메뉴 건너뛰기




Volumn 71, Issue 8, 2005, Pages 4744-4750

Mutation of glutamic acid 103 of toluene o-xylene monooxygenase as a means to control the catabolic efficiency of a recombinant upper pathway for degradation of methylated aromatic compounds

Author keywords

[No Author keywords available]

Indexed keywords

AROMATIC HYDROCARBONS; DEGRADATION; ENZYMES; ISOMERS; METABOLISM;

EID: 23744453849     PISSN: 00992240     EISSN: None     Source Type: Journal    
DOI: 10.1128/AEM.71.8.4744-4750.2005     Document Type: Article
Times cited : (18)

References (21)
  • 1
    • 0035404556 scopus 로고    scopus 로고
    • Organization and regulation of meta cleavage pathway gene for toluene and o-xylene derivative degradation in Pseudomonas stutzeri OX1
    • Arenghi, F. L., D. Berlanda, E. Galli, G. Sello, and P. Barbieri. 2001. Organization and regulation of meta cleavage pathway gene for toluene and o-xylene derivative degradation in Pseudomonas stutzeri OX1. Appl. Environ. Microbiol. 67:3304-3308.
    • (2001) Appl. Environ. Microbiol. , vol.67 , pp. 3304-3308
    • Arenghi, F.L.1    Berlanda, D.2    Galli, E.3    Sello, G.4    Barbieri, P.5
  • 2
    • 0029783360 scopus 로고    scopus 로고
    • Cloning of the genes for and characterization of the early stages of toluene catabolism in Pseudomonas stutzeri OX1
    • Bertoni, G., F. Bolognesi, E. Galli, and P. Barbieri. 1996. Cloning of the genes for and characterization of the early stages of toluene catabolism in Pseudomonas stutzeri OX1. Appl. Environ. Microbiol. 62:3704-3711.
    • (1996) Appl. Environ. Microbiol. , vol.62 , pp. 3704-3711
    • Bertoni, G.1    Bolognesi, F.2    Galli, E.3    Barbieri, P.4
  • 3
    • 0031684004 scopus 로고    scopus 로고
    • Analysis of the gene cluster encoding toluene/o-xylene monooxygenase from Pseudomonas stutzeri OX1
    • Bertoni, G., M. Martino, E. Galli, and P. Barbieri. 1998. Analysis of the gene cluster encoding toluene/o-xylene monooxygenase from Pseudomonas stutzeri OX1. Appl. Environ. Microbiol. 64:3626-3632.
    • (1998) Appl. Environ. Microbiol. , vol.64 , pp. 3626-3632
    • Bertoni, G.1    Martino, M.2    Galli, E.3    Barbieri, P.4
  • 4
    • 23744478280 scopus 로고    scopus 로고
    • Regiospecificity of two multicomponent monooxygenases from Pseudomonas stutzeri OX1: Molecular basis for catabolic adaptation of this microorganism to methylated aromatic compounds
    • Cafaro, V., E. Notomista, P. Capasso, and A. Di Donate. 2005. Regiospecificity of two multicomponent monooxygenases from Pseudomonas stutzeri OX1: molecular basis for catabolic adaptation of this microorganism to methylated aromatic compounds. Appl. Environ. Microbiol. 71:4736-4743.
    • (2005) Appl. Environ. Microbiol. , vol.71 , pp. 4736-4743
    • Cafaro, V.1    Notomista, E.2    Capasso, P.3    Di Donate, A.4
  • 5
    • 0033982698 scopus 로고    scopus 로고
    • Enzymes involved in the aerobic bacterial degradation of N-heteroaromatic compounds: Molybdenum hydroxylases and ring-opening 2,4-dioxygenases
    • Fetzner, S., and J. R. van der Meer. 2000. Enzymes involved in the aerobic bacterial degradation of N-heteroaromatic compounds: molybdenum hydroxylases and ring-opening 2,4-dioxygenases. Naturwissenschaften 87:59-69.
    • (2000) Naturwissenschaften , vol.87 , pp. 59-69
    • Fetzner, S.1    Van Der Meer, J.R.2
  • 6
    • 0030754267 scopus 로고    scopus 로고
    • Multiple pathways for toluene degradation in Burkholderia sp. strain JS150
    • Johnson, G. R., and R. H. Olsen. 1997. Multiple pathways for toluene degradation in Burkholderia sp. strain JS150. Appl. Environ. Microbiol. 63:4047-4052.
