메뉴 건너뛰기




Volumn 65, Issue 6, 2011, Pages 853-858

High activity catechol 2,3-dioxygenase from the cresols - Degrading Stenotrophomonas maltophilia strain KB2

Author keywords

Aromatic compounds; Biodegradation; Dioxygenases; Stenotrophomonas

Indexed keywords

2-METHYLPHENOL; 4-METHYLPHENOL; AROMATIC SUBSTRATES; BIOCHEMICAL ANALYSIS; DIOXYGENASES; ENERGY SOURCE; EXTRADIOL; HIGH ACTIVITY; HISTIDINE RESIDUES; ION BINDING; KINETIC STUDY; PHYLOGENETIC ANALYSIS; SOLE CARBON; STENOTROPHOMONAS; STENOTROPHOMONAS MALTOPHILIA; WIDE SPECTRUM;

EID: 79961208826     PISSN: 09648305     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ibiod.2011.06.006     Document Type: Article
Times cited : (41)

References (40)
  • 1
    • 0034907757 scopus 로고    scopus 로고
    • New metabolic pathway for o-cresol degradation by Pseudomonas sp. CP4 as evidenced by 1H NMR spectroscopic studies
    • Ahamad P.Y.A., Kunhi A.A.M., Divakar S. New metabolic pathway for o-cresol degradation by Pseudomonas sp. CP4 as evidenced by 1H NMR spectroscopic studies. World Journal of Microbiology and Biotechnology 2001, 17:371-377.
    • (2001) World Journal of Microbiology and Biotechnology , vol.17 , pp. 371-377
    • Ahamad, P.Y.A.1    Kunhi, A.A.M.2    Divakar, S.3
  • 2
    • 0032898962 scopus 로고    scopus 로고
    • Genetic and biochemical analyses of the tec operon suggest a route for evolution of chlorobenzene degradation genes
    • Beil S., Timmis K.N., Pieper D.H. Genetic and biochemical analyses of the tec operon suggest a route for evolution of chlorobenzene degradation genes. Journal of Bacteriology 1999, 181:341-346.
    • (1999) Journal of Bacteriology , vol.181 , pp. 341-346
    • Beil, S.1    Timmis, K.N.2    Pieper, D.H.3
  • 3
    • 0028210260 scopus 로고
    • Aliphatic and aromatic inhibitors binding to the active site of catechol 2,3-dioxygenase from Pseudomonas putida mt-2
    • Bertini I., Briganti F., Scozzafava A. Aliphatic and aromatic inhibitors binding to the active site of catechol 2,3-dioxygenase from Pseudomonas putida mt-2. FEBS Letters 1994, 242:56-60.
    • (1994) FEBS Letters , vol.242 , pp. 56-60
    • Bertini, I.1    Briganti, F.2    Scozzafava, A.3
  • 4
    • 0017184389 scopus 로고
    • A rapid and sensitive method of the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method of the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Analytical Biochemistry 1976, 72:248-258.
    • (1976) Analytical Biochemistry , vol.72 , pp. 248-258
    • Bradford, M.M.1
  • 5
    • 34247539831 scopus 로고    scopus 로고
    • Comparative analysis of the catechol 2,3-dioxygenase gene locus in thermoacidophilic archeon Sulfolobus solfataricus strain 98/2
    • Chae J.Ch., Kim E., Bini E., Zylstra G.J. Comparative analysis of the catechol 2,3-dioxygenase gene locus in thermoacidophilic archeon Sulfolobus solfataricus strain 98/2. Biochemical and Biophysical Research Communications 2007, 357:815-819.
    • (2007) Biochemical and Biophysical Research Communications , vol.357 , pp. 815-819
    • Chae, J.1    Kim, E.2    Bini, E.3    Zylstra, G.J.4
  • 6
    • 77951141722 scopus 로고    scopus 로고
    • Enhanced biotransformation of mononitrophenols by Stenotrophomonas maltophilia KB2 in the presence of aromatic compounds of plant origin
    • Greń I., Wojcieszyńska D., Guzik U., Perkosz M., Hupert-Kocurek K. Enhanced biotransformation of mononitrophenols by Stenotrophomonas maltophilia KB2 in the presence of aromatic compounds of plant origin. World Journal of Microbiology and Biotechnology 2010, 26:289-295.
