메뉴 건너뛰기




Volumn 72, Issue 3, 2006, Pages 1817-1824

Control of substrate specificity by active-site residues in nitrobenzene dioxygenase

Author keywords

[No Author keywords available]

Indexed keywords

ALCOHOLS; BENZENE; CARBON; CATALYSIS; DEGRADATION; HYDROGEN BONDS; MUTAGENESIS; OXIDATION; SUBSTRATES; TOLUENE;

EID: 33644958744     PISSN: 00992240     EISSN: None     Source Type: Journal    
DOI: 10.1128/AEM.72.3.1817-1824.2006     Document Type: Article
Times cited : (54)

References (47)
  • 2
    • 0035711112 scopus 로고    scopus 로고
    • Aromatic dioxygenases: Molecular biocatalysis and applications
    • Boyd, D. R., N. D. Sharma, and C. C. R. Allen. 2001. Aromatic dioxygenases: molecular biocatalysis and applications. Curr. Opin. Biotechnol. 12:564-573.
    • (2001) Curr. Opin. Biotechnol. , vol.12 , pp. 564-573
    • Boyd, D.R.1    Sharma, N.D.2    Allen, C.C.R.3
  • 3
    • 0031831881 scopus 로고    scopus 로고
    • The dioxygenase-catalysed formation of vicinal cis-diols
    • Boyd, D. R., and G. N. Sheldrake. 1998. The dioxygenase-catalysed formation of vicinal cis-diols. Nat. Prod. Rep. 15:309-324.
    • (1998) Nat. Prod. Rep. , vol.15 , pp. 309-324
    • Boyd, D.R.1    Sheldrake, G.N.2
  • 4
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 7
    • 0031967070 scopus 로고    scopus 로고
    • A gene cluster encoding steps in the conversion of naphthalene to gentisate in Pseudomonas sp. strain U2
    • Fuenmayor, S. L., M. Wild, A. L. Boyles, and P. A. Williams. 1998. A gene cluster encoding steps in the conversion of naphthalene to gentisate in Pseudomonas sp. strain U2. J. Bacteriol. 180:2522-2530.
    • (1998) J. Bacteriol. , vol.180 , pp. 2522-2530
    • Fuenmayor, S.L.1    Wild, M.2    Boyles, A.L.3    Williams, P.A.4
  • 8
    • 0028022845 scopus 로고
    • Biodegradation of 2-nitrotoluene by Pseudomonas sp. strain JS42
    • Haigler, B. E., W. H. Wallace, and J. C. Spain. 1994. Biodegradation of 2-nitrotoluene by Pseudomonas sp. strain JS42. Appl. Environ. Microbiol. 60:3466-3469.
    • (1994) Appl. Environ. Microbiol. , vol.60 , pp. 3466-3469
    • Haigler, B.E.1    Wallace, W.H.2    Spain, J.C.3
  • 9
    • 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
  • 10
    • 0001846314 scopus 로고    scopus 로고
    • Enzymatic dihydroxylation of aromatics in enantioselective synthesis: Expanding asymmetric methodology
    • Hudlicky, T., D. Gonzalez, and D. T. Gibson. 1999. Enzymatic dihydroxylation of aromatics in enantioselective synthesis: expanding asymmetric methodology. Aldrichim. Acta 32:35-62.
    • (1999) Aldrichim. Acta , vol.32 , pp. 35-62
    • Hudlicky, T.1    Gonzalez, D.2    Gibson, D.T.3
  • 12
    • 0014974950 scopus 로고
    • cis-1,2-dihydroxy-1,2-dihydronaphthalene: A bacterial metabolite from naphthalene
    • Jerina, D. M., J. W. Daly, A. M. Jeffrey, and D. T. Gibson. 1971. cis-1,2-Dihydroxy-1,2-dihydronaphthalene: a bacterial metabolite from naphthalene. Arch. Biochem. Biophys. 142:394-396.
    • (1971) Arch. Biochem. Biophys. , vol.142 , pp. 394-396
    • Jerina, D.M.1    Daly, J.W.2    Jeffrey, A.M.3    Gibson, D.T.4
  • 13
    • 0036064709 scopus 로고    scopus 로고
    • Origins of the 2,4-dinitrotoluene pathway
    • Johnson, G. R., R. K. Jain, and J. C. Spain. 2002. Origins of the 2,4-dinitrotoluene pathway. J. Bacteriol. 184:4219-4232.
