메뉴 건너뛰기




Volumn 131, Issue 4, 2007, Pages 425-432

Directed evolution of transketolase activity on non-phosphorylated substrates

Author keywords

Biocatalysis; Directed evolution; Phylogenetics; Protein engineering; Transketolase

Indexed keywords

MUTAGENESIS; PHOSPHATES; PHOSPHORYLATION; REACTION KINETICS; SATURATION (MATERIALS COMPOSITION); SUBSTITUTION REACTIONS;

EID: 34648843275     PISSN: 01681656     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jbiotec.2007.07.949     Document Type: Article
Times cited : (74)

References (43)
  • 3
    • 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.H. Tuning the activity of an enzyme for unusual environments: sequential random mutagenesis of subtilisin E for catalysis in dimethylformamide. Proc. Natl. Acad. Sci. U.S.A. 90 (1993) 5618-5622
    • (1993) Proc. Natl. Acad. Sci. U.S.A. , vol.90 , pp. 5618-5622
    • Chen, K.1    Arnold, F.H.2
  • 4
    • 33745726188 scopus 로고    scopus 로고
    • Improved mutants from directed evolution are biased to orthologous substitutions
    • Cochran J.R., Kim Y.S., Lippow S.M., Rao B., and Wittrup K.D. Improved mutants from directed evolution are biased to orthologous substitutions. Protein Eng. Des. Sel. 19 (2006) 245-253
    • (2006) Protein Eng. Des. Sel. , vol.19 , pp. 245-253
    • Cochran, J.R.1    Kim, Y.S.2    Lippow, S.M.3    Rao, B.4    Wittrup, K.D.5
  • 5
    • 0042430535 scopus 로고    scopus 로고
    • Optimising enzyme function by directed evolution
    • Dalby P.A. Optimising enzyme function by directed evolution. Curr. Opin. Struct. Biol. 13 (2003) 500-505
    • (2003) Curr. Opin. Struct. Biol. , vol.13 , pp. 500-505
    • Dalby, P.A.1
  • 6
    • 33750317306 scopus 로고    scopus 로고
    • Bioinformatics-driven, rational engineering of protein thermostability
    • DiTursi M.K., Kwon S.J., Reeder P.J., and Dordick J.S. Bioinformatics-driven, rational engineering of protein thermostability. Protein Eng. Des. Sel. 19 (2006) 517-524
    • (2006) Protein Eng. Des. Sel. , vol.19 , pp. 517-524
    • DiTursi, M.K.1    Kwon, S.J.2    Reeder, P.J.3    Dordick, J.S.4
  • 7
    • 3042655537 scopus 로고    scopus 로고
    • Computational design of a biologically active enzyme
    • Dwyer M.A., Looger L.L., and Hellinga H.W. Computational design of a biologically active enzyme. Science 304 (2004) 1967-1971
    • (2004) Science , vol.304 , pp. 1967-1971
    • Dwyer, M.A.1    Looger, L.L.2    Hellinga, H.W.3
  • 8
    • 0000122573 scopus 로고
    • PHYLIP - Phylogeny Inference Package (Version 3.2)
    • Felsenstein J. PHYLIP - Phylogeny Inference Package (Version 3.2). Cladistics 5 (1989) 164-166
    • (1989) Cladistics , vol.5 , pp. 164-166
    • Felsenstein, J.1
  • 9
    • 23944434781 scopus 로고    scopus 로고
    • A modified consensus approach to mutagenesis inverts the cofactor specificity of Bacillus stearothermophilus lactate dehydrogenase
    • Flores H., and Ellington A.D. A modified consensus approach to mutagenesis inverts the cofactor specificity of Bacillus stearothermophilus lactate dehydrogenase. Protein Eng. Des. Sel. 18 (2005) 369-377
    • (2005) Protein Eng. Des. Sel. , vol.18 , pp. 369-377
    • Flores, H.1    Ellington, A.D.2
  • 10
    • 0028922711 scopus 로고
    • Improved production and stability of E. coli recombinants expressing transketolase for large scale biotransformation