    • (2010) World Journal of Microbiology and Biotechnology , vol.26 , pp. 289-295
    • Greń, I.1    Wojcieszyńska, D.2    Guzik, U.3    Perkosz, M.4    Hupert-Kocurek, K.5
  • 7
    • 69249137529 scopus 로고    scopus 로고
    • Isolation and characterization of a novel strain of Stenotrophomonas maltophilia possessing various dioxygenases for monocyclic hydrocarbon degradation
    • Guzik U., Greń I., Wojcieszyńska D., Łabużek S. Isolation and characterization of a novel strain of Stenotrophomonas maltophilia possessing various dioxygenases for monocyclic hydrocarbon degradation. Brazilian Journal of Microbiology 2009, 40:285-291.
    • (2009) Brazilian Journal of Microbiology , vol.40 , pp. 285-291
    • Guzik, U.1    Greń, I.2    Wojcieszyńska, D.3    Łabuzek, S.4
  • 8
    • 0029795374 scopus 로고    scopus 로고
    • The β-ketoadipate pathway and the biology of self-identity
    • Harwood C.S., Parales R.E. The β-ketoadipate pathway and the biology of self-identity. Annual Review of Microbiology 1996, 50:553-590.
    • (1996) Annual Review of Microbiology , vol.50 , pp. 553-590
    • Harwood, C.S.1    Parales, R.E.2
  • 9
    • 0038159602 scopus 로고    scopus 로고
    • Characterization of a novel thermostable Mn(II)-dependent 2,3-dihydroxybophenyl 1,2-dioxygenase from a PCB and naphthalene-degrading Bacillus sp. JF8
    • Hatta T., Mukerjee-Dhar G., Damborsky J., Kiyohara H., Kimbara K. Characterization of a novel thermostable Mn(II)-dependent 2,3-dihydroxybophenyl 1,2-dioxygenase from a PCB and naphthalene-degrading Bacillus sp. JF8. Journal of Biological Chemistry 2003, 278:21483-21492.
    • (2003) Journal of Biological Chemistry , vol.278 , pp. 21483-21492
    • Hatta, T.1    Mukerjee-Dhar, G.2    Damborsky, J.3    Kiyohara, H.4    Kimbara, K.5
  • 10
    • 0034052473 scopus 로고    scopus 로고
    • Three types of phenol and p-cresol- degrading bacteria isolated from river water continuously polluted with phenolic compounds
    • Heinaru E., Truu J., Stottmeister U., Heinaru A. Three types of phenol and p-cresol- degrading bacteria isolated from river water continuously polluted with phenolic compounds. FEMS Microbiology Ecology 2000, 31:195-205.
    • (2000) FEMS Microbiology Ecology , vol.31 , pp. 195-205
    • Heinaru, E.1    Truu, J.2    Stottmeister, U.3    Heinaru, A.4
  • 11
    • 77955657761 scopus 로고    scopus 로고
    • Functional consortia for cresol- degrading activated sludge: toxicity- to- extinction approach
    • Ho K.-L., Chen Y.-Y., Lee D.-J. Functional consortia for cresol- degrading activated sludge: toxicity- to- extinction approach. Bioresource Technology 2010, 101:9000-9005.
    • (2010) Bioresource Technology , vol.101 , pp. 9000-9005
    • Ho, K.-L.1    Chen, Y.-Y.2    Lee, D.-J.3
  • 13
    • 4644317596 scopus 로고    scopus 로고
    • Catechol 2,3-dioxygenase from Pseudomonas sp. strain ND6: gene sequence and enzyme characterization
    • Jiang Y., Yang Z., Liu B., Zhao H., Cheng Q., Cai B. Catechol 2,3-dioxygenase from Pseudomonas sp. strain ND6: gene sequence and enzyme characterization. Bioscience, Biotechnology and Biochemistry 2004, 68:1798-1800.
    • (2004) Bioscience, Biotechnology and Biochemistry , vol.68 , pp. 1798-1800
    • Jiang, Y.1    Yang, Z.2    Liu, B.3    Zhao, H.4    Cheng, Q.5    Cai, B.6
  • 14
    • 79961210061 scopus 로고    scopus 로고
    • Oxidative inactivation of ring-cleavage extradiol dioxygenases: mechanism and ferredoxin-mediated reactivation
    • Springer, New York, K.N. Timmis (Ed.)