    • (2002) J. Bacteriol. , vol.184 , pp. 4219-4232
    • Johnson, G.R.1    Jain, R.K.2    Spain, J.C.3
  • 15
    • 18244374438 scopus 로고    scopus 로고
    • Protein engineering of the archetypal nitroarene dioxygenase of Ralstonia sp. strain U2 for activity on aminonitrotoluenes and dinitrotoluenes through alpha-subunit residues leucine 225, phenylalanine 350, and glycine 407
    • Keenan, B. G., T. Leungsakul, B. F. Smets, M. A. Mori, D. E. Henderson, and T. K. Wood. 2005. Protein engineering of the archetypal nitroarene dioxygenase of Ralstonia sp. strain U2 for activity on aminonitrotoluenes and dinitrotoluenes through alpha-subunit residues leucine 225, phenylalanine 350, and glycine 407. J. Bacteriol. 187:3302-3310.
    • (2005) J. Bacteriol. , vol.187 , pp. 3302-3310
    • Keenan, B.G.1    Leungsakul, T.2    Smets, B.F.3    Mori, M.A.4    Henderson, D.E.5    Wood, T.K.6
  • 16
    • 2942530416 scopus 로고    scopus 로고
    • Saturation mutagenesis of Burkholderia cepacia R34 2,4-dinitrotoluene dioxygenase at DntAc valine 350 for synthesizing nitrohydroquinone, methylhydroquinone, and methoxyhydroquinone
    • Keenan, B. G., T. Leungsakul, B. F. Smets, and T. K. Wood. 2004. Saturation mutagenesis of Burkholderia cepacia R34 2,4-dinitrotoluene dioxygenase at DntAc valine 350 for synthesizing nitrohydroquinone, methylhydroquinone, and methoxyhydroquinone. Appl. Environ. Microbiol. 70:3222-3231.
    • (2004) Appl. Environ. Microbiol. , vol.70 , pp. 3222-3231
    • Keenan, B.G.1    Leungsakul, T.2    Smets, B.F.3    Wood, T.K.4
  • 17
    • 0018410446 scopus 로고
    • Metabolism of dibenzo[1,4]dioxan by a Pseudomonas species
    • Klecka, G. M., and D. T. Gibson. 1979. Metabolism of dibenzo[1,4]dioxan by a Pseudomonas species. Biochem. J. 180:639-645.
    • (1979) Biochem. J. , vol.180 , pp. 639-645
    • Klecka, G.M.1    Gibson, D.T.2
  • 18
    • 27444439187 scopus 로고    scopus 로고
    • Active site residues controlling substrate specificity in 2-nitrotoluene dioxygenase from Acidovorax sp. strain JS42
    • Lee, K.-S., J. V. Parales, R. Friemann, and R. E. Parales. 2005. Active site residues controlling substrate specificity in 2-nitrotoluene dioxygenase from Acidovorax sp. strain JS42. J. Ind. Microbiol. Biotechnol. 32:465-473.
    • (2005) J. Ind. Microbiol. Biotechnol. , vol.32 , pp. 465-473
    • Lee, K.-S.1    Parales, J.V.2    Friemann, R.3    Parales, R.E.4
  • 19
    • 0025258442 scopus 로고
    • A simple procedure for maximum yield of high-quality plasmid DNA
    • Lee, S.-Y., and S. Rasbeed. 1990. A simple procedure for maximum yield of high-quality plasmid DNA. BioTechniques 9:676-679.
    • (1990) BioTechniques , vol.9 , pp. 676-679
    • Lee, S.-Y.1    Rasbeed, S.2
  • 20
    • 0036158077 scopus 로고    scopus 로고
    • Molecular characterization and substrate specificity of nitrobenzene dioxygenase from Comamonas sp. strain JS765
    • Lessner, D. J., G. R. Johnson, R. E. Parales, J. C. Spain, and D. T. Gibson. 2002. Molecular characterization and substrate specificity of nitrobenzene dioxygenase from Comamonas sp. strain JS765. Appl. Environ. Microbiol. 68:634-641.
    • (2002) Appl. Environ. Microbiol. , vol.68 , pp. 634-641
    • Lessner, D.J.1    Johnson, G.R.2    Parales, R.E.3    Spain, J.C.4    Gibson, D.T.5
  • 21
    • 0038377410 scopus 로고    scopus 로고
    • Expression of nitroarene dioxygenase genes in Comamonas sp. strain JS765 and Acidovorax sp. strain JS42 is induced by multiple aromatic compounds
    • Lessner, D. J., R. E. Parales, S. Narayan, and D. T. Gibson. 2003. Expression of nitroarene dioxygenase genes in Comamonas sp. strain JS765 and Acidovorax sp. strain JS42 is induced by multiple aromatic compounds. J. Bacteriol. 185:3895-3904.
    • (2003) J. Bacteriol. , vol.185 , pp. 3895-3904
    • Lessner, D.J.1    Parales, R.E.2    Narayan, S.3    Gibson, D.T.4
  • 22
    • 28444458447 scopus 로고    scopus 로고
    • Saturation mutagenesis of 2,4-DNT dioxygenase of Burkholderia sp. strain DNT for enhanced dinitrotoluene degradation
    • Leungsakul, T., B. G. Keenan, H. Yin, B. F. Smets, and T. K. Wood. 2005. Saturation mutagenesis of 2,4-DNT dioxygenase of Burkholderia sp. strain DNT for enhanced dinitrotoluene degradation. Biotechnol. Bioeng. 92:416-420.
    • (2005) Biotechnol. Bioeng. , vol.92 , pp. 416-420
    • Leungsakul, T.1    Keenan, B.G.2    Yin, H.3    Smets, B.F.4    Wood, T.K.5
  • 23
    • 0034061462 scopus 로고    scopus 로고
    • Aerobic degradation of dinitrotoluenes and the pathway for bacterial degradation of 2,6-dinitrotoluene
    • Nishino, S. F., G. C. Paoli, and J. C. Spain. 2000. Aerobic degradation of dinitrotoluenes and the pathway for bacterial degradation of 2,6-dinitrotoluene. Appl. Environ. Microbiol. 66:2139-2147.
    • (2000) Appl. Environ. Microbiol. , vol.66 , pp. 2139-2147
    • Nishino, S.F.1    Paoli, G.C.2    Spain, J.C.3
  • 24
    • 0029070669 scopus 로고
    • Oxidative pathway for the biodegradation of nitrobenzene by Comamonas sp. strain JS765
    • Nishino, S. F., and J. C. Spain. 1995. Oxidative pathway for the biodegradation of nitrobenzene by Comamonas sp. strain JS765. Appl. Environ. Microbiol. 61:2308-2313.
    • (1995) Appl. Environ. Microbiol. , vol.61 , pp. 2308-2313
    • Nishino, S.F.1    Spain, J.C.2
  • 26
    • 0344499798 scopus 로고    scopus 로고
    • Cloning and sequencing of the genes encoding 2-nitrotoluene dioxygenase from Pseudomonas sp. JS42
    • Parales, J. V., A. Kumar, R. E. Parales, and D. T. Gibson. 1996. Cloning and sequencing of the genes encoding 2-nitrotoluene dioxygenase from Pseudomonas sp. JS42. Gene 181:57-61.
    • (1996) Gene , vol.181 , pp. 57-61
    • Parales, J.V.1    Kumar, A.2    Parales, R.E.3    Gibson, D.T.4
  • 27
    • 0031932850 scopus 로고    scopus 로고
    • Enzyme specificity of 2-nitrotoluene 2,3-dioxygenase from Pseudomonas sp. strain JS42 is determined by the C-terminal region of the α subunit of the oxygenase component
    • Parales, J. V., R. E. Parales, S. M. Resnick, and D. T. Gibson. 1998. Enzyme specificity of 2-nitrotoluene 2,3-dioxygenase from Pseudomonas sp. strain JS42 is determined by the C-terminal region of the α subunit of the oxygenase component. J. Bacteriol. 180:1194-1199.
    • (1998) J. Bacteriol. , vol.180 , pp. 1194-1199
    • Parales, J.V.1    Parales, R.E.2    Resnick, S.M.3    Gibson, D.T.4
  • 28
    • 0031958521 scopus 로고    scopus 로고
    • Substrate specificities of hybrid naphthalene and 2,4-dinitrotoluene dioxygenase enzyme systems
    • Parales, R. E., M. D. Emig, N. A. Lynch, and D. T. Gibson. 1998. Substrate specificities of hybrid naphthalene and 2,4-dinitrotoluene dioxygenase enzyme systems. J. Bacteriol. 180:2337-2344.
    • (1998) J. Bacteriol. , vol.180 , pp. 2337-2344
    • Parales, R.E.1    Emig, M.D.2    Lynch, N.A.3    Gibson, D.T.4
  • 30
    • 0034051818 scopus 로고    scopus 로고
    • Substrate specificity of naphthalene dioxygenase: Effect of specific amino acids at the active site of the enzyme
    • Parales, R. E., K. Lee, S. M. Resnick, H. Jiang, D. J. Lessner, and D. T. Gibson. 2000. Substrate specificity of naphthalene dioxygenase: effect of specific amino acids at the active site of the enzyme. J. Bacteriol. 182:1641-1649.