    • French C., and Ward J.M. Improved production and stability of E. coli recombinants expressing transketolase for large scale biotransformation. Biotechnol. Lett. 17 (1995) 247-252
    • (1995) Biotechnol. Lett. , vol.17 , pp. 247-252
    • French, C.1    Ward, J.M.2
  • 11
    • 0035121685 scopus 로고    scopus 로고
    • Specific glycosidase activity isolated from a random phage display antibody library
    • Goud G.N., Artsaenko O., Bols M., and Sierks M. Specific glycosidase activity isolated from a random phage display antibody library. Biotechnol. Prog. 17 (2001) 197-202
    • (2001) Biotechnol. Prog. , vol.17 , pp. 197-202
    • Goud, G.N.1    Artsaenko, O.2    Bols, M.3    Sierks, M.4
  • 12
    • 0031081566 scopus 로고    scopus 로고
    • Kinetics of overexpressed transketolase from Escherichia coli JM 107/pQR 700
    • Gyamerah M., and Willetts A.J. Kinetics of overexpressed transketolase from Escherichia coli JM 107/pQR 700. Enzyme Microb. Technol. 20 (1997) 127-134
    • (1997) Enzyme Microb. Technol. , vol.20 , pp. 127-134
    • Gyamerah, M.1    Willetts, A.J.2
  • 13
    • 34648870929 scopus 로고    scopus 로고
    • Hall, T.A., 1999. BioEdit: a user-friendly biological sequence alignment editor and analysis. http://www.mbio.ncsu.edu/BioEdit/bioedit.html.
  • 15
    • 33846904594 scopus 로고    scopus 로고
    • One-pot synthesis of amino-alcohols using a de-novo transketolase and β-alanine:pyruvate transaminase pathway in Escherichia coli
    • Ingram C.U., Bommer M., Smith M.E.B., Dalby P.A., Ward J.M., Hailes H.C., and Lye G.J. One-pot synthesis of amino-alcohols using a de-novo transketolase and β-alanine:pyruvate transaminase pathway in Escherichia coli. Biotechnol. Bioeng. 96 (2007) 559-569
    • (2007) Biotechnol. Bioeng. , vol.96 , pp. 559-569
    • Ingram, C.U.1    Bommer, M.2    Smith, M.E.B.3    Dalby, P.A.4    Ward, J.M.5    Hailes, H.C.6    Lye, G.J.7
  • 17
    • 0026762799 scopus 로고
    • 3-Dimensional structure of transketolase, a thiamine diphosphate dependent enzyme, at 2.5 Angstrom resolution
    • Lindqvist Y., Schneider G., Ermler U., and Sundstrom M. 3-Dimensional structure of transketolase, a thiamine diphosphate dependent enzyme, at 2.5 Angstrom resolution. EMBO J. 11 (1992) 2373-2379
    • (1992) EMBO J. , vol.11 , pp. 2373-2379
    • Lindqvist, Y.1    Schneider, G.2    Ermler, U.3    Sundstrom, M.4
  • 18
    • 0029199270 scopus 로고
    • Crystallization and preliminary-X-ray crystallographic data with Escherichia-coli transketolase
    • Littlechild J.A., Turner N.J., Hobbs G.R., Lilly M.D., Rawas A., and Watson H. Crystallization and preliminary-X-ray crystallographic data with Escherichia-coli transketolase. Acta Crystallogr. D 51 (1995) 1074-1076
    • (1995) Acta Crystallogr. , vol.D 51 , pp. 1074-1076
    • Littlechild, J.A.1    Turner, N.J.2    Hobbs, G.R.3    Lilly, M.D.4    Rawas, A.5    Watson, H.6
  • 19
    • 0033280672 scopus 로고    scopus 로고
    • Exploring nonnatural evolutionary pathways by saturation mutagenesis: rapid improvement of protein function
    • Miyazaki K., and Arnold F.H. Exploring nonnatural evolutionary pathways by saturation mutagenesis: rapid improvement of protein function. J. Mol. Evol. 49 (1999) 716-720
    • (1999) J. Mol. Evol. , vol.49 , pp. 716-720
    • Miyazaki, K.1    Arnold, F.H.2
  • 20
    • 18144403554 scopus 로고    scopus 로고
    • Improving enzyme properties: when are closer mutations better?
