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Volumn 77, Issue 24, 2011, Pages 8754-8764

A novel hydrolase identified by genomic-proteomic analysis of phenylurea herbicide mineralization by Variovorax sp. strain SRS16

Author keywords

[No Author keywords available]

Indexed keywords

AMIDASE; BACTERIAL ISOLATES; BACTERIAL PATHWAY; CATABOLIC PATHWAY; CHLOROANILINE; CHLOROCATECHOL; DIOXYGENASES; DIVERGENT EVOLUTION; GENETIC ORGANIZATION; GENOME SEQUENCES; GRAM-NEGATIVE BACTERIA; GRAM-POSITIVE BACTERIUM; KREBS CYCLE; LINURON; MULTICOMPONENTS; ORTHO-CLEAVAGE PATHWAY; ORTHOLOGUES; PHENYLUREA HERBICIDES; PROTEOMIC ANALYSIS; TRANSCRIPTION ANALYSIS; UP-REGULATION;

EID: 83155182616     PISSN: 00992240     EISSN: 10985336     Source Type: Journal    
DOI: 10.1128/AEM.06162-11     Document Type: Article
Times cited : (65)

References (62)
  • 2
    • 23444461618 scopus 로고    scopus 로고
    • The periplasmic binding protein of a tripartite tricarboxylate transporter is involved in signal transduction
    • Antoine, R., et al. 2005. The periplasmic binding protein of a tripartite tricarboxylate transporter is involved in signal transduction. J. Mol. Biol. 351:799-809.
    • (2005) J. Mol. Biol. , vol.351 , pp. 799-809
    • Antoine, R.1
  • 3
    • 0037312887 scopus 로고    scopus 로고
    • Overrepresentation of a gene family encoding extracytoplasmic solute receptors in Bordetella
    • Antoine, R., et al. 2003. Overrepresentation of a gene family encoding extracytoplasmic solute receptors in Bordetella. J. Bacteriol. 185:1470-1474.
    • (2003) J. Bacteriol. , vol.185 , pp. 1470-1474
    • Antoine, R.1
  • 4
    • 0031733645 scopus 로고    scopus 로고
    • Purification, gene cloning, targeted knockout, overexpression, and biochemical characterization of the major pyrazinamidase from Mycobacterium smegmatis
    • Boshoff, H. I. M., and V. Mizrahi. 1998. Purification, gene cloning, targeted knockout, overexpression, and biochemical characterization of the major pyrazinamidase from Mycobacterium smegmatis. J. Bacteriol. 180:5809-5814.
    • (1998) J. Bacteriol. , vol.180 , pp. 5809-5814
    • Boshoff, H.I.M.1    Mizrahi, V.2
  • 5
    • 35948948729 scopus 로고    scopus 로고
    • Characterization of novel linuron-mineralizing bacterial consortia enriched from long-term linuron-treated agricultural soils
    • Breugelmans, P., P. J. D'Huys, R. De Mot, and D. Springael. 2007. Characterization of novel linuron-mineralizing bacterial consortia enriched from long-term linuron-treated agricultural soils. FEMS Microbiol. Ecol. 62:374-385.
    • (2007) FEMS Microbiol. Ecol. , vol.62 , pp. 374-385
    • Breugelmans, P.1    D'Huys, P.J.2    De Mot, R.3    Springael, D.4
  • 6
    • 77952953559 scopus 로고    scopus 로고
    • Proteomic study of linuron and 3,4-dichloroaniline degradation by Variovorax sp. WDL1: evidence for the involvement of an aniline dioxygenase-related multicomponent protein
    • Breugelmans, P., et al. 2010. Proteomic study of linuron and 3,4-dichloroaniline degradation by Variovorax sp. WDL1: evidence for the involvement of an aniline dioxygenase-related multicomponent protein. Res. Microbiol. 161: 208-218.
    • (2010) Res. Microbiol. , vol.161 , pp. 208-218
    • Breugelmans, P.1
  • 7
    • 33750283857 scopus 로고    scopus 로고
    • Burkholderia xenovorans LB400 harbors a multireplicon, 9.73-Mbp genome shaped for versatility
    • Chain, P. S. G., et al. 2006. Burkholderia xenovorans LB400 harbors a multireplicon, 9.73-Mbp genome shaped for versatility. Proc. Natl. Acad. Sci. U. S. A. 103:15280-15287.