    • (2000) J. Bacteriol. , vol.182 , pp. 1641-1649
    • Parales, R.E.1    Lee, K.2    Resnick, S.M.3    Jiang, H.4    Lessner, D.J.5    Gibson, D.T.6
  • 31
    • 0033797753 scopus 로고    scopus 로고
    • Regioselectivity and enantioselectivity of naphthalene dioxygenase during arene cis-dihydroxylation: Control by phenylalanine 352 in the α subunit
    • Parales, R. E., S. M. Resnick, C. L. Yu, D. R. Boyd, N. D. Sharma, and D. T. Gibson. 2000. Regioselectivity and enantioselectivity of naphthalene dioxygenase during arene cis-dihydroxylation: control by phenylalanine 352 in the α subunit. J. Bacteriol. 182:5495-5504.
    • (2000) J. Bacteriol. , vol.182 , pp. 5495-5504
    • Parales, R.E.1    Resnick, S.M.2    Yu, C.L.3    Boyd, D.R.4    Sharma, N.D.5    Gibson, D.T.6
  • 32
    • 0038028659 scopus 로고    scopus 로고
    • Rational engineering of the regioselectivity of TecA tetrachlorobenzene dioxygenase for the transformation of chlorinated toluenes
    • Pollmann, K., V. Wray, H.-J. Hecht, and D. H. Pieper. 2003. Rational engineering of the regioselectivity of TecA tetrachlorobenzene dioxygenase for the transformation of chlorinated toluenes. Microbiology 149:903-913.
    • (2003) Microbiology , vol.149 , pp. 903-913
    • Pollmann, K.1    Wray, V.2    Hecht, H.-J.3    Pieper, D.H.4
  • 33
    • 0028085603 scopus 로고
    • Regiospecific and stereoselective hydroxylation of 1-indanone and 2-indanone by naphthalene dioxygenase and toluene dioxygenase
    • Resnick, S. M., D. S. Torok, K. Lee, J. M. Brand, and D. T. Gibson. 1994. Regiospecific and stereoselective hydroxylation of 1-indanone and 2-indanone by naphthalene dioxygenase and toluene dioxygenase. Appl. Environ. Microbiol. 60:3323-3328.
    • (1994) Appl. Environ. Microbiol. , vol.60 , pp. 3323-3328
    • Resnick, S.M.1    Torok, D.S.2    Lee, K.3    Brand, J.M.4    Gibson, D.T.5
  • 34
    • 0001941045 scopus 로고
    • Basic knowledge and perspectives on biodegradation of 2,4,6-trinitrotoluene and related nitroaromatic compounds in contaminated soil
    • J. C. Spain (ed.). Plenum Press, New York, N.Y.
    • Rieger, P.-G., and H.-J. Knackmuss. 1995. Basic knowledge and perspectives on biodegradation of 2,4,6-trinitrotoluene and related nitroaromatic compounds in contaminated soil, p. 1-18. In J. C. Spain (ed.), Biodegradation of nitroaromatic compounds, vol. 49. Plenum Press, New York, N.Y.
    • (1995) Biodegradation of Nitroaromatic Compounds , vol.49 , pp. 1-18
    • Rieger, P.-G.1    Knackmuss, H.-J.2
  • 36
    • 0002842741 scopus 로고
    • Biologically derived arene cis-dihydrodiols as synthetic building blocks
    • A. N. Collins, G. N. Sheldrake, and J. Crosby (ed.). John Wiley & Sons Ltd., Chichester, United Kingdom
    • Sheldrake, G. N. 1992. Biologically derived arene cis-dihydrodiols as synthetic building blocks, p. 127-166. In A. N. Collins, G. N. Sheldrake, and J. Crosby (ed.), Chirality in industry: the commercial manufacture and application of optically active compounds. John Wiley & Sons Ltd., Chichester, United Kingdom.
    • (1992) Chirality in Industry: The Commercial Manufacture and Application of Optically Active Compounds , pp. 127-166
    • Sheldrake, G.N.1
  • 37
    • 0000221252 scopus 로고
    • General characterization
    • P. Gerhardt, R. G. E. Murray, R. N. Costilow, E. W. Nester, W. A. Wood, N. R. Krieg, and G. B. Phillips (ed.). American Society for Microbiology, Washington, D.C.
