메뉴 건너뛰기




Volumn 72, Issue 12, 2006, Pages 7510-7517

Identification of novel benzoylformate decarboxylases by growth selection

Author keywords

[No Author keywords available]

Indexed keywords

ALDEHYDES; CARBON; DNA SEQUENCES; ENZYMES; GENES; SUBSTRATES;

EID: 33845526196     PISSN: 00992240     EISSN: None     Source Type: Journal    
DOI: 10.1128/AEM.01541-06     Document Type: Article
Times cited : (17)

References (50)
  • 2
    • 0022374435 scopus 로고
    • Phenylglyoxylate decarboxylase and phenylpyruvate decarboxylase from Acinetobacter calcoaceticus
    • Barrowman, M. M., and C. A. Fewson. 1985. Phenylglyoxylate decarboxylase and phenylpyruvate decarboxylase from Acinetobacter calcoaceticus. Curr. Microbiol. 12:235-239.
    • (1985) Curr. Microbiol. , vol.12 , pp. 235-239
    • Barrowman, M.M.1    Fewson, C.A.2
  • 3
    • 0022612491 scopus 로고
    • Immunological comparison of microbial TPP-dependent nonoxidative alpha-keto acid decarboxylases
    • 2a.Barrowman, M. M., W. Harnett, A. J. Scott, C. A. Fewson, and J. R. Kusel. 1986. Immunological comparison of microbial TPP-dependent nonoxidative alpha-keto acid decarboxylases. FEMS Microbiol. Lett. 34:57-60.
    • (1986) FEMS Microbiol. Lett. , vol.34 , pp. 57-60
    • Barrowman, M.M.1    Harnett, W.2    Scott, A.J.3    Fewson, C.A.4    Kusel, J.R.5
  • 4
    • 4344646564 scopus 로고    scopus 로고
    • Engineering a ligand-dependent RNA transcriptional activator
    • Buskirk, A. R., A. Landrigan, and D. R. Liu. 2004. Engineering a ligand-dependent RNA transcriptional activator. Chem. Biol. 11:1157-1163.
    • (2004) Chem. Biol. , vol.11 , pp. 1157-1163
    • Buskirk, A.R.1    Landrigan, A.2    Liu, D.R.3
  • 5
    • 0042008057 scopus 로고    scopus 로고
    • Role of GlnB and GlnK in ammonium control of both nitrogenase systems in the phototrophic bacterium Rhodobacter capsulatus
    • Drepper, T., S. Gross, A. F. Yakunin, P. C. Hallenbeck, B. Masepohl, and W. Klipp. 2003. Role of GlnB and GlnK in ammonium control of both nitrogenase systems in the phototrophic bacterium Rhodobacter capsulatus. Microbiology 149:2203-2212.
    • (2003) Microbiology , vol.149 , pp. 2203-2212
    • Drepper, T.1    Gross, S.2    Yakunin, A.F.3    Hallenbeck, P.C.4    Masepohl, B.5    Klipp, W.6
  • 6
    • 11044237901 scopus 로고    scopus 로고
    • Hydroxynitrile lyases: Biological sources and application as biocatalysts
    • Fechter, M. H., and H. Griengl. 2004. Hydroxynitrile lyases: biological sources and application as biocatalysts. Food Technol. Biotechnol. 42:287-294.
    • (2004) Food Technol. Biotechnol. , vol.42 , pp. 287-294
    • Fechter, M.H.1    Griengl, H.2
  • 7
    • 0000527903 scopus 로고
    • Replication of an origin-containing derivative of plasmid RK2 dependent on a plasmid function provided in trans
    • Figurski, D. H., and D. R. Helinski. 1979. Replication of an origin-containing derivative of plasmid RK2 dependent on a plasmid function provided in trans. Proc. Natl. Acad. Sci. USA 76:1648-1652.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 1648-1652
    • Figurski, D.H.1    Helinski, D.R.2
  • 8
    • 0034700263 scopus 로고    scopus 로고
    • Probing the role of the C-terminus of Bacillus subtilis chorismate mutase by a novel random protein-termination strategy
    • Gamper, M., D. Hilvert, and P. Kast. 2000. Probing the role of the C-terminus of Bacillus subtilis chorismate mutase by a novel random protein-termination strategy. Biochemistry 39:14087-14094.
