, K. S., C. S. Chua, and T. S. Sim. 29 August 2007, posting date. A complete library of amino acid alterations at R306 in Streptomyces clavuligerus deacetoxycephalosporin C synthase demonstrates its structural role in the ring-expansion activity. Proteins. doi:10.1002/prot.21549.
  • 11
    • 9744226460 scopus 로고    scopus 로고
    • A twisted base? The role of arginine in enzyme-catalyzed proton abstractions
    • Guillen Schlippe, Y. V., and L. Hedstrom. 2005. A twisted base? The role of arginine in enzyme-catalyzed proton abstractions. Arch. Biochem. Biophys. 433:266-278.
    • (2005) Arch. Biochem. Biophys , vol.433 , pp. 266-278
    • Guillen Schlippe, Y.V.1    Hedstrom, L.2
  • 12
    • 8144223713 scopus 로고    scopus 로고
    • Family shuffling of expandase genes to enhance substrate specificity for penicillin G
    • Hsu, J. S., Y. B. Yang, C. H. Deng, C. L. Wei, S. H. Liaw, and Y. C. Tsai. 2004. Family shuffling of expandase genes to enhance substrate specificity for penicillin G. Appl. Environ. Microbiol. 70:6257-6263.
    • (2004) Appl. Environ. Microbiol , vol.70 , pp. 6257-6263
    • Hsu, J.S.1    Yang, Y.B.2    Deng, C.H.3    Wei, C.L.4    Liaw, S.H.5    Tsai, Y.C.6
  • 13
    • 0036294889 scopus 로고    scopus 로고
    • Active site mutations of recombinant deacetoxycephalosporin C synthase
    • Lee, H. J., C. J. Schofield, and M. D. Lloyd. 2002. Active site mutations of recombinant deacetoxycephalosporin C synthase. Biochem. Biophys. Res. Commun. 292:66-70.
    • (2002) Biochem. Biophys. Res. Commun , vol.292 , pp. 66-70
    • Lee, H.J.1    Schofield, C.J.2    Lloyd, M.D.3
  • 14
    • 0036268258 scopus 로고    scopus 로고
    • The role of arginine residues in substrate binding and catalysis by deacetoxycephalosporin C synthase
    • Lipscomb, S. J., H. J. Lee, M. Mukherji, J. E. Baldwin, C. J. Schofield, and M. D. Lloyd. 2002. The role of arginine residues in substrate binding and catalysis by deacetoxycephalosporin C synthase. Eur. J. Biochem. 269:2735-2739.
    • (2002) Eur. J. Biochem , vol.269 , pp. 2735-2739
    • Lipscomb, S.J.1    Lee, H.J.2    Mukherji, M.3    Baldwin, J.E.4    Schofield, C.J.5    Lloyd, M.D.6
  • 16
    • 0028921970 scopus 로고
    • Structural and functional effects of multiple mutations at distal sites in cytochrome c
    • Lo, T. P., S. Komar-Panicucci, F. Sherman, G. McLendon, and G. D. Brayer. 1995. Structural and functional effects of multiple mutations at distal sites in cytochrome c. Biochemistry 34:5259-5268.
    • (1995) Biochemistry , vol.34 , pp. 5259-5268
    • Lo, T.P.1    Komar-Panicucci, S.2    Sherman, F.3    McLendon, G.4    Brayer, G.D.5
  • 17
    • 0034759282 scopus 로고    scopus 로고
    • A comparison of three site-directed mutagenesis kits
    • Loke, P., and T. S. Sim. 2001. A comparison of three site-directed mutagenesis kits. Z. Naturforsch. 56:810-813.
    • (2001) Z. Naturforsch , vol.56 , pp. 810-813
    • Loke, P.1    Sim, T.S.2
  • 18
    • 0026681635 scopus 로고
    • Quantitative interpretations of double mutations of enzymes
    • Mildvan, A. S., D. J. Weber, and A. Kuliopulos. 1992. Quantitative interpretations of double mutations of enzymes. Arch. Biochem. Biophys. 294:327-340.