    • Smibert, R. M., and N. R. Krieg. 1981. General characterization, p. 409-443. In P. Gerhardt, R. G. E. Murray, R. N. Costilow, E. W. Nester, W. A. Wood, N. R. Krieg, and G. B. Phillips (ed.), Manual of methods for general bacteriology. American Society for Microbiology, Washington, D.C.
    • (1981) Manual of Methods for General Bacteriology , pp. 409-443
    • Smibert, R.M.1    Krieg, N.R.2
  • 38
    • 0031799215 scopus 로고    scopus 로고
    • Spreadsheet method for evaluation of biochemical reaction rate coefficients and their uncertainties by weighted nonlinear least-squares analysis of the integrated monod equation
    • Smith, L. H., P. L. McCarty, and P. K. Kitanidis. 1998. Spreadsheet method for evaluation of biochemical reaction rate coefficients and their uncertainties by weighted nonlinear least-squares analysis of the integrated monod equation. Appl. Environ. Microbiol. 64:2044-2050.
    • (1998) Appl. Environ. Microbiol. , vol.64 , pp. 2044-2050
    • Smith, L.H.1    McCarty, P.L.2    Kitanidis, P.K.3
  • 39
    • 12444281969 scopus 로고    scopus 로고
    • Perspectives of bioelimination of polynitroaromatic compounds
    • H. Lenke, C. Achnich, and H.-J. Knackmuss (ed.). CRC Press, Boca Raton, Fla.
    • Spain, J. C., J. B. Hughes, and H.-J. Knackmuss. 2000. Perspectives of bioelimination of polynitroaromatic compounds, p. 91-126. In H. Lenke, C. Achnich, and H.-J. Knackmuss (ed.), Biodegradation of nitroaromaic compounds and explosives. CRC Press, Boca Raton, Fla.
    • (2000) Biodegradation of Nitroaromaic Compounds and Explosives , pp. 91-126
    • Spain, J.C.1    Hughes, J.B.2    Knackmuss, H.-J.3
  • 43
    • 0029779548 scopus 로고    scopus 로고
    • 2,4-Dinitrotoluene dioxygenase from Burkholderia sp. strain DNT: Similarity to naphthalene dioxygenase
    • Suen, W.-C., B. E. Haigler, and J. C. Spain. 1996. 2,4-Dinitrotoluene dioxygenase from Burkholderia sp. strain DNT: similarity to naphthalene dioxygenase. J. Bacteriol. 178:4926-4934.
    • (1996) J. Bacteriol. , vol.178 , pp. 4926-4934
    • Suen, W.-C.1    Haigler, B.E.2    Spain, J.C.3
  • 44
    • 33644965308 scopus 로고    scopus 로고
    • 20 January posting date. [Online]
    • U.S. Environmental Protection Agency. 20 January 2006, posting date. Water Quality Standards Database. [Online.] http://oaspub.epa.gov/wqsdatabase/ wqsi_epa_criteria.rep_parameter.
    • (2006) Water Quality Standards Database
  • 45
    • 0021943518 scopus 로고
    • Improved M13 phage cloning vectors and host strains: Nucleotide sequences of the M13mp18 and pUC19 vectors
    • Yanisch-Perron, C., J. Vieira, and J. Messing. 1985. Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mp18 and pUC19 vectors. Gene 33:103-119.
    • (1985) Gene , vol.33 , pp. 103-119
    • Yanisch-Perron, C.1    Vieira, J.2    Messing, J.3
  • 46
    • 0035434478 scopus 로고    scopus 로고
    • Multiple mutations at the active site of naphthalene dioxygenase affect regioselectivity and enantioselectivity
    • Yu, C.-L., R. E. Parales, and D. T. Gibson. 2001. Multiple mutations at the active site of naphthalene dioxygenase affect regioselectivity and enantioselectivity. J. Ind. Microbiol. Biotechnol. 27:94-103.
    • (2001) J. Ind. Microbiol. Biotechnol. , vol.27 , pp. 94-103
    • Yu, C.-L.1    Parales, R.E.2    Gibson, D.T.3
  • 47
    • 0344393452 scopus 로고    scopus 로고
    • Pinpointing biphenyl dioxygenase residues that are crucial for substrate interaction
    • Zielinski, M., S. Kahl, H. J. Hecht, and B. Hofer. 2003. Pinpointing biphenyl dioxygenase residues that are crucial for substrate interaction. J. Bacteriol. 185:6976-6980.
    • (2003) J. Bacteriol. , vol.185 , pp. 6976-6980
    • Zielinski, M.1    Kahl, S.2    Hecht, H.J.3    Hofer, B.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.