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 15280-15287
    • Chain, P.S.G.1
  • 8
    • 67649491102 scopus 로고    scopus 로고
    • Regulatory interactions between quorum-sensing, auxin, cytokinin, and the Hrp regulon in relation to gall formation and epiphytic fitness of Pantoea agglomerans pv. gypsophilae
    • Chalupowicz, L., I. Barash, M. Panijel, G. Sessa, and S. Manulis-Sasson. 2009. Regulatory interactions between quorum-sensing, auxin, cytokinin, and the Hrp regulon in relation to gall formation and epiphytic fitness of Pantoea agglomerans pv. gypsophilae. Mol. Plant-Microbe Interact. 22:849-856.
    • (2009) Mol. Plant-Microbe Interact. , vol.22 , pp. 849-856
    • Chalupowicz, L.1    Barash, I.2    Panijel, M.3    Sessa, G.4    Manulis-Sasson, S.5
  • 10
    • 0037336952 scopus 로고    scopus 로고
    • Synergistic degradation of linuron by a bacterial consortium and isolation of a single linuron-degrading Variovorax strain
    • Dejonghe, W., et al. 2003. Synergistic degradation of linuron by a bacterial consortium and isolation of a single linuron-degrading Variovorax strain. Appl. Environ. Microbiol. 69:1532-1541.
    • (2003) Appl. Environ. Microbiol. , vol.69 , pp. 1532-1541
    • Dejonghe, W.1
  • 11
    • 83155189304 scopus 로고    scopus 로고
    • Biomatters, Ltd., Auckland, New Zealand
    • Drummond, A., et al. 2011. Geneious v5.4.4. Biomatters, Ltd., Auckland, New Zealand.
    • (2011) Geneious v5.4.4
    • Drummond, A.1
  • 12
    • 0015119225 scopus 로고
    • Degradation of linuron and some other herbicides and fungicides by a linuron-inducible enzyme obtained from Bacillus sphaericus
    • Engelhardt, G., P. Wallnofer, and R. Plapp. 1971. Degradation of linuron and some other herbicides and fungicides by a linuron-inducible enzyme obtained from Bacillus sphaericus. Appl. Microbiol. 22:284-288.
    • (1971) Appl. Microbiol. , vol.22 , pp. 284-288
    • Engelhardt, G.1    Wallnofer, P.2    Plapp, R.3
  • 13
    • 0015910297 scopus 로고
    • Purification and properties of an aryl acylamidase of Bacillus sphaericus, catalyzing hydrolysis of various phenylamide herbicides and fungicides
    • Engelhardt, G., P. Wallnofer, and R. Plapp. 1973. Purification and properties of an aryl acylamidase of Bacillus sphaericus, catalyzing hydrolysis of various phenylamide herbicides and fungicides. Appl. Microbiol. 26:709-718.
    • (1973) Appl. Microbiol. , vol.26 , pp. 709-718
    • Engelhardt, G.1    Wallnofer, P.2    Plapp, R.3
  • 14
    • 0023374169 scopus 로고
    • Organization and nucleotidesequence determination of a gene cluster involved in 3-chlorocatechol degradation
    • Frantz, B., and A. M. Chakrabarty. 1987. Organization and nucleotidesequence determination of a gene cluster involved in 3-chlorocatechol degradation. Proc. Natl. Acad. Sci. U. S. A. 84:4460-4464.
    • (1987) Proc. Natl. Acad. Sci. U. S. A. , vol.84 , pp. 4460-4464
    • Frantz, B.1    Chakrabarty, A.M.2
  • 15
    • 74149094499 scopus 로고    scopus 로고
    • A new aryl acylamidase from Rhodococcus sp. strain Oct1 acting on omega-lactams: its characterization and gene expression in Escherichia coli
    • Fukuta, Y., S. Koizumi, H. Komeda, and Y. Asano. 2010. A new aryl acylamidase from Rhodococcus sp. strain Oct1 acting on omega-lactams: its characterization and gene expression in Escherichia coli. Enzyme Microb. Technol. 46:237-245.
    • (2010) Enzyme Microb. Technol. , vol.46 , pp. 237-245
    • Fukuta, Y.1    Koizumi, S.2    Komeda, H.3    Asano, Y.4
  • 16
    • 67650152204 scopus 로고    scopus 로고
    • Functional analysis of a putative regulatory gene, tadR, involved in aniline degradation in Delftia tsuruhatensis AD9
    • Geng, L. Z., et al. 2009. Functional analysis of a putative regulatory gene, tadR, involved in aniline degradation in Delftia tsuruhatensis AD9. Arch. Microbiol. 191:603-614.
    • (2009) Arch. Microbiol. , vol.191 , pp. 603-614
    • Geng, L.Z.1
  • 17
    • 2942724459 scopus 로고    scopus 로고
    • Mandelamide hydrolase from Pseudomonas putida: characterization of a new member of the amidase signature family
    • Gopalakrishna, K. N., et al. 2004. Mandelamide hydrolase from Pseudomonas putida: characterization of a new member of the amidase signature family. Biochemistry 43:7725-7735.
    • (2004) Biochemistry , vol.43 , pp. 7725-7735
    • Gopalakrishna, K.N.1
  • 18
    • 54949121792 scopus 로고    scopus 로고
    • The missing link: Bordetella petrii is endowed with both the metabolic versatility of environmental bacteria and virulence traits of pathogenic Bordetellae
    • Gross, R., et al. 2008. The missing link: Bordetella petrii is endowed with both the metabolic versatility of environmental bacteria and virulence traits of pathogenic Bordetellae. BMC Genomics 9:449.
    • (2008) BMC Genomics , vol.9 , pp. 449
    • Gross, R.1
  • 19
    • 0242578620 scopus 로고    scopus 로고
    • A simple, fast, and accurate algorithm to estimate large phylogenies by maximum likelihood
    • Guindon, S., and O. Gascuel. 2003. A simple, fast, and accurate algorithm to estimate large phylogenies by maximum likelihood. Syst. Biol. 52:696-704.
    • (2003) Syst. Biol. , vol.52 , pp. 696-704
    • Guindon, S.1    Gascuel, O.2
  • 20
    • 79951606290 scopus 로고    scopus 로고
    • Complete genome sequence of the metabolically versatile plant growth-promoting endophyte Variovorax paradoxus S110
    • Han, J. I., et al. 2011. Complete genome sequence of the metabolically versatile plant growth-promoting endophyte Variovorax paradoxus S110. J. Bacteriol. 193:1183-1190.
    • (2011) J. Bacteriol. , vol.193 , pp. 1183-1190
    • Han, J.I.1
  • 21
    • 0036934790 scopus 로고    scopus 로고
    • Induction characteristics of reductive dehalogenation in the ortho-halophenol-respiring bacterium, Anaeromyxobacter dehalogenans
    • He, Q., and R. A. Sanford. 2002. Induction characteristics of reductive dehalogenation in the ortho-halophenol-respiring bacterium, Anaeromyxobacter dehalogenans. Biodegradation 13:307-316.
    • (2002) Biodegradation , vol.13 , pp. 307-316
    • He, Q.1    Sanford, R.A.2
  • 22
    • 28644452655 scopus 로고    scopus 로고
    • Purification, characterization, gene cloning and nucleotide sequencing of D-stereospecific amino acid amidase from soil bacterium: Delftia acidovorans
    • Hongpattarakere, T., H. Komeda, and Y. Asano. 2005. Purification, characterization, gene cloning and nucleotide sequencing of D-stereospecific amino acid amidase from soil bacterium: Delftia acidovorans. J. Ind. Microbiol. Biotechnol. 32:567-576.
    • (2005) J. Ind. Microbiol. Biotechnol. , vol.32 , pp. 567-576
    • Hongpattarakere, T.1    Komeda, H.2    Asano, Y.3
  • 23
    • 61449205250 scopus 로고    scopus 로고
    • Characterization of the phenylurea hydrolases A and B: founding members of a novel amidohydrolase subgroup
    • Khurana, J. L., et al. 2009. Characterization of the phenylurea hydrolases A and B: founding members of a novel amidohydrolase subgroup. Biochem. J. 418:431-441.
    • (2009) Biochem. J. , vol.418 , pp. 431-441
    • Khurana, J.L.1
  • 24
    • 78349260170 scopus 로고    scopus 로고
    • Molecular characterization of a novel bacterial aryl acylamidase belonging to the amidase signature enzyme family
    • Ko, H. J., et al. 2010. Molecular characterization of a novel bacterial aryl acylamidase belonging to the amidase signature enzyme family. Mol. Cells 29:485-492.
    • (2010) Mol. Cells , vol.29 , pp. 485-492
    • Ko, H.J.1
  • 25
    • 12544255173 scopus 로고    scopus 로고
    • Identification and characterization of a novel D-amidase gene from Variovorax paradoxus and its expression in Escherichia coli
    • Krieg, L., H. Slusarczyk, S. Verseck, and M. R. Kula. 2005. Identification and characterization of a novel D-amidase gene from Variovorax paradoxus and its expression in Escherichia coli. Appl. Microbiol. Biotechnol. 66:542-550.
    • (2005) Appl. Microbiol. Biotechnol. , vol.66 , pp. 542-550
    • Krieg, L.1    Slusarczyk, H.2    Verseck, S.3    Kula, M.R.4
  • 26
    • 77958473926 scopus 로고    scopus 로고
    • A new acylamidase from Rhodococcus erythropolis TA37 can hydrolyze N-substituted amides
    • Lavrov, K. V., I. A. Zalunin, E. K. Kotlova, and A. S. Yanenko. 2010. A new acylamidase from Rhodococcus erythropolis TA37 can hydrolyze N-substituted amides. Biochemistry (Moscow) 75:1006-1013.
    • (2010) Biochemistry (Moscow) , vol.75 , pp. 1006-1013
    • Lavrov, K.V.1    Zalunin, I.A.2    Kotlova, E.K.3    Yanenko, A.S.4
  • 27
    • 77953846853 scopus 로고    scopus 로고
    • Differential proteomic analysis using isotope-coded protein-labeling strategies: comparison, improvements, and application to simulated microgravity effect on Cupriavidus metallidurans CH34
    • Leroy, B., et al. 2010. Differential proteomic analysis using isotope-coded protein-labeling strategies: comparison, improvements, and application to simulated microgravity effect on Cupriavidus metallidurans CH34. Proteomics 10:2281-2291.
    • (2010) Proteomics , vol.10 , pp. 2281-2291
    • Leroy, B.1
  • 28
    • 0025747960 scopus 로고
    • Purification, cloning, and primary structure of a new enantiomer-selective amidase from a Rhodococcus strain: structural evidence for a conserved genetic coupling with nitrile hydratase
    • Mayaux, J. F., et al. 1991. Purification, cloning, and primary structure of a new enantiomer-selective amidase from a Rhodococcus strain: structural evidence for a conserved genetic coupling with nitrile hydratase. J. Bacteriol. 173:6694-6704.
    • (1991) J. Bacteriol. , vol.173 , pp. 6694-6704
    • Mayaux, J.F.1
  • 30
    • 0036253171 scopus 로고    scopus 로고
    • Gene cloning, overexpression, and biochemical characterization of the peptide amidase from Stenotrophomonas maltophilia
    • Neumann, S., and M. R. Kula. 2002. Gene cloning, overexpression, and biochemical characterization of the peptide amidase from Stenotrophomonas maltophilia. Appl. Microbiol. Biotechnol. 58:772-780.
    • (2002) Appl. Microbiol. Biotechnol. , vol.58 , pp. 772-780
    • Neumann, S.1    Kula, M.R.2
  • 31
    • 0141608699 scopus 로고    scopus 로고
    • Microbial genes and enzymes in the degradation of chlorinated compounds
    • Ogawa, N., K. Miyashita, and A. M. Chakrabarty. 2003. Microbial genes and enzymes in the degradation of chlorinated compounds. Chem. Rec. 3:158-171.
    • (2003) Chem. Rec. , vol.3 , pp. 158-171
    • Ogawa, N.1    Miyashita, K.2    Chakrabarty, A.M.3
  • 32
    • 71649107994 scopus 로고    scopus 로고
    • Structure and characterization of amidase from Rhodococcus sp. N-771: insight into the molecular mechanism of substrate recognition
    • Ohtaki, A., et al. 2010. Structure and characterization of amidase from Rhodococcus sp. N-771: insight into the molecular mechanism of substrate recognition. Biochim. Biophys. Acta Prot. Proteom. 1804:184-192.
    • (2010) Biochim. Biophys. Acta Prot. Proteom. , vol.1804 , pp. 184-192
    • Ohtaki, A.1
  • 33
    • 0027154591 scopus 로고
    • Positive regulation of phenolic catabolism in Agrobacterium tumefaciens by the pcaQ gene in response to beta-carboxy-cis,cis-muconate
    • Parke, D. 1993. Positive regulation of phenolic catabolism in Agrobacterium tumefaciens by the pcaQ gene in response to beta-carboxy-cis,cis-muconate. J. Bacteriol. 175:3529-3535.
    • (1993) J. Bacteriol. , vol.175 , pp. 3529-3535
    • Parke, D.1
  • 34
    • 33947472245 scopus 로고
    • Separation and colorimetric determination of monuron and diuron residues
    • Pease, H. L. 1962. Separation and colorimetric determination of monuron and diuron residues. J. Agric. Food Chem. 10:279-281.
    • (1962) J. Agric. Food Chem. , vol.10 , pp. 279-281
    • Pease, H.L.1
  • 35
    • 33749863920 scopus 로고    scopus 로고
    • Genome sequence of the bioplastic-producing "Knallgas" bacterium Ralstonia eutropha H16
    • Pohlmann, A., et al. 2006. Genome sequence of the bioplastic-producing "Knallgas" bacterium Ralstonia eutropha H16. Nat. Biotechnol. 24:1257-1262.
    • (2006) Nat. Biotechnol. , vol.24 , pp. 1257-1262
    • Pohlmann, A.1
  • 36
    • 0035148730 scopus 로고    scopus 로고
    • Chlorocatechols substituted at positions 4 and 5 are substrates of the broad-spectrum chlorocatechol 1,2-dioxygenase of Pseudomonas chlororaphis RW71
    • Potrawfke, T., J. Armengaud, and R. M. Wittich. 2001. Chlorocatechols substituted at positions 4 and 5 are substrates of the broad-spectrum chlorocatechol 1,2-dioxygenase of Pseudomonas chlororaphis RW71. J. Bacteriol. 183:997-1011.
    • (2001) J. Bacteriol. , vol.183 , pp. 997-1011
    • Potrawfke, T.1    Armengaud, J.2    Wittich, R.M.3
  • 37
    • 0043122986 scopus 로고    scopus 로고
    • CODEHOP (COnsensus- DEgenerate hybrid oligonucleotide primer) PCR primer design
    • Rose, T. M., J. G. Henikoff, and S. Henikoff. 2003. CODEHOP (COnsensus- DEgenerate hybrid oligonucleotide primer) PCR primer design. Nucleic Acids Res. 31:3763-3766.
    • (2003) Nucleic Acids Res. , vol.31 , pp. 3763-3766
    • Rose, T.M.1    Henikoff, J.G.2    Henikoff, S.3
  • 39
    • 77954634063 scopus 로고    scopus 로고
    • Mineralization of the herbicide linuron by Variovorax sp. strain RA8 isolated from Japanese river sediment using an ecosystem model (microcosm)
    • Satsuma, K. 2010. Mineralization of the herbicide linuron by Variovorax sp. strain RA8 isolated from Japanese river sediment using an ecosystem model (microcosm). Pest Manag. Sci. 66:847-852.
    • (2010) Pest Manag. Sci. , vol.66 , pp. 847-852
    • Satsuma, K.1
  • 40
    • 55049083717 scopus 로고    scopus 로고
    • Involvement of a novel enzyme, MdpA, in methyl tert-butyl ether degradation in Methylibium petroleiphilum PM1
    • Schmidt, R., V. Battaglia, K. Scow, S. Kane, and K. R. Hristova. 2008. Involvement of a novel enzyme, MdpA, in methyl tert-butyl ether degradation in Methylibium petroleiphilum PM1. Appl. Environ. Microbiol. 74:6631-6638.
    • (2008) Appl. Environ. Microbiol. , vol.74 , pp. 6631-6638
    • Schmidt, R.1    Battaglia, V.2    Scow, K.3    Kane, S.4    Hristova, K.R.5
  • 41
    • 0016186256 scopus 로고
    • Regulation of naphtalene oxygenase in Pseudomonas
    • Shamsuzzaman, K. M., and E. A. Barnsley. 1974. Regulation of naphtalene oxygenase in Pseudomonas. J. Gen. Microbiol. 83:165-170.
    • (1974) J. Gen. Microbiol. , vol.83 , pp. 165-170
    • Shamsuzzaman, K.M.1    Barnsley, E.A.2
  • 42
    • 33646120110 scopus 로고    scopus 로고
    • Purification and characterization of TrzF: biuret hydrolysis by allophanate hydrolase supports growth
    • Shapir, N., G. Cheng, M. J. Sadowsky, and L. P. Wackett. 2006. Purification and characterization of TrzF: biuret hydrolysis by allophanate hydrolase supports growth. Appl. Environ. Microbiol. 72:2491-2495.
    • (2006) Appl. Environ. Microbiol. , vol.72 , pp. 2491-2495
    • Shapir, N.1    Cheng, G.2    Sadowsky, M.J.3    Wackett, L.P.4
  • 43
    • 18944379412 scopus 로고    scopus 로고
    • Purification and characterization of allophanate hydrolase (AtzF) from Pseudomonas sp. strain ADP
    • Shapir, N., M. J. Sadowsky, and L. P. Wackett. 2005. Purification and characterization of allophanate hydrolase (AtzF) from Pseudomonas sp. strain ADP. J. Bacteriol. 187:3731-3738.
    • (2005) J. Bacteriol. , vol.187 , pp. 3731-3738
    • Shapir, N.1    Sadowsky, M.J.2    Wackett, L.P.3
  • 44
    • 65549153949 scopus 로고    scopus 로고
    • Pathway and evolutionary implications of diphenylamine biodegradation by Burkholderia sp. strain JS667
    • Shin, K. A., and J. C. Spain. 2009. Pathway and evolutionary implications of diphenylamine biodegradation by Burkholderia sp. strain JS667. Appl. Environ. Microbiol. 75:2694-2704.
    • (2009) Appl. Environ. Microbiol. , vol.75 , pp. 2694-2704
    • Shin, K.A.1    Spain, J.C.2
  • 45
    • 0043092112 scopus 로고    scopus 로고
    • Characterization of a novel Ser-cisSer-Lys catalytic triad in comparison with the classical Ser-His-Asp triad
    • Shin, S., et al. 2003. Characterization of a novel Ser-cisSer-Lys catalytic triad in comparison with the classical Ser-His-Asp triad. J. Biol. Chem. 278:24937-24943.
    • (2003) J. Biol. Chem. , vol.278 , pp. 24937-24943
    • Shin, S.1
  • 46
    • 22144463550 scopus 로고    scopus 로고
    • Elucidating the key member of a linuronmineralizing bacterial community by PCR and reverse transcription-PCR denaturing gradient gel electrophoresis 16S rRNA gene fingerprinting and cultivation
    • Sorensen, S. R., et al. 2005. Elucidating the key member of a linuronmineralizing bacterial community by PCR and reverse transcription-PCR denaturing gradient gel electrophoresis 16S rRNA gene fingerprinting and cultivation. Appl. Environ. Microbiol. 71:4144-4148.
    • (2005) Appl. Environ. Microbiol. , vol.71 , pp. 4144-4148
    • Sorensen, S.R.1
  • 47
    • 60349112649 scopus 로고    scopus 로고
    • Constitutive mineralization of low concentrations of the herbicide linuron by a Variovorax sp. strain
    • Sorensen, S. R., A. Simonsen, and J. Aamand. 2009. Constitutive mineralization of low concentrations of the herbicide linuron by a Variovorax sp. strain. FEMS Microbiol. Lett. 292:291-296.
    • (2009) FEMS Microbiol. Lett. , vol.292 , pp. 291-296
    • Sorensen, S.R.1    Simonsen, A.2    Aamand, J.3
  • 48
    • 13844253486 scopus 로고    scopus 로고
    • Two unusual chlorocatechol catabolic gene clusters in Sphingomonas sp. TFD44
    • Thiel, M., S. Kaschabek, J. Groning, M. Mau, and M. Schlomann. 2005. Two unusual chlorocatechol catabolic gene clusters in Sphingomonas sp. TFD44. Arch. Microbiol. 183:80-94.