    • Morley K.L., and Kazlauskas R.J. Improving enzyme properties: when are closer mutations better?. Trends Biotechnol. 23 (2005) 231-237
    • (2005) Trends Biotechnol. , vol.23 , pp. 231-237
    • Morley, K.L.1    Kazlauskas, R.J.2
  • 21
    • 0030220903 scopus 로고    scopus 로고
    • Transketolase from Escherichia coli: a practical procedure for using the biocatalyst for asymmetric carbon-carbon bond synthesis
    • Morris K.G., Smith M.E.B., Turner N.J., Lilly M.D., Mitra R.K., and Woodley J.M. Transketolase from Escherichia coli: a practical procedure for using the biocatalyst for asymmetric carbon-carbon bond synthesis. Tetrahedron Asymm. 7 (1996) 2185-2188
    • (1996) Tetrahedron Asymm. , vol.7 , pp. 2185-2188
    • Morris, K.G.1    Smith, M.E.B.2    Turner, N.J.3    Lilly, M.D.4    Mitra, R.K.5    Woodley, J.M.6
  • 22
    • 17144411489 scopus 로고    scopus 로고
    • Engineering of a thioglycoligase: randomized mutagenesis of the acid-base residue leads to the identification of improved catalysts
    • Mullegger J., Jahn M., Chen H.M., Warren R.A.J., and Withers S.G. Engineering of a thioglycoligase: randomized mutagenesis of the acid-base residue leads to the identification of improved catalysts. Protein Eng. Des. Sel. 18 (2005) 33-40
    • (2005) Protein Eng. Des. Sel. , vol.18 , pp. 33-40
    • Mullegger, J.1    Jahn, M.2    Chen, H.M.3    Warren, R.A.J.4    Withers, S.G.5
  • 23
    • 0037325329 scopus 로고    scopus 로고
    • EF-Tu binding peptides identified, dissected, and affinity optimized by phage display
    • Murase K., Morrison K.L., Tam P.Y., Stafford R.L., Jurnak F., and Weiss G.A. EF-Tu binding peptides identified, dissected, and affinity optimized by phage display. Chem. Biol. 10 (2003) 161-168
    • (2003) Chem. Biol. , vol.10 , pp. 161-168
    • Murase, K.1    Morrison, K.L.2    Tam, P.Y.3    Stafford, R.L.4    Jurnak, F.5    Weiss, G.A.6
  • 25
    • 0028305456 scopus 로고
    • Refined structure of transketolase from Saccharomyces cerevisiae at 2.0 Å resolution
    • Nikkola M., Lindqvist Y., and Schneider G. Refined structure of transketolase from Saccharomyces cerevisiae at 2.0 Å resolution. J. Mol. Biol. 238 (1994) 387-404
    • (1994) J. Mol. Biol. , vol.238 , pp. 387-404
    • Nikkola, M.1    Lindqvist, Y.2    Schneider, G.3
  • 26
    • 0031029945 scopus 로고    scopus 로고
    • Examination of substrate binding in thiamin diphosphate-dependent transketolase by protein crystallography and site-directed mutagenesis
    • Nilsson U., Meshalkina L., Lindqvist Y., and Schneider G. Examination of substrate binding in thiamin diphosphate-dependent transketolase by protein crystallography and site-directed mutagenesis. J. Biol. Chem. 272 (1997) 1864-1869
    • (1997) J. Biol. Chem. , vol.272 , pp. 1864-1869
    • Nilsson, U.1    Meshalkina, L.2    Lindqvist, Y.3    Schneider, G.4
  • 27
    • 24044554219 scopus 로고    scopus 로고
    • Site-saturation mutagenesis is more efficient than DNA shuffling for the directed evolution of β-fucosidase from β-galactosidase
    • Parikh M.R., and Matsumura I. Site-saturation mutagenesis is more efficient than DNA shuffling for the directed evolution of β-fucosidase from β-galactosidase. J. Mol. Biol. 352 (2005) 621-628
    • (2005) J. Mol. Biol. , vol.352 , pp. 621-628