    • (1997) Appl. Environ. Microbiol. , vol.63 , pp. 4047-4052
    • Johnson, G.R.1    Olsen, R.H.2
  • 7
    • 2642699794 scopus 로고
    • Rapid and efficient site-specific mutagenesis without phenotypic selection
    • Kunkel, T. A. 1987. Rapid and efficient site-specific mutagenesis without phenotypic selection. Proc. Natl. Acad. Sci. USA 82:488-492.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 488-492
    • Kunkel, T.A.1
  • 8
    • 0037022829 scopus 로고    scopus 로고
    • Combined participation of hydroxylase active site residues and effector protein binding in a para to ortho modulation of toluene 4-monooxygenase regiospecificity
    • Mitchell, K. H., J. M. Studts, and B. G. Fox. 2002. Combined participation of hydroxylase active site residues and effector protein binding in a para to ortho modulation of toluene 4-monooxygenase regiospecificity. Biochemistry 41:3176-3188.
    • (2002) Biochemistry , vol.41 , pp. 3176-3188
    • Mitchell, K.H.1    Studts, J.M.2    Fox, B.G.3
  • 9
    • 0037381328 scopus 로고    scopus 로고
    • Evolution of bacterial and archaeal multicomponent monooxygenases
    • Notomista, E., A. Lahm, A. Di Donato, and A. Tramontano. 2003. Evolution of bacterial and archaeal multicomponent monooxygenases. J. Mol. Evol. 56:435-445.
    • (2003) J. Mol. Evol. , vol.56 , pp. 435-445
    • Notomista, E.1    Lahm, A.2    Di Donato, A.3    Tramontano, A.4
  • 10
    • 0029942829 scopus 로고    scopus 로고
    • Recombinant toluene-4-monooxygenase: Catalytic and Mossbauer studies of the purified diiron and Rieske components of a four-protein complex
    • Pikus, J. D., J. M. Studts, C. Achim, K. E. Kauffmann, E. Munck, R. J. Steffan, K. McClay, and B. G. Fox. 1996. Recombinant toluene-4-monooxygenase: catalytic and Mossbauer studies of the purified diiron and Rieske components of a four-protein complex. Biochemistry 35:9106-9119.
    • (1996) Biochemistry , vol.35 , pp. 9106-9119
    • Pikus, J.D.1    Studts, J.M.2    Achim, C.3    Kauffmann, K.E.4    Munck, E.5    Steffan, R.J.6    McClay, K.7    Fox, B.G.8
  • 11
    • 0030739171 scopus 로고    scopus 로고
    • Changes in the regiospecificity of aromatic hydroxylation produced by active site engineering in the diiron toluene 4-monooxygenase
    • Pikus, J. D., J. M. Studts, K. McClay, R. J. Steffan, and B. G. Fox. 1997. Changes in the regiospecificity of aromatic hydroxylation produced by active site engineering in the diiron toluene 4-monooxygenase. Biochemistry 36:9283-9289.
    • (1997) Biochemistry , vol.36 , pp. 9283-9289
    • Pikus, J.D.1    Studts, J.M.2    McClay, K.3    Steffan, R.J.4    Fox, B.G.5
  • 12
    • 0028672047 scopus 로고
    • Genetics and biochemistry of phenol degradation by Pseudomonas sp. CF600
    • Powlowski, J., and V. Shingler. 1994. Genetics and biochemistry of phenol degradation by Pseudomonas sp. CF600. Biodegradation 5:219-236.
    • (1994) Biodegradation , vol.5 , pp. 219-236
    • Powlowski, J.1    Shingler, V.2
  • 14
    • 0027180726 scopus 로고
    • Plasmid-mediated mineralization of naphthalene, phenanthrene, and anthracene
    • Sanseverino, J., B. M. Applegate, J. M. King, and G. S. Sayler. 1993. Plasmid-mediated mineralization of naphthalene, phenanthrene, and anthracene. Appl. Environ. Microbiol. 59:1931-1937.
    • (1993) Appl. Environ. Microbiol. , vol.59 , pp. 1931-1937
    • Sanseverino, J.1    Applegate, B.M.2    King, J.M.3    Sayler, G.S.4
  • 15
    • 3142777798 scopus 로고    scopus 로고
    • Crystal structure of the toluene/o-xylene monooxygenase hydroxylase from Pseudomonas stutzeri OX1. Insight into the substrate specificity, substrate channeling, and active site tuning of multicomponent monooxygenases