    • (2005) Arch. Microbiol. , vol.183 , pp. 80-94
    • Thiel, M.1    Kaschabek, S.2    Groning, J.3    Mau, M.4    Schlomann, M.5
  • 49
    • 0038820052 scopus 로고    scopus 로고
    • The role of mobile genetic elements in bacterial adaptation to xenobiotic organic compounds
    • Top, E. M., and D. Springael. 2003. The role of mobile genetic elements in bacterial adaptation to xenobiotic organic compounds. Curr. Opin. Biotechnol. 14:262-269.
    • (2003) Curr. Opin. Biotechnol. , vol.14 , pp. 262-269
    • Top, E.M.1    Springael, D.2
  • 50
    • 3042826882 scopus 로고    scopus 로고
    • Genetic organization of the catabolic plasmid pJP4 from Ralstonia eutropha JMP134 (pJP4) reveals mechanisms of adaptation to chloroaromatic pollutants and evolution of specialized chloroaromatic degradation pathways
    • Trefault, N., et al. 2004. Genetic organization of the catabolic plasmid pJP4 from Ralstonia eutropha JMP134 (pJP4) reveals mechanisms of adaptation to chloroaromatic pollutants and evolution of specialized chloroaromatic degradation pathways. Environ. Microbiol. 6:655-668.
    • (2004) Environ. Microbiol. , vol.6 , pp. 655-668
    • Trefault, N.1
  • 51
    • 4544275675 scopus 로고    scopus 로고
    • Bacterial transcriptional regulators for degradation pathways of aromatic compounds
    • Tropel, D., and J. R. van der Meer. 2004. Bacterial transcriptional regulators for degradation pathways of aromatic compounds. Microbiol. Mol. Biol. Rev. 68:474-500.
    • (2004) Microbiol. Mol. Biol. Rev. , vol.68 , pp. 474-500
    • Tropel, D.1    van der Meer, J.R.2
  • 52
    • 0035349911 scopus 로고    scopus 로고
    • Degradation of substituted phenylurea herbicides by Arthrobacter globiformis strain D47 and characterization of a plasmid-associated hydrolase gene, puhA
    • Turnbull, G. A., M. Ousley, A. Walker, E. Shaw, and J. A. W. Morgan. 2001. Degradation of substituted phenylurea herbicides by Arthrobacter globiformis strain D47 and characterization of a plasmid-associated hydrolase gene, puhA. Appl. Environ. Microbiol. 67:2270-2275.
    • (2001) Appl. Environ. Microbiol. , vol.67 , pp. 2270-2275
    • Turnbull, G.A.1    Ousley, M.2    Walker, A.3    Shaw, E.4    Morgan, J.A.W.5
  • 53
    • 31644444476 scopus 로고    scopus 로고
    • MaGe: a microbial genome annotation system supported by synteny results
    • Vallenet, D., et al. 2006. MaGe: a microbial genome annotation system supported by synteny results. Nucleic Acids Res. 34:53-65.
    • (2006) Nucleic Acids Res. , vol.34 , pp. 53-65
    • Vallenet, D.1
  • 54
    • 0031028986 scopus 로고    scopus 로고
    • Evolution of novel metabolic pathways for the degradation of chloroaromatic compounds
    • Vandermeer, J. R. 1997. Evolution of novel metabolic pathways for the degradation of chloroaromatic compounds. Antonie Van Leeuwenhoek Int. J. Gen. Mol. Microbiol. 71:159-178.
    • (1997) Antonie Van Leeuwenhoek Int. J. Gen. Mol. Microbiol. , vol.71 , pp. 159-178
    • Vandermeer, J.R.1
  • 55
    • 0025806414 scopus 로고
    • Sequence analysis of the Pseudomonas sp. strain P51 tcb gene cluster, which encodes metabolism of chlorinated catechols: evidence for specialization of catechol 1,2-dioxygenases for chlorinated substrates
    • Vandermeer, J. R., R. I. L. Eggen, A. J. B. Zehnder, and W. M. Devos. 1991. Sequence analysis of the Pseudomonas sp. strain P51 tcb gene cluster, which encodes metabolism of chlorinated catechols: evidence for specialization of catechol 1,2-dioxygenases for chlorinated substrates. J. Bacteriol. 173:2425-2434.
    • (1991) J. Bacteriol. , vol.173 , pp. 2425-2434
    • Vandermeer, J.R.1    Eggen, R.I.L.2    Zehnder, A.J.B.3    Devos, W.M.4
  • 56
    • 0342844467 scopus 로고    scopus 로고
    • Analysis of the 2,4-dichlorophenoxyacetic acid-degradative plasmid pEST4011 of Achromobacter xylosoxidans subsp denitrificans strain EST4002
    • Vedler, E., V. Koiv, and A. Heinaru. 2000. Analysis of the 2,4-dichlorophenoxyacetic acid-degradative plasmid pEST4011 of Achromobacter xylosoxidans subsp denitrificans strain EST4002. Gene 255:281-288.
    • (2000) Gene , vol.255 , pp. 281-288
    • Vedler, E.1    Koiv, V.2    Heinaru, A.3
  • 57
    • 0022397667 scopus 로고
    • Nucleotide sequences of the Pseudomonas savastanoi indoleacetic acid genes show homology with Agrobacterium tumefaciens T-DNA
    • Yamada, T., C. J. Palm, B. Brooks, and T. Kosuge. 1985. Nucleotide sequences of the Pseudomonas savastanoi indoleacetic acid genes show homology with Agrobacterium tumefaciens T-DNA. Proc. Natl. Acad. Sci. U. S. A. 82:6522-6526.
    • (1985) Proc. Natl. Acad. Sci. U. S. A. , vol.82 , pp. 6522-6526
    • Yamada, T.1    Palm, C.J.2    Brooks, B.3    Kosuge, T.4
  • 58
    • 0030024321 scopus 로고    scopus 로고
    • Production of R-(-)-ketoprofen from an amide compound by Comamonas acidovorans KPO-2771-4
    • Yamamoto, K., et al. 1996. Production of R-(-)-ketoprofen from an amide compound by Comamonas acidovorans KPO-2771-4. Appl. Environ. Microbiol. 62:152-155.
    • (1996) Appl. Environ. Microbiol. , vol.62 , pp. 152-155
    • Yamamoto, K.1
  • 59
    • 74049115832 scopus 로고    scopus 로고
    • X-ray crystallographic analysis of the 6-aminohexanoate cyclic dimer hydrolase: catalytic mechanism and evolution of an enzyme responsible for nylon-6 by-product degradation
    • Yasuhira, K., et al. 2009. X-ray crystallographic analysis of the 6-aminohexanoate cyclic dimer hydrolase: catalytic mechanism and evolution of an enzyme responsible for nylon-6 by-product degradation. J. Biol. Chem. 285: 1239-1248.
    • (2009) J. Biol. Chem. , vol.285 , pp. 1239-1248
    • Yasuhira, K.1
  • 60
    • 58149109275 scopus 로고    scopus 로고
    • Proteomic analysis of outer membrane proteins from Acinetobacter baumannii DU202 in tetracycline stress condition
    • Yun, S. H., et al. 2008. Proteomic analysis of outer membrane proteins from Acinetobacter baumannii DU202 in tetracycline stress condition. J. Microbiol. 46:720-727.
    • (2008) J. Microbiol. , vol.46 , pp. 720-727
    • Yun, S.H.1
  • 61
    • 45149100613 scopus 로고    scopus 로고
    • A novel and complete gene cluster involved in the degradation of aniline by Delftia sp. AN3
    • Zhang, T., J. L. Zhang, S. J. Liu, and Z. P. Liu. 2008. A novel and complete gene cluster involved in the degradation of aniline by Delftia sp. AN3. J. Environ. Sci. China 20:717-724.
    • (2008) J. Environ. Sci. China , vol.20 , pp. 717-724
    • Zhang, T.1    Zhang, J.L.2    Liu, S.J.3    Liu, Z.P.4
  • 62
    • 79251480450 scopus 로고    scopus 로고
    • The R-R-type MYB-like transcription factor, At- MYBL, is involved in promoting leaf senescence and modulates an abiotic stress response in Arabidopsis
    • Zhang, X., et al. 2011. The R-R-type MYB-like transcription factor, At-MYBL, is involved in promoting leaf senescence and modulates an abiotic stress response in Arabidopsis. Plant Cell Physiol. 52:138-148.
    • (2011) Plant Cell Physiol. , vol.52 , pp. 138-148
    • Zhang, X.1


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