    • Parikh, M.R.1    Matsumura, I.2
  • 28
    • 12344337569 scopus 로고    scopus 로고
    • Focusing mutations into the P. fluorescens esterase binding site increases enantioselectivity more effectively than distant mutations
    • Park S., Morley K.L., Horsman G.P., Holmquist M., Hult K., and Kazlauskas R.J. Focusing mutations into the P. fluorescens esterase binding site increases enantioselectivity more effectively than distant mutations. Chem. Biol. 12 (2005) 45-54
    • (2005) Chem. Biol. , vol.12 , pp. 45-54
    • Park, S.1    Morley, K.L.2    Horsman, G.P.3    Holmquist, M.4    Hult, K.5    Kazlauskas, R.J.6
  • 29
    • 0037245613 scopus 로고    scopus 로고
    • Evolutionary engineering of a beta-lactamase activity on a d-Ala d-Ala transpeptidase fold
    • Peimbert M., and Segovia L. Evolutionary engineering of a beta-lactamase activity on a d-Ala d-Ala transpeptidase fold. Protein Eng. 16 (2003) 27-35
    • (2003) Protein Eng. , vol.16 , pp. 27-35
    • Peimbert, M.1    Segovia, L.2
  • 30
    • 0037007010 scopus 로고    scopus 로고
    • Directed evolution of the site specificity of Cre recombinase
    • Santoro S.W., and Schultz P.G. Directed evolution of the site specificity of Cre recombinase. Proc. Natl. Acad. Sci. U.S.A. 99 (2002) 4185-4190
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 4185-4190
    • Santoro, S.W.1    Schultz, P.G.2
  • 31
    • 3342927059 scopus 로고    scopus 로고
    • Dissecting the engrailed homeodomain-DNA interaction by phage-displayed shotgun scanning
    • Sato K., Simon M.D., Levin A.M., Shokat K.M., and Weiss G.A. Dissecting the engrailed homeodomain-DNA interaction by phage-displayed shotgun scanning. Chem. Biol. 11 (2004) 1017-1023
    • (2004) Chem. Biol. , vol.11 , pp. 1017-1023
    • Sato, K.1    Simon, M.D.2    Levin, A.M.3    Shokat, K.M.4    Weiss, G.A.5
  • 32
    • 0032423288 scopus 로고    scopus 로고
    • Properties and functions of the thiamin diphosphate dependent enzyme transketolase
    • Schenk G., Duggleby R.G., and Nixon P.F. Properties and functions of the thiamin diphosphate dependent enzyme transketolase. Int. J. Biochem. Cell B 30 (1998) 1297-1318
    • (1998) Int. J. Biochem. Cell B , vol.30 , pp. 1297-1318
    • Schenk, G.1    Duggleby, R.G.2    Nixon, P.F.3
  • 33
    • 14644433770 scopus 로고    scopus 로고
    • Combinatorial exploration of the catalytic site of a drug- resistant dihydrofolate reductase: creating alternative functional configurations
    • Schmitzer A.R., Lepine F., and Pelletier J.N. Combinatorial exploration of the catalytic site of a drug- resistant dihydrofolate reductase: creating alternative functional configurations. Protein Eng. Des. Sel. 17 (2004) 809-819
    • (2004) Protein Eng. Des. Sel. , vol.17 , pp. 809-819
    • Schmitzer, A.R.1    Lepine, F.2    Pelletier, J.N.3
  • 34
    • 33745756312 scopus 로고    scopus 로고
    • Semiquantitative process screening for the biocatalytic synthesis of d-xylulose-5-phosphate
    • Shaeri J., Wohlgemuth R., and Woodley J.M. Semiquantitative process screening for the biocatalytic synthesis of d-xylulose-5-phosphate. Org. Process. Res. Dev. 10 (2006) 605-610
    • (2006) Org. Process. Res. Dev. , vol.10 , pp. 605-610
    • Shaeri, J.1    Wohlgemuth, R.2    Woodley, J.M.3
  • 35
    • 0035374671 scopus 로고    scopus 로고