    • (2000) Biochemistry , vol.39 , pp. 14087-14094
    • Gamper, M.1    Hilvert, D.2    Kast, P.3
  • 10
    • 0020959710 scopus 로고
    • Studies on transformation of Escherichia coli with plasmids
    • Hanahan, D. 1983. Studies on transformation of Escherichia coli with plasmids. J. Mol. Biol. 166:557-580.
    • (1983) J. Mol. Biol. , vol.166 , pp. 557-580
    • Hanahan, D.1
  • 11
    • 0029795374 scopus 로고    scopus 로고
    • The β-ketoadipate pathway and the biology of self-identity
    • Harwood, C. S., and R. E. Parales. 1996. The β-ketoadipate pathway and the biology of self-identity. Annu. Rev. Microbiol. 50:553-590.
    • (1996) Annu. Rev. Microbiol. , vol.50 , pp. 553-590
    • Harwood, C.S.1    Parales, R.E.2
  • 12
    • 0032516465 scopus 로고    scopus 로고
    • The crystal structure of benzoylformate decarboxylase at 1.6 Å resolution: Diversity of catalytic residues in thiamin diphosphate-dependent enzymes
    • Hasson, M. S., A. Muscate, M. J. McLeish, L. S. Polovnikova, J. A. Gerlt, G. L. Kenyon, G. A. Petsko, and D. Ringe. 1998. The crystal structure of benzoylformate decarboxylase at 1.6 Å resolution: diversity of catalytic residues in thiamin diphosphate-dependent enzymes. Biochemistry 37:9918-9930.
    • (1998) Biochemistry , vol.37 , pp. 9918-9930
    • Hasson, M.S.1    Muscate, A.2    McLeish, M.J.3    Polovnikova, L.S.4    Gerlt, J.A.5    Kenyon, G.L.6    Petsko, G.A.7    Ringe, D.8
  • 14
    • 0013888121 scopus 로고
    • Synthesis of the enzymes of the mandelate pathway by Pseudomonas putida. III. Isolation and properties of constitutive mutants
    • Hegeman, G. D. 1966. Synthesis of the enzymes of the mandelate pathway by Pseudomonas putida. III. Isolation and properties of constitutive mutants. J. Bacteriol. 91:1161-1167.
    • (1966) J. Bacteriol. , vol.91 , pp. 1161-1167
    • Hegeman, G.D.1
  • 15
    • 0013892853 scopus 로고
    • Synthesis of the enzymes of the mandelate pathway by Pseudomonas putida. I. Synthesis of enzymes by the wild type
    • Hegeman, G. D. 1966. Synthesis of the enzymes of the mandelate pathway by Pseudomonas putida. I. Synthesis of enzymes by the wild type. J. Bacteriol. 91:1140-1154.
    • (1966) J. Bacteriol. , vol.91 , pp. 1140-1154
    • Hegeman, G.D.1
  • 16
    • 0013892193 scopus 로고
    • Synthesis of the enzymes of the mandelate pathway by Pseudomonas putida. II. Isolation and properties of blocked mutants
    • Hegeman, G. D. 1966. Synthesis of the enzymes of the mandelate pathway by Pseudomonas putida. II. Isolation and properties of blocked mutants. J. Bacteriol. 91:1155-1160.
    • (1966) J. Bacteriol. , vol.91 , pp. 1155-1160
    • Hegeman, G.D.1
  • 19
    • 3543088511 scopus 로고    scopus 로고
    • Protein technologies and commercial enzymes: White is the hype-biocatalysts on the move
    • Jaeger, K. E. 2004. Protein technologies and commercial enzymes: white is the hype-biocatalysts on the move. Curr. Opin. Biotechnol. 15:269-271.
    • (2004) Curr. Opin. Biotechnol. , vol.15 , pp. 269-271
    • Jaeger, K.E.1
  • 20
    • 0028118547 scopus 로고
    • Biosynthetic pathway for veratryl alcohol in the ligninolytic fungus Phanerochaete chrysosporium
    • Jensen, K. A., K. M. Evans, T. K. Kirk, and K. E. Hammel. 1994. Biosynthetic pathway for veratryl alcohol in the ligninolytic fungus Phanerochaete chrysosporium. Appl. Environ. Microbiol. 60:709-714.
