메뉴 건너뛰기




Volumn 270, Issue 7, 2003, Pages 1567-1577

Functional expression of the quinoline 2-oxidoreductase genes (qorMSL) in Pseudomonas putida KT2440 pUF1 and in P. putida 86-1 Δqor pUF1 and analysis of the Qor proteins

Author keywords

Expression cloning; Molybdenum hydroxylase; Molybdopterin cytosine dinucleotide; Pseudomonas sp.; Quinoline 2 oxidoreductase

Indexed keywords

DINUCLEOTIDE; MOLYBDENUM; MOLYBDENUM COMPLEX; MOLYBDOPTERIN; OXIDOREDUCTASE; OXYGENASE; QUINOLINE 2 OXIDOREDUCTASE; UNCLASSIFIED DRUG;

EID: 0037395528     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1033.2003.03526.x     Document Type: Article
Times cited : (29)

References (68)
  • 1
    • 0025641367 scopus 로고
    • Quinoline oxidoreductase from Pseudomonas putida: A molybdenum-containing enzyme
    • Bauder, R., Tshisuaka, B. & Lingens, F. (1990) Quinoline oxidoreductase from Pseudomonas putida: a molybdenum-containing enzyme. Biol. Chem. Hoppe-Seyler 371, 1137-1144.
    • (1990) Biol. Chem. Hoppe-Seyler , vol.371 , pp. 1137-1144
    • Bauder, R.1    Tshisuaka, B.2    Lingens, F.3
  • 2
    • 0027139907 scopus 로고
    • Quinoline oxidoreductase from Pseudomonas putida 86: An improved purification procedure and electron paramagnetic resonance spectroscopy
    • Tshisuaka, B., Kappl, R., Hüttermann, J. & Lingens, F. (1993) Quinoline oxidoreductase from Pseudomonas putida 86: an improved purification procedure and electron paramagnetic resonance spectroscopy. Biochemistry 32, 12928-12934.
    • (1993) Biochemistry , vol.32 , pp. 12928-12934
    • Tshisuaka, B.1    Kappl, R.2    Hüttermann, J.3    Lingens, F.4
  • 3
    • 0029983270 scopus 로고    scopus 로고
    • Quinaldine 4-oxidase from Arthrobacter sp. Rü6la, a versatile procaryotic molybdenum-containing hydroxylase active towards N-containing heterocyclic compounds and aromatic aldehydes
    • Stephan, I., Tshisuaka, B., Fetzner, S. & Lingens, F. (1996) Quinaldine 4-oxidase from Arthrobacter sp. Rü6la, a versatile procaryotic molybdenum-containing hydroxylase active towards N-containing heterocyclic compounds and aromatic aldehydes. Eur. J. Biochem. 236, 155-162.
    • (1996) Eur. J. Biochem. , vol.236 , pp. 155-162
    • Stephan, I.1    Tshisuaka, B.2    Fetzner, S.3    Lingens, F.4
  • 4
    • 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. (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
  • 5
    • 0000273676 scopus 로고    scopus 로고
    • The mononuclear molybdenum enzymes
    • Hille, R. (1996) The mononuclear molybdenum enzymes. Chem. Rev. 96, 2757-2816.
    • (1996) Chem. Rev. , vol.96 , pp. 2757-2816
    • Hille, R.1
  • 6
    • 0033288654 scopus 로고    scopus 로고
    • Molybdenum enzymes
    • Hille, R. (1999) Molybdenum enzymes. Essays Biochem. 34, 125-137.
    • (1999) Essays Biochem. , vol.34 , pp. 125-137
    • Hille, R.1
  • 7
    • 0036365692 scopus 로고    scopus 로고
    • Molybdenum enzymes containing the pyranopterin cofactor: An overview
    • Sigel, A. & Sigel, H., eds. of Met. Ions Biol. Syst. Marcel Dekker, New York
    • Hille, R. (2002) Molybdenum enzymes containing the pyranopterin cofactor: an overview. In Molybdenum and Tungsten. Their Roles in Biological Processes (Sigel, A. & Sigel, H., eds), pp. 187-226, Vol. 39 of Met. Ions Biol. Syst. Marcel Dekker, New York.
    • (2002) Molybdenum and Tungsten. Their Roles in Biological Processes , vol.39 , pp. 187-226
    • Hille, R.1
  • 8
    • 0036359682 scopus 로고    scopus 로고
    • The molybdenum-containing hydroxylases of nicotinate, isonicotinate, and nicotine
    • Sigel, A. & Sigel, H., eds. of Met. Ions Biol. Syst. Marcel Dekker, New York
    • Andreesen, J.R. & Fetzner, S. (2002) The molybdenum-containing hydroxylases of nicotinate, isonicotinate, and nicotine. In Molybdenum and Tungsten. Their Roles in Biological Processes (Sigel, A. & Sigel, H., eds), pp. 405-430, Vol. 39 of Met. Ions Biol. Syst. Marcel Dekker, New York.
    • (2002) Molybdenum and Tungsten. Their Roles in Biological Processes , vol.39 , pp. 405-430
    • Andreesen, J.R.1    Fetzner, S.2
  • 9
    • 0036365279 scopus 로고    scopus 로고
    • The molybdenum-containing hydroxylases of quinoline, isoquinoline, and quinaldine
    • Sigel, A. & Sigel, H., eds. of Met. Ions Biol. Syst. Marcel Dekker, New York
    • Kappl, R., Hüttermann, J. & Fetzner, S. (2002) The molybdenum-containing hydroxylases of quinoline, isoquinoline, and quinaldine. In Molybdenum and Tungsten. Their Roles in Biological Processes (Sigel, A. & Sigel, H., eds), pp. 481-537, Vol. 39 of Met. Ions Biol. Syst. Marcel Dekker, New York.
    • (2002) Molybdenum and Tungsten. Their Roles in Biological Processes , vol.39 , pp. 481-537
    • Kappl, R.1    Hüttermann, J.2    Fetzner, S.3
  • 10
    • 0030771511 scopus 로고    scopus 로고
    • Towards the reaction mechanism of xanthine oxidase from EPR studies
    • Bray, R.C. & Lowe, D.J. (1997) Towards the reaction mechanism of xanthine oxidase from EPR studies. Biochem. Soc. Trans. 25, 762-768.
    • (1997) Biochem. Soc. Trans. , vol.25 , pp. 762-768
    • Bray, R.C.1    Lowe, D.J.2
  • 12
    • 0002155983 scopus 로고    scopus 로고
    • Structure and function of the xanthine-oxidase family of molybdenum enzymes
    • Romão, M.J. & Huber, R. (1998) Structure and function of the xanthine-oxidase family of molybdenum enzymes. Structure Bonding 90, 69-95.
    • (1998) Structure Bonding , vol.90 , pp. 69-95
    • Romão, M.J.1    Huber, R.2
  • 13
    • 0035846965 scopus 로고    scopus 로고
    • Xanthine dehydrogenase from Pseudomonas putida 86: Specificity, oxidation-reduction potentials of its redox-active centers, and first EPR characterization
    • Parschat, K., Canne, C., Hüttermann, J., Kappl, R. & Fetzner, S. (2001) Xanthine dehydrogenase from Pseudomonas putida 86: Specificity, oxidation-reduction potentials of its redox-active centers, and first EPR characterization. Biochim. Biophys. Acta 1544, 151-165.
    • (2001) Biochim. Biophys. Acta , vol.1544 , pp. 151-165
    • Parschat, K.1    Canne, C.2    Hüttermann, J.3    Kappl, R.4    Fetzner, S.5
  • 14
    • 0026198605 scopus 로고
    • