메뉴 건너뛰기




Volumn 142, Issue 9, 1996, Pages 2419-2427

Degradative pathways for p-toluenecarboxylate and p-toluenesulfonate and their multicomponent oxygenases in Comamonas testosteroni strains PSB-4 and T-2

Author keywords

Camamonas testosteroni; Identical enzymes; p sulfobenzoate dioxygenase system; Terephthalate dioxygenase system

Indexed keywords

CARBON; CARBOXYLIC ACID DERIVATIVE; IRON SULFUR PROTEIN; OXIDOREDUCTASE; OXYGENASE; PROTOCATECHUIC ACID; SULFONIC ACID DERIVATIVE; TEREPHTHALIC ACID; TOLUENE DERIVATIVE;

EID: 0029785521     PISSN: 13500872     EISSN: None     Source Type: Journal    
DOI: 10.1099/00221287-142-9-2419     Document Type: Article
Times cited : (23)

References (27)
  • 1
    • 0025005226 scopus 로고
    • The TOL plasmids: Determinants of the catabolism of toluene and the xylenes
    • Assinder, S. J. & Williams, P. A. (1990). The TOL plasmids: determinants of the catabolism of toluene and the xylenes. Adv Microb Physiol 31, 1-69.
    • (1990) Adv Microb Physiol , vol.31 , pp. 1-69
    • Assinder, S.J.1    Williams, P.A.2
  • 3
    • 0002557598 scopus 로고
    • Phthalate dioxygenase reductase and related flavin-iron-sulfur containing electron transferases
    • Edited by F. Müller. Boca Raton: CRC Press
    • Batie, C. J., Ballou, D. P. & Correll, C. C. (1992). Phthalate dioxygenase reductase and related flavin-iron-sulfur containing electron transferases. In Chemistry and Biochemistry of Flavoenzymes, pp. 543-556. Edited by F. Müller. Boca Raton: CRC Press.
    • (1992) Chemistry and Biochemistry of Flavoenzymes , pp. 543-556
    • Batie, C.J.1    Ballou, D.P.2    Correll, C.C.3
  • 4
    • 0014902482 scopus 로고
    • Pigments of Pseudomonas species. Part III. The synthesis of dimethylaeruginosin B and aeruginosin B
    • Bentley, R. K. & Holliman, F. G. (1970). Pigments of Pseudomonas species. Part III. The synthesis of dimethylaeruginosin B and aeruginosin B. J Chem Soc (C) 1970, 2447-2457.
    • (1970) J Chem Soc (C) , vol.1970 , pp. 2447-2457
    • Bentley, R.K.1    Holliman, F.G.2
  • 5
    • 84988074679 scopus 로고
    • Improved silver staining of plant proteins, RNA and DNA in polyacrylamide gels
    • Bloom, H., Beyer, H. & Gross, H. S. (1987). Improved silver staining of plant proteins, RNA and DNA in polyacrylamide gels. Electrophoresis 8, 93-99.
    • (1987) Electrophoresis , vol.8 , pp. 93-99
    • Bloom, H.1    Beyer, H.2    Gross, H.S.3
  • 6
    • 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
    • 0026515685 scopus 로고
    • Identification of xenobiotic-degrading isolates from the beta subclass of the Proteobacteria by a polyphasic approach including 16S rRNA partial sequencing
    • Busse, H.-J., El-Banna, T., Oyaizu, H. & Auling, G. (1992). Identification of xenobiotic-degrading isolates from the beta subclass of the Proteobacteria by a polyphasic approach including 16S rRNA partial sequencing. Int J Syst Bacteriol 42, 19-26.
    • (1992) Int J Syst Bacteriol , vol.42 , pp. 19-26
    • Busse, H.-J.1    El-Banna, T.2    Oyaizu, H.3    Auling, G.4
  • 8
    • 0002624801 scopus 로고
    • Biodegradation of aromatics with industrial relevance
    • Edited by T. Leisinger, A. M. Cook, R. Hütter & J. Nüesch. London: Academic Press
    • Fewson, C. A. (1981). Biodegradation of aromatics with industrial relevance. In Microbial Degradation of Xenobiotics and Recalcitrant Compounds, pp. 141-179. Edited by T. Leisinger, A. M. Cook, R. Hütter & J. Nüesch. London: Academic Press.
    • (1981) Microbial Degradation of Xenobiotics and Recalcitrant Compounds , pp. 141-179
    • Fewson, C.A.1
  • 9
    • 0027223958 scopus 로고
    • Gene components responsible for discrete substrate specificity in the metabolism of biphenyl (bph operon) and toluene (tod operon)
    • Furukawa, K., Hirose, J., Suyama, A., Zaiki, T. & Hayashida, S. (1993). Gene components responsible for discrete substrate specificity in the metabolism of biphenyl (bph operon) and toluene (tod operon). J Bacteriol 175, 5224-5232.
    • (1993) J Bacteriol , vol.175 , pp. 5224-5232
    • Furukawa, K.1    Hirose, J.2    Suyama, A.3    Zaiki, T.4    Hayashida, S.5
  • 10
    • 0026805891 scopus 로고
    • Functional and evolutionary relationships among diverse oxygenases
    • Harayama, S., Kok, M. & Neidle, E. L. (1992). Functional and evolutionary relationships among diverse oxygenases. Annu Rev Microbiol 46, 565-601.
    • (1992) Annu Rev Microbiol , vol.46 , pp. 565-601
    • Harayama, S.1    Kok, M.2    Neidle, E.L.3
  • 11
    • 0028215858 scopus 로고
    • Construction of hybrid biphenyl (bph) and toluene (tod) genes for functional analysis of aromatic ring dioxygenases
    • Hirose, J., Suyama, A., Hayashida, S. & Furukawa, K. (1994). Construction of hybrid biphenyl (bph) and toluene (tod) genes for functional analysis of aromatic ring dioxygenases. Gene 138, 27-33.
    • (1994) Gene , vol.138 , pp. 27-33
    • Hirose, J.1    Suyama, A.2    Hayashida, S.3    Furukawa, K.4
  • 12
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 13
    • 0024696849 scopus 로고
    • Degradation of p-toluenesulphonic acid via sidechain oxidation, desulphonation and meta ring cleavage in Pseudomonas (Comamonas) testosteroni T-2
    • Locher, H. H., Leisinger, T. & Cook, A. M. (1989). Degradation of p-toluenesulphonic acid via sidechain oxidation, desulphonation and meta ring cleavage in Pseudomonas (Comamonas) testosteroni T-2. J Gen Microbiol 135, 1969-1978.
    • (1989) J Gen Microbiol , vol.135 , pp. 1969-1978
    • Locher, H.H.1    Leisinger, T.2    Cook, A.M.3
  • 14
    • 0026035916 scopus 로고
    • 4-Sulphobenzoate 3,4-dioxygenase: Purification and properties of a desulphonative two-component enzyme system from Comamonas testosteroni T-2
    • Locher, H. H., Leisinger, T. & Cook, A. M. (1991a). 4-Sulphobenzoate 3,4-dioxygenase: purification and properties of a desulphonative two-component enzyme system from Comamonas testosteroni T-2. Biochem J 274, 833-842.
    • (1991) Biochem J , vol.274 , pp. 833-842
    • Locher, H.H.1    Leisinger, T.2    Cook, A.M.3
  • 15
    • 0025895072 scopus 로고
    • 4-Toluene sulfonate methyl-monooxygenase from Comamonas testosteroni T-2: Purification and some properties of the oxygenase component
    • Locher, H. H., Leisinger, T. & Cook, A. M. (1991b). 4-Toluene sulfonate methyl-monooxygenase from Comamonas testosteroni T-2: purification and some properties of the oxygenase component. J Bacteriol 173, 3741-3748.
    • (1991) J Bacteriol , vol.173 , pp. 3741-3748
    • Locher, H.H.1    Leisinger, T.2    Cook, A.M.3
  • 16
    • 0025743807 scopus 로고
    • Degradation of p-toluic acid (p-toluene carboxylic acid) and p-toluene sulphonic acid via oxygenation of the methyl sidechain is initiated by the same set of enzymes in Comamonas testosteroni T-2
    • Locher, H. H., Malli, C., Hooper, S., Vorherr, T., Leisinger, T. & Cook, A. M. (1991c). Degradation of p-toluic acid (p-toluene carboxylic acid) and p-toluene sulphonic acid via oxygenation of the methyl sidechain is initiated by the same set of enzymes in Comamonas testosteroni T-2. J Gen Microbiol 137, 2201-2208.
    • (1991) J Gen Microbiol , vol.137 , pp. 2201-2208
    • Locher, H.H.1    Malli, C.2    Hooper, S.3    Vorherr, T.4    Leisinger, T.5    Cook, A.M.6
  • 17
    • 0027368422 scopus 로고
    • Quantitative analysis of sulfonic acid groups in macromolecular lignosulfonic acids and aquatic humic substances by temperature-resolved pyrolysis-mass spectrometry
    • van Loon, W. M. G. M., Boon, J. J. & de Groot, B. (1993). Quantitative analysis of sulfonic acid groups in macromolecular lignosulfonic acids and aquatic humic substances by temperature- resolved pyrolysis-mass spectrometry. Environ Sci Technol 27, 2387-2396.
    • (1993) Environ Sci Technol , vol.27 , pp. 2387-2396
    • Van Loon, W.M.G.M.1    Boon, J.J.2    De Groot, B.3
  • 18
    • 0026743341 scopus 로고
    • The electron-transport proteins of hydroxylating bacterial dioxygenases
    • Mason, J. R. & Cammack, R. (1992). The electron-transport proteins of hydroxylating bacterial dioxygenases. Annu Rev Microbiol 46, 277-305.
    • (1992) Annu Rev Microbiol , vol.46 , pp. 277-305
    • Mason, J.R.1    Cammack, R.2
  • 19
    • 0028914126 scopus 로고
    • The nucleotide sequence of the Tn5271 3-chlorobenzoate 3,4-dioxygenase genes (cbaAB) unites the class IA oxygenases in a single lineage