    • (1994) Appl. Environ. Microbiol. , vol.60 , pp. 709-714
    • Jensen, K.A.1    Evans, K.M.2    Kirk, T.K.3    Hammel, K.E.4
  • 21
    • 0842345383 scopus 로고    scopus 로고
    • Polaromonas naphthalenivorans sp. nov., a naphthalene-degrading bacterium from naphthalene-contaminated sediment
    • Jeon, C. O., W. Park, W. C. Ghiorse, and E. L. Madsen. 2004. Polaromonas naphthalenivorans sp. nov., a naphthalene-degrading bacterium from naphthalene-contaminated sediment. Int. J. Syst. Evol. Microbiol. 54:93-97.
    • (2004) Int. J. Syst. Evol. Microbiol. , vol.54 , pp. 93-97
    • Jeon, C.O.1    Park, W.2    Ghiorse, W.C.3    Madsen, E.L.4
  • 22
    • 0036933805 scopus 로고    scopus 로고
    • Genomic analysis of the aromatic catabolic pathways from Pseudomonas putida KT2440
    • Jimenez, J. I., B. Minambres, J. L. Garcia, and E. Diaz. 2002. Genomic analysis of the aromatic catabolic pathways from Pseudomonas putida KT2440. Environ. Microbiol. 4:824-841.
    • (2002) Environ. Microbiol. , vol.4 , pp. 824-841
    • Jimenez, J.I.1    Minambres, B.2    Garcia, J.L.3    Diaz, E.4
  • 23
    • 33744810604 scopus 로고    scopus 로고
    • Select the best: Novel biocatalysts for industrial applications
    • Konarzycka-Bessler, M., and K. E. Jaeger. 2006. Select the best: novel biocatalysts for industrial applications. Trends Biotechnol. 24:248-250.
    • (2006) Trends Biotechnol. , vol.24 , pp. 248-250
    • Konarzycka-Bessler, M.1    Jaeger, K.E.2
  • 24
    • 0028793123 scopus 로고
    • Four new derivatives of the broad-host-range cloning vector pBBR1MCS, carrying different antibiotic-resistance cassettes
    • Kovach, M. E., P. H. Elzer, D. S. Hill, G. T. Robertson, M. A. Farris, R. M. Roop II, and K. M. Peterson. 1995. Four new derivatives of the broad-host-range cloning vector pBBR1MCS, carrying different antibiotic-resistance cassettes. Gene 166:175-176.
    • (1995) Gene , vol.166 , pp. 175-176
    • Kovach, M.E.1    Elzer, P.H.2    Hill, D.S.3    Robertson, G.T.4    Farris, M.A.5    Roop II, R.M.6    Peterson, K.M.7
  • 26
    • 0034087468 scopus 로고    scopus 로고
    • Novel scheme for biosynthesis of aryl metabolites from L-phenylalanine in the fungus Bjerkandera adusta
    • Lapadatescu, C., C. Ginies, J. L. Le Quere, and P. Bonnarme. 2000. Novel scheme for biosynthesis of aryl metabolites from L-phenylalanine in the fungus Bjerkandera adusta. Appl. Environ. Microbiol. 66:1517-1522.
    • (2000) Appl. Environ. Microbiol. , vol.66 , pp. 1517-1522
    • Lapadatescu, C.1    Ginies, C.2    Le Quere, J.L.3    Bonnarme, P.4
  • 27
    • 0036656222 scopus 로고    scopus 로고
    • Improving the carboligase activity of benzoylformate decarboxylase from Pseudomonas putida by a combination of directed evolution and site-directed mutagenesis
    • Lingen, B., J. Grötzinger, D. Kolter, M. R. Kula, and M. Pohl. 2002. Improving the carboligase activity of benzoylformate decarboxylase from Pseudomonas putida by a combination of directed evolution and site-directed mutagenesis. Protein Eng. 15:585-593.