    • Jouanneau Y. Oxidative inactivation of ring-cleavage extradiol dioxygenases: mechanism and ferredoxin-mediated reactivation. Microbiology of hydrocarbons, oils, lipids, and derived compounds 2010, 1-10. Springer, New York. first ed. K.N. Timmis (Ed.).
    • (2010) Microbiology of hydrocarbons, oils, lipids, and derived compounds , pp. 1-10
    • Jouanneau, Y.1
  • 15
    • 11044228534 scopus 로고    scopus 로고
    • Difference in kinetic behavior of catechol 2,3-dioxygenase variants from a polluted environment
    • Junca H., Plumeier I., Hecht H.J., Pieper D.H. Difference in kinetic behavior of catechol 2,3-dioxygenase variants from a polluted environment. Microbiology 2004, 150:4181-4187.
    • (2004) Microbiology , vol.150 , pp. 4181-4187
    • Junca, H.1    Plumeier, I.2    Hecht, H.J.3    Pieper, D.H.4
  • 17
    • 0031936515 scopus 로고    scopus 로고
    • Degradation of chloroaromatics: purification and characterization of a novel type of chlorocatechol 2,3-dioxygenase of Pseudomonas putida GJ31
    • Kaschabek S.R., Kasberg T., Muller D., Mars A.E., Janssen D.B., Reineke W. Degradation of chloroaromatics: purification and characterization of a novel type of chlorocatechol 2,3-dioxygenase of Pseudomonas putida GJ31. Journal of Bacteriology 1998, 180:296-302.
    • (1998) Journal of Bacteriology , vol.180 , pp. 296-302
    • Kaschabek, S.R.1    Kasberg, T.2    Muller, D.3    Mars, A.E.4    Janssen, D.B.5    Reineke, W.6
  • 18
    • 34547840264 scopus 로고    scopus 로고
    • Diversity of catechol 2,3-dioxygenase genes of bacteria responding to dissolved organic matter derived from different sources in a eutrophic lake
    • Kasuga I., Nakajima F., Furumai H. Diversity of catechol 2,3-dioxygenase genes of bacteria responding to dissolved organic matter derived from different sources in a eutrophic lake. FEMS Microbiology Ecology 2007, 61:449-458.
    • (2007) FEMS Microbiology Ecology , vol.61 , pp. 449-458
    • Kasuga, I.1    Nakajima, F.2    Furumai, H.3
  • 19
    • 10644234814 scopus 로고    scopus 로고
    • Functional characterization and molecular modeling of methylcatechol 2,3-dioxygenase from o-xylene-degrading Rhodococcus sp. strain DK17
    • Kim D., Chae J.Ch., Jang J.Y., Zylstra G.J., Kim Y.M., Kang B.S., Kim E. Functional characterization and molecular modeling of methylcatechol 2,3-dioxygenase from o-xylene-degrading Rhodococcus sp. strain DK17. Biochemical and Biophysical Research Communications 2005, 326:880-886.
    • (2005) Biochemical and Biophysical Research Communications , vol.326 , pp. 880-886
    • Kim, D.1    Chae, J.2    Jang, J.Y.3    Zylstra, G.J.4    Kim, Y.M.5    Kang, B.S.6    Kim, E.7
  • 20
    • 0033556265 scopus 로고    scopus 로고
    • An archetypical extradiol-cleaving catecholic dioxygenase: the crystal structure of catechol 2,3-dioxygenase (metapyrocatechase) from Pseudomonas putida mt-2
    • Kita A., Kita S., Fujisawa I., Inaka K., Ishida T., Horiike K., Nozaki M., Mik K. An archetypical extradiol-cleaving catecholic dioxygenase: the crystal structure of catechol 2,3-dioxygenase (metapyrocatechase) from Pseudomonas putida mt-2. Structure 1999, 7:25-34.
    • (1999) Structure , vol.7 , pp. 25-34
    • Kita, A.1    Kita, S.2    Fujisawa, I.3    Inaka, K.4    Ishida, T.5    Horiike, K.6    Nozaki, M.7    Mik, K.8
  • 21
    • 34247534094 scopus 로고    scopus 로고
    • Crystal structures of Fe2+ dioxygenase superoxo, alkylperoxo, and bound product intermediates
    • Kovaleva E.G., Lipscomb J.D. Crystal structures of Fe2+ dioxygenase superoxo, alkylperoxo, and bound product intermediates. Science 2007, 316:453-547.