    • The conserved active site motif a of Escherichia coli DNA polymerase I is highly mutable
    • Shinkai A., Patel P.H., and Loeb L.A. The conserved active site motif a of Escherichia coli DNA polymerase I is highly mutable. J. Biol. Chem. 276. (2001) 18836-18842
    • (2001) J. Biol. Chem. , vol.276 , pp. 18836-18842
    • Shinkai, A.1    Patel, P.H.2    Loeb, L.A.3
  • 36
    • 0033545539 scopus 로고    scopus 로고
    • Synthetic potential of thiamin diphosphate-dependent enzymes
    • Sprenger G.A., and Pohl M. Synthetic potential of thiamin diphosphate-dependent enzymes. J. Mol. Catal. B: Enzyme 6 (1999) 145-159
    • (1999) J. Mol. Catal. B: Enzyme , vol.6 , pp. 145-159
    • Sprenger, G.A.1    Pohl, M.2
  • 37
    • 0029067816 scopus 로고
    • Transketolase A of Escherichia coli K12. Purification and properties of the enzyme from recombinant strains
    • Sprenger G.A., Schorken U., Sprenger G., and Sahm H. Transketolase A of Escherichia coli K12. Purification and properties of the enzyme from recombinant strains. Eur. J. Biochem. 230 (1995) 525-532
    • (1995) Eur. J. Biochem. , vol.230 , pp. 525-532
    • Sprenger, G.A.1    Schorken, U.2    Sprenger, G.3    Sahm, H.4
  • 38
    • 0028050350 scopus 로고
    • Rapid evolution of a protein in vitro by DNA shuffling
    • Stemmer W.P.C. Rapid evolution of a protein in vitro by DNA shuffling. Nature 370 (1994) 389-391
    • (1994) Nature , vol.370 , pp. 389-391
    • Stemmer, W.P.C.1
  • 39
    • 0035682509 scopus 로고    scopus 로고
    • Phage-display evolution of tyrosine kinases with altered nucleotide specificity
    • Ting A.Y., Witte K., Shah K., Kraybill B., Shokat K.M., and Schultz P.G. Phage-display evolution of tyrosine kinases with altered nucleotide specificity. Biopolymers 60 (2001) 220-228
    • (2001) Biopolymers , vol.60 , pp. 220-228
    • Ting, A.Y.1    Witte, K.2    Shah, K.3    Kraybill, B.4    Shokat, K.M.5    Schultz, P.G.6
  • 40
    • 0033638491 scopus 로고    scopus 로고
    • Applications of transketolases in organic synthesis
    • Turner N.J. Applications of transketolases in organic synthesis. Curr. Opin. Biotechnol. 11 (2000) 527-531
    • (2000) Curr. Opin. Biotechnol. , vol.11 , pp. 527-531
    • Turner, N.J.1
  • 41
    • 0035917812 scopus 로고    scopus 로고
    • Expanding the genetic code of Escherichia coli
    • Wang L., Brock A., Herberich B., and Schultz P.G. Expanding the genetic code of Escherichia coli. Science 292 (2001) 498-500
    • (2001) Science , vol.292 , pp. 498-500
    • Wang, L.1    Brock, A.2    Herberich, B.3    Schultz, P.G.4
  • 42
    • 33645666942 scopus 로고    scopus 로고
    • Darwinian evolution can follow only very few mutational paths to fitter proteins
    • Weinreich D.M., Delaney N.F., DePristo M.A., and Hartl D.L. Darwinian evolution can follow only very few mutational paths to fitter proteins. Science 312 (2006) 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
  • 43
    • 0030683599 scopus 로고    scopus 로고
    • PAML: a program package for phylogenetic analysis by maximum likelihood
    • Yang Z. PAML: a program package for phylogenetic analysis by maximum likelihood. Comput. Appl. Biosci. 13 (1997) 555-556
    • (1997) Comput. Appl. Biosci. , vol.13 , pp. 555-556
    • Yang, Z.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.