    • (2002) Protein Eng. , vol.15 , pp. 585-593
    • Lingen, B.1    Grötzinger, J.2    Kolter, D.3    Kula, M.R.4    Pohl, M.5
  • 28
    • 0041977179 scopus 로고    scopus 로고
    • Alteration of the substrate specificity of benzoylformate decarboxylase from Pseudomonas putida by directed evolution
    • Lingen, B., D. Kolter-Jung, P. Duenkelmann, R. Feldmann, J. Grötzinger, M. Pohl, and M. Müller. 2003. Alteration of the substrate specificity of benzoylformate decarboxylase from Pseudomonas putida by directed evolution. Chembiochemistry 4:721-726.
    • (2003) Chembiochemistry , vol.4 , pp. 721-726
    • Lingen, B.1    Kolter-Jung, D.2    Duenkelmann, P.3    Feldmann, R.4    Grötzinger, J.5    Pohl, M.6    Müller, M.7
  • 29
    • 0032549781 scopus 로고    scopus 로고
    • Redesigning enzyme topology by directed evolution
    • MacBeath, G., P. Kast, and D. Hilvert. 1998. Redesigning enzyme topology by directed evolution. Science 279:1958-1961.
    • (1998) Science , vol.279 , pp. 1958-1961
    • MacBeath, G.1    Kast, P.2    Hilvert, D.3
  • 30
    • 33644956913 scopus 로고    scopus 로고
    • Surveying biotransformations with a la carte genetic traps: Translating dehydrochlorination of lindane (gamma-hexachlorocyclohexane) into lacZ-based phenotypes
    • Mohn, W. W., J. Garmendia, T. C. Galvao, and V. de Lorenzo. 2006. Surveying biotransformations with a la carte genetic traps: translating dehydrochlorination of lindane (gamma-hexachlorocyclohexane) into lacZ-based phenotypes. Environ. Microbiol. 8:546-555.
    • (2006) Environ. Microbiol. , vol.8 , pp. 546-555
    • Mohn, W.W.1    Garmendia, J.2    Galvao, T.C.3    De Lorenzo, V.4
  • 32
    • 0034050548 scopus 로고    scopus 로고
    • Overexpression of trigger factor prevents aggregation of recombinant proteins in Escherichia coli
    • Nishihara, K., M. Kanemori, H. Yanagi, and T. Yura. 2000. Overexpression of trigger factor prevents aggregation of recombinant proteins in Escherichia coli. Appl. Environ. Microbiol. 66:884-889.
    • (2000) Appl. Environ. Microbiol. , vol.66 , pp. 884-889
    • Nishihara, K.1    Kanemori, M.2    Yanagi, H.3    Yura, T.4
  • 33
    • 0345310070 scopus 로고    scopus 로고
    • Engineering of quasi-natural Pseudomonas putida strains for toluene metabolism through an ortho-cleavage degradation pathway
    • Panke, S., J. M. Sanchez-Romero, and V. de Lorenzo. 1998. Engineering of quasi-natural Pseudomonas putida strains for toluene metabolism through an ortho-cleavage degradation pathway. Appl. Environ. Microbiol. 64:748-751.
    • (1998) Appl. Environ. Microbiol. , vol.64 , pp. 748-751
    • Panke, S.1    Sanchez-Romero, J.M.2    De Lorenzo, V.3
  • 34
    • 0042628455 scopus 로고    scopus 로고
    • Thiamin-diphosphate-dependent enzymes: New aspects of asymmetric C-C bond formation
    • Pohl, M., B. Lingen, and M. Müller. 2002. Thiamin-diphosphate- dependent enzymes: new aspects of asymmetric C-C bond formation. Chem. Eur. J. 8:5288-5295.