    • (1992) Arch. Biochem. Biophys , vol.294 , pp. 327-340
    • Mildvan, A.S.1    Weber, D.J.2    Kuliopulos, A.3
  • 19
    • 0035812391 scopus 로고    scopus 로고
    • In vitro conversion of penicillin G and ampicillin by recombinant Streptomyces clavuligerus NRRL 3585 deacetoxycephalosporin C synthase
    • Sim, J., and T. S. Sim. 2001. In vitro conversion of penicillin G and ampicillin by recombinant Streptomyces clavuligerus NRRL 3585 deacetoxycephalosporin C synthase. Enzyme Microb. Technol. 29:240-245.
    • (2001) Enzyme Microb. Technol , vol.29 , pp. 240-245
    • Sim, J.1    Sim, T.S.2
  • 20
    • 0029785464 scopus 로고    scopus 로고
    • Potential use of additivity of mutational effects in simplifying protein engineering
    • Skinner, M. M., and T. C. Terwilliger. 1996. Potential use of additivity of mutational effects in simplifying protein engineering. Proc. Natl. Acad. Sci. USA 93:10753-10757.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 10753-10757
    • Skinner, M.M.1    Terwilliger, T.C.2
  • 21
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson, J. D., D. G. Higgins, and T. J. Gibson. 1994. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22:4673-4680.
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 24
    • 0033898359 scopus 로고    scopus 로고
    • Environmentally safe production of 7- aminodeacetoxycephalosporanic acid (7-ADCA) using recombinant strains of Acremonium chrysogenum
    • Velasco, J., J. L. Adrio, M. Angel-Moreno, B. Diez, G. Soler, and J. L. Barredo. 2000. Environmentally safe production of 7- aminodeacetoxycephalosporanic acid (7-ADCA) using recombinant strains of Acremonium chrysogenum. Nat. Biotechnol. 18:857-861.
    • (2000) Nat. Biotechnol , vol.18 , pp. 857-861
    • Velasco, J.1    Adrio, J.L.2    Angel-Moreno, M.3    Diez, B.4    Soler, G.5    Barredo, J.L.6
  • 25
    • 0028922586 scopus 로고
    • LIGPLOT: A program to generate schematic diagrams of protein-ligand interactions
    • Wallace, A. C., R. A. Laskowski, and J. M. Thornton. 1995. LIGPLOT: a program to generate schematic diagrams of protein-ligand interactions. Prot. Eng. 8:127-134.
    • (1995) Prot. Eng , vol.8 , pp. 127-134
    • Wallace, A.C.1    Laskowski, R.A.2    Thornton, J.M.3
  • 26
    • 29144459217 scopus 로고    scopus 로고
    • Directed evolution of Streptomyces clavuligerus deacetoxycephalosporin C synthase for enhancement of penicillin G expansion
    • Wei, C. L., Y. B. Yang, C. H. Deng, W. C. Liu, J. S. Hsu, Y. C. Lin, S. H. Liaw, and Y. C. Tsai. 2005. Directed evolution of Streptomyces clavuligerus deacetoxycephalosporin C synthase for enhancement of penicillin G expansion. Appl. Environ. Microbiol. 71:8873-8880.
    • (2005) Appl. Environ. Microbiol , vol.71 , pp. 8873-8880
    • Wei, C.L.1    Yang, Y.B.2    Deng, C.H.3    Liu, W.C.4    Hsu, J.S.5    Lin, Y.C.6    Liaw, S.H.7    Tsai, Y.C.8
  • 27
    • 0242416599 scopus 로고    scopus 로고
    • Engineering Streptomyces clavuligerus deacetoxycephalosporin C synthase for optimal ring expansion activity toward penicillin G
    • Wei, C. L., Y. B. Yang, W. C. Wang, W. C. Liu, J. S. Hsu, and Y. C. Tsa. 2003. Engineering Streptomyces clavuligerus deacetoxycephalosporin C synthase for optimal ring expansion activity toward penicillin G. Appl. Environ. Microbiol. 69:2306-2312.
    • (2003) Appl. Environ. Microbiol , vol.69 , pp. 2306-2312
    • Wei, C.L.1    Yang, Y.B.2    Wang, W.C.3    Liu, W.C.4    Hsu, J.S.5    Tsa, Y.C.6
  • 28
    • 0025082684 scopus 로고
    • Additivity of mutational effects in proteins
    • Wells, J. A. 1990. Additivity of mutational effects in proteins. Biochemistry 29:8509-8517.
    • (1990) Biochemistry , vol.29 , pp. 8509-8517
    • Wells, J.A.1


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