    • (2007) Science , vol.316 , pp. 453-547
    • Kovaleva, E.G.1    Lipscomb, J.D.2
  • 22
    • 0030012764 scopus 로고    scopus 로고
    • Catechol 2,3-dioxygenases functional in oxygen-limited (hypoxic) environments
    • Kukor J.J., Olsen R.H. Catechol 2,3-dioxygenases functional in oxygen-limited (hypoxic) environments. Applied of Environmental Microbiology 1996, 62:1728-1740.
    • (1996) Applied of Environmental Microbiology , vol.62 , pp. 1728-1740
    • Kukor, J.J.1    Olsen, R.H.2
  • 23
    • 79952196305 scopus 로고    scopus 로고
    • Identification of phenol-degrading Nocardia sp. strain C-14-1 and characterization of its ring-cleavage 2,3-dioxygenase
    • Ma H., Li G., Fang P., Zhang Y., Xu D. Identification of phenol-degrading Nocardia sp. strain C-14-1 and characterization of its ring-cleavage 2,3-dioxygenase. International Journal of Biology 2010, 2:79-83.
    • (2010) International Journal of Biology , vol.2 , pp. 79-83
    • Ma, H.1    Li, G.2    Fang, P.3    Zhang, Y.4    Xu, D.5
  • 24
    • 0033064439 scopus 로고    scopus 로고
    • Conversion of 3-chlorocatechol by various catechol 2,3-dioxygenases and sequence analysis of the chlorocatechol dioxygenase region of Pseudomonas putida GJ31
    • Mars A.E., Kingman J., Kaschabek S.R., Reineke W., Janssen D.B. Conversion of 3-chlorocatechol by various catechol 2,3-dioxygenases and sequence analysis of the chlorocatechol dioxygenase region of Pseudomonas putida GJ31. Journal of Bacteriology 1999, 181:1309-1318.
    • (1999) Journal of Bacteriology , vol.181 , pp. 1309-1318
    • Mars, A.E.1    Kingman, J.2    Kaschabek, S.R.3    Reineke, W.4    Janssen, D.B.5
  • 25
    • 0033180041 scopus 로고    scopus 로고
    • Catechol 2,3-dioxygenase from the thermophilic, phenol-degrading Bacillus thermoleovorans strain A2 has unexpected low thermal stability
    • Milo R.E., Duffner F.M., Muller R. Catechol 2,3-dioxygenase from the thermophilic, phenol-degrading Bacillus thermoleovorans strain A2 has unexpected low thermal stability. Extremophiles 1999, 3:185-190.
    • (1999) Extremophiles , vol.3 , pp. 185-190
    • Milo, R.E.1    Duffner, F.M.2    Muller, R.3
  • 26
    • 0034963502 scopus 로고    scopus 로고
    • Enzymes and operons mediating xenobiotic degradation in bacteria
    • Mishira V., Lal R., Srinivas A.N. Enzymes and operons mediating xenobiotic degradation in bacteria. Critical Review in Microbiology 2001, 27:133-166.
    • (2001) Critical Review in Microbiology , vol.27 , pp. 133-166
    • Mishira, V.1    Lal, R.2    Srinivas, A.N.3
  • 28
    • 0038301610 scopus 로고    scopus 로고
    • Intersubunit interaction and catalytic activity of catechol 2,3-dioxygenases
    • Okuta A., Ohnishi K., Yagame S., Harayama S. Intersubunit interaction and catalytic activity of catechol 2,3-dioxygenases. Biochemical Journal 2003, 371:557-564.
    • (2003) Biochemical Journal , vol.371 , pp. 557-564
    • Okuta, A.1    Ohnishi, K.2    Yagame, S.3    Harayama, S.4
  • 29
    • 47249105112 scopus 로고    scopus 로고
    • Feasibility of m-cresol degradation using an indigenous mixed microbial culture with glucose as co-substrate
    • Pakshirajan K., Chugh D., Saravanan P. Feasibility of m-cresol degradation using an indigenous mixed microbial culture with glucose as co-substrate. Clean Technologies and Environmental Policy 2008, 10:303-308.
    • (2008) Clean Technologies and Environmental Policy , vol.10 , pp. 303-308
    • Pakshirajan, K.1    Chugh, D.2    Saravanan, P.3
  • 30
    • 0019778558 scopus 로고
    • 3,4-Dihydroxyphenylacetate 2,3-dioxygenase. A manganese (II) dioxygenase from Bacillus brevis
    • Que L., Widom J., Crawford R.L. 3,4-Dihydroxyphenylacetate 2,3-dioxygenase. A manganese (II) dioxygenase from Bacillus brevis. Journal of Biological Chemistry 1981, 256:10941-10944.