    • Nakatsu, C. H., Straus, N. A. & Wyndham, R. C. (1995). The nucleotide sequence of the Tn5271 3-chlorobenzoate 3,4-dioxygenase genes (cbaAB) unites the class IA oxygenases in a single lineage. Microbiology 141, 485-495.
    • (1995) Microbiology , vol.141 , pp. 485-495
    • Nakatsu, C.H.1    Straus, N.A.2    Wyndham, R.C.3
  • 20
    • 0024959342 scopus 로고
    • Nitrous oxide reductase from Pseudomonas stutzeri: Redox properties and spectroscopic characterization of different forms of the multicopper enzyme
    • Riester, J., Zumft, W. G. & Kroneck, P. M. H. (1989). Nitrous oxide reductase from Pseudomonas stutzeri: redox properties and spectroscopic characterization of different forms of the multicopper enzyme. Eur J Biochem 178, 751-762.
    • (1989) Eur J Biochem , vol.178 , pp. 751-762
    • Riester, J.1    Zumft, W.G.2    Kroneck, P.M.H.3
  • 21
    • 0029015678 scopus 로고
    • Purification and some properties of (1R,2S)-1,2-dihydroxy-3,5- Cyclohexadiene-1,4-dicarboxylate dehydrogenase from Comamonas testosteroni T-2
    • Saller, E., Laue, H., Schläfli Oppenberg, H. R. & Cook, A. M. (1995). Purification and some properties of (1R,2S)-1,2-dihydroxy-3,5- cyclohexadiene-1,4-dicarboxylate dehydrogenase from Comamonas testosteroni T-2. FEMS Microbiol Lett 130, 97-102.
    • (1995) FEMS Microbiol Lett , vol.130 , pp. 97-102
    • Saller, E.1    Laue, H.2    Schläfli Oppenberg, H.R.3    Cook, A.M.4
  • 22
    • 0028037006 scopus 로고
    • Terephthalate 1,2-dioxygenase system from Comamonas testosteroni T-2: Purification and some properties of the oxygenase component
    • Schläfli, H. R., Weiss, M. A., Leisinger, T. & Cook, A. M. (1994). Terephthalate 1,2-dioxygenase system from Comamonas testosteroni T-2: purification and some properties of the oxygenase component. J Bacteriol 176, 6644-6652.
    • (1994) J Bacteriol , vol.176 , pp. 6644-6652
    • Schläfli, H.R.1    Weiss, M.A.2    Leisinger, T.3    Cook, A.M.4
  • 23
    • 0028918091 scopus 로고
    • Stereospecificity of hydride removal from NADH by reductases of multicomponent nonheme iron oxygenase systems
    • Schläfli, H. R., Baker, D. P., Leisinger, T. & Cook, A. M. (1995). Stereospecificity of hydride removal from NADH by reductases of multicomponent nonheme iron oxygenase systems. J Bacteriol 177, 831-834.
    • (1995) J Bacteriol , vol.177 , pp. 831-834
    • Schläfli, H.R.1    Baker, D.P.2    Leisinger, T.3    Cook, A.M.4
  • 24
    • 0029115030 scopus 로고
    • Regulation of the degradative pathways from 4-toluenesulfonate and 4-toluenecarboxylate to protocatechuate in Comamonas testosteroni T-2
    • Schläfli Oppenberg, H. R., Chen, G., Leisinger, T. & Cook, A. M. (1995). Regulation of the degradative pathways from 4-toluenesulfonate and 4-toluenecarboxylate to protocatechuate in Comamonas testosteroni T-2. Microbiology 141, 1891-1899.
    • (1995) Microbiology , vol.141 , pp. 1891-1899
    • Schläfli Oppenberg, H.R.1    Chen, G.2    Leisinger, T.3    Cook, A.M.4
  • 26
    • 0022621550 scopus 로고
    • Orthanilic acid and analogues as carbon sources for bacteria: Growth physiology and enzymic desulphonation
    • Thurnheer, T., Köhler, T., Cook, A. M. & Leisinger, T. (1986). Orthanilic acid and analogues as carbon sources for bacteria: growth physiology and enzymic desulphonation. J Gen Microbiol 132, 1215-1220.
    • (1986) J Gen Microbiol , vol.132 , pp. 1215-1220
    • Thurnheer, T.1    Köhler, T.2    Cook, A.M.3    Leisinger, T.4
  • 27
    • 0025832054 scopus 로고
    • Polyphasic taxonomic study of the emended genus Comamonas: Relationship to Aquaspirillum aquaticum, E. Falsen group 10, and other clinical isolates
    • Willems, A., Pot, B., Falsen, E., Vandamme, P., Gillis, M., Kersters, K. & de Ley, J. (1991). Polyphasic taxonomic study of the emended genus Comamonas: relationship to Aquaspirillum aquaticum, E. Falsen group 10, and other clinical isolates. Int J Syst Bacteriol 41, 427-444.
    • (1991) Int J Syst Bacteriol , vol.41 , pp. 427-444
    • Willems, A.1    Pot, B.2    Falsen, E.3    Vandamme, P.4    Gillis, M.5    Kersters, K.6    De Ley, J.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.