    • Sazinsky, M. H., J. Bard, A. Di Donato, and S. J. Lippard. 2004. Crystal structure of the toluene/o-xylene monooxygenase hydroxylase from Pseudomonas stutzeri OX1. Insight into the substrate specificity, substrate channeling, and active site tuning of multicomponent monooxygenases. J. Biol. Chem. 279:30600-30610.
    • (2004) J. Biol. Chem. , vol.279 , pp. 30600-30610
    • Sazinsky, M.H.1    Bard, J.2    Di Donato, A.3    Lippard, S.J.4
  • 16
    • 3042815981 scopus 로고    scopus 로고
    • Altering toluene 4-monooxygenase by active-site engineering for the synthesis of 3-methoxycatechol, methoxyhydroquinone, and methylhydroquinone
    • Tao, Y., A. Fishman, W. E. Bentley, and T. K. Wood. 2004. Altering toluene 4-monooxygenase by active-site engineering for the synthesis of 3-methoxycatechol, methoxyhydroquinone, and methylhydroquinone. J. Bacteriol. 186:4705-4713.
    • (2004) J. Bacteriol. , vol.186 , pp. 4705-4713
    • Tao, Y.1    Fishman, A.2    Bentley, W.E.3    Wood, T.K.4
  • 17
    • 0031028986 scopus 로고    scopus 로고
    • Evolution of novel metabolic pathways for the degradation of chloroaromatic compounds
    • van der Meer, J. R. 1997. Evolution of novel metabolic pathways for the degradation of chloroaromatic compounds. Antonie Leeuwenhoek 71:159-178.
    • (1997) Antonie Leeuwenhoek , vol.71 , pp. 159-178
    • Van Der Meer, J.R.1
  • 18
    • 2942592050 scopus 로고    scopus 로고
    • Protein engineering of toluene-o-xylene monooxygenase from Pseudomonas stutzeri OX1 for synthesizing 4-methylresorcinol, methylhydroquinone, and pyrogallol
    • Vardar, G., and T. K. Wood. 2004. Protein engineering of toluene-o-xylene monooxygenase from Pseudomonas stutzeri OX1 for synthesizing 4-methylresorcinol, methylhydroquinone, and pyrogallol. Appl. Environ. Microbiol. 70:3253-3262.
    • (2004) Appl. Environ. Microbiol. , vol.70 , pp. 3253-3262
    • Vardar, G.1    Wood, T.K.2
  • 19
    • 10344235266 scopus 로고    scopus 로고
    • The role of conserved residues H246, H199 and Y255 in the catalysis of catechol 2,3-dioxygenase from Pseudomonas stutzeri OX1
    • Viggiani, A., L. Siani, E. Notomista, L. Birolo, P. Pucci, and A. Di Donato. 2004. The role of conserved residues H246, H199 and Y255 in the catalysis of catechol 2,3-dioxygenase from Pseudomonas stutzeri OX1. J. Biol. Chem. 279:48630-48639.
    • (2004) J. Biol. Chem. , vol.279 , pp. 48630-48639
    • Viggiani, A.1    Siani, L.2    Notomista, E.3    Birolo, L.4    Pucci, P.5    Di Donato, A.6
  • 20
    • 0025805280 scopus 로고
    • Separation and partial characterization of the enzymes of the toluene-4-monooxygenase catabolic pathway in Pseudomonas mendocina KR1
    • Whited, G. M., and D. T. Gibson. 1991. Separation and partial characterization of the enzymes of the toluene-4-monooxygenase catabolic pathway in Pseudomonas mendocina KR1. J. Bacteriol. 173:3017-3020.
    • (1991) J. Bacteriol. , vol.173 , pp. 3017-3020
    • Whited, G.M.1    Gibson, D.T.2
  • 21
    • 0025906028 scopus 로고
    • Toluene-4-monooxygenase, a three component enzyme system that catalyzes the oxidation of toluene to p-cresol in Pseudomonas mendocina KR1
    • Whited, G. M., and D. T. Gibson. 1991. Toluene-4-monooxygenase, a three component enzyme system that catalyzes the oxidation of toluene to p-cresol in Pseudomonas mendocina KR1. J. Bacteriol. 173:3010-3016.
    • (1991) J. Bacteriol. , vol.173 , pp. 3010-3016
    • Whited, G.M.1    Gibson, D.T.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.