    • (1981) Journal of Biological Chemistry , vol.256 , pp. 10941-10944
    • Que, L.1    Widom, J.2    Crawford, R.L.3
  • 32
    • 0030008087 scopus 로고    scopus 로고
    • Three-dimensional structures of free form and two substrate complexes of an extradiol ring-cleavage type dioxygenase, the BphC enzyme from Pseudomonas sp. strain KKS102
    • Senda T., Sugiyama K., Narita H., Yamamoto T., Kimbara K., Fukuda M., Sato M., Yano K., Mitsui Y. Three-dimensional structures of free form and two substrate complexes of an extradiol ring-cleavage type dioxygenase, the BphC enzyme from Pseudomonas sp. strain KKS102. Journal of Molecular Biology 1996, 255:735-752.
    • (1996) Journal of Molecular Biology , vol.255 , pp. 735-752
    • Senda, T.1    Sugiyama, K.2    Narita, H.3    Yamamoto, T.4    Kimbara, K.5    Fukuda, M.6    Sato, M.7    Yano, K.8    Mitsui, Y.9
  • 34
    • 1642264726 scopus 로고    scopus 로고
    • Crystallographic comparison of manganes- and iron-dependent homoprotocatechuate 2,3-dioxyegnase
    • Vetting M.W., Wackett L.P., Que L., Lipscomb J.D., Ohlendorf D.H. Crystallographic comparison of manganes- and iron-dependent homoprotocatechuate 2,3-dioxyegnase. Journal of Bacteriology 2004, 186:1945-1958.
    • (2004) Journal of Bacteriology , vol.186 , pp. 1945-1958
    • Vetting, M.W.1    Wackett, L.P.2    Que, L.3    Lipscomb, J.D.4    Ohlendorf, D.H.5
  • 35
    • 10344235266 scopus 로고    scopus 로고
    • The role of the conserved residues His-246, His-199, and Tyr-255 in the catalysis of catechol 2,3-dioxygenase from Pseudomonas stutzeri OX1
    • Viggiani A., Siani L., Notomista E., Birolo L., Pucci P., Donato A. The role of the conserved residues His-246, His-199, and Tyr-255 in the catalysis of catechol 2,3-dioxygenase from Pseudomonas stutzeri OX1. Journal of Biological Chemistry 2004, 279:48630-48639.
    • (2004) Journal of Biological Chemistry , vol.279 , pp. 48630-48639
    • Viggiani, A.1    Siani, L.2    Notomista, E.3    Birolo, L.4    Pucci, P.5    Donato, A.6
  • 36
    • 0025317414 scopus 로고
    • Isolation and partial characterization of an extradiol non- haem iron dioxygenase which preferentially cleaves 3-methylcatechol
    • Wallis M.G., Chapman S.K. Isolation and partial characterization of an extradiol non- haem iron dioxygenase which preferentially cleaves 3-methylcatechol. Biochemical Journal 1990, 266:605-609.
    • (1990) Biochemical Journal , vol.266 , pp. 605-609
    • Wallis, M.G.1    Chapman, S.K.2
  • 37
    • 77952890947 scopus 로고    scopus 로고
    • Rational design of catechol 2,3-dioxygenase for improving the enzyme characteristic
    • Wei J., Zhou Y., Xu T., Lu B. Rational design of catechol 2,3-dioxygenase for improving the enzyme characteristic. Applied Biochemistry and Biotechnology 2010, 162:116-126.
    • (2010) Applied Biochemistry and Biotechnology , vol.162 , pp. 116-126
    • Wei, J.1    Zhou, Y.2    Xu, T.3    Lu, B.4
  • 39
    • 79251619522 scopus 로고    scopus 로고
    • Biodegradation characterization and kinetics of m-cresol by Lysinibacillus cresolivorans
    • Yao H., Ren Y., Wei Ch, Yue S. Biodegradation characterization and kinetics of m-cresol by Lysinibacillus cresolivorans. Water SA 2011, 37:15-20.
    • (2011) Water SA , vol.37 , pp. 15-20
    • Yao, H.1    Ren, Y.2    Wei, C.3    Yue, S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.