    • (2002) Chem. Eur. J. , vol.8 , pp. 5288-5295
    • Pohl, M.1    Lingen, B.2    Müller, M.3
  • 40
    • 6944229634 scopus 로고    scopus 로고
    • Creation and discovery of ligand-receptor pairs for transcriptional control with small molecules
    • Schwimmer, L. J., P. Rohatgi, B. Azizi, K. L. Seley, and D. F. Doyle. 2004. Creation and discovery of ligand-receptor pairs for transcriptional control with small molecules. Proc. Natl. Acad. Sci. USA 101:14707-14712.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 14707-14712
    • Schwimmer, L.J.1    Rohatgi, P.2    Azizi, B.3    Seley, K.L.4    Doyle, D.F.5
  • 41
    • 25844473249 scopus 로고    scopus 로고
    • Exchanging the substrate specificities of pyruvate decarboxylase from Zymomonas mobilis and benzoylformate decarboxylase from Pseudomonas putida
    • Siegert, P., M. J. McLeish, M. Baumann, H. Iding, M. M. Kneen, G. L. Kenyon, and M. Pohl. 2005. Exchanging the substrate specificities of pyruvate decarboxylase from Zymomonas mobilis and benzoylformate decarboxylase from Pseudomonas putida. Protein Eng. Des. Sel. 18:345-357.
    • (2005) Protein Eng. Des. Sel. , vol.18 , pp. 345-357
    • Siegert, P.1    McLeish, M.J.2    Baumann, M.3    Iding, H.4    Kneen, M.M.5    Kenyon, G.L.6    Pohl, M.7
  • 42
    • 0021027842 scopus 로고
    • A broad host range mobilization system for in vivo genetic-engineering- transposon mutagenesis in gram-negative bacteria
    • Simon, R., U. Priefer, and A. Pühler. 1983. A broad host range mobilization system for in vivo genetic-engineering-transposon mutagenesis in gram-negative bacteria. Biotechnology 1:784-791.
    • (1983) Biotechnology , vol.1 , pp. 784-791
    • Simon, R.1    Priefer, U.2    Pühler, A.3
  • 43
    • 9844232795 scopus 로고
    • Acetic acid production from ethanol by fluorescent pseudomonads
    • Stanier, R. Y. 1947. Acetic acid production from ethanol by fluorescent pseudomonads. J. Bacteriol. 54:191-194.
    • (1947) J. Bacteriol. , vol.54 , pp. 191-194
    • Stanier, R.Y.1
  • 44
    • 84984532077 scopus 로고
    • Simultaneous adaptation: A new technique for the study of metabolic pathways
    • Stanier, R. Y. 1947. Simultaneous adaptation: a new technique for the study of metabolic pathways. J. Bacteriol. 54:339-348.
    • (1947) J. Bacteriol. , vol.54 , pp. 339-348
    • Stanier, R.Y.1
  • 46
    • 0026279733 scopus 로고
    • Use of bacteriophage T7 lysozyme to improve an inducible T7 expression system
    • Studier, F. W. 1991. Use of bacteriophage T7 lysozyme to improve an inducible T7 expression system. J. Mol. Biol. 219:37-47.
    • (1991) J. Mol. Biol. , vol.219 , pp. 37-47
    • Studier, F.W.1
  • 47
    • 0023042283 scopus 로고
    • Use of bacteriophage T7 RNA polymerase to direct selective high level expression of cloned genes
    • Studier, F. W., and B. A. Moffatt. 1986. Use of bacteriophage T7 RNA polymerase to direct selective high level expression of cloned genes. J. Mol. Biol. 189:113-130.
    • (1986) J. Mol. Biol. , vol.189 , pp. 113-130
    • Studier, F.W.1    Moffatt, B.A.2
  • 48
    • 0025013451 scopus 로고
    • Mandelate pathway of Pseudomonas putida: Sequence relationships involving mandelate racemase, (S)-mandelate dehydrogenase, and benzoylformate decarboxylase and expression of benzoylformate decarboxylase in Escherichia coli
    • Tsou, A. Y., S. C. Ransom, J. A. Gerlt, D. D. Buechter, P. C. Babbitt, and G. L. Kenyon. 1990. Mandelate pathway of Pseudomonas putida: sequence relationships involving mandelate racemase, (S)-mandelate dehydrogenase, and benzoylformate decarboxylase and expression of benzoylformate decarboxylase in Escherichia coli. Biochemistry 29:9856-9862.
    • (1990) Biochemistry , vol.29 , pp. 9856-9862
    • Tsou, A.Y.1    Ransom, S.C.2    Gerlt, J.A.3    Buechter, D.D.4    Babbitt, P.C.5    Kenyon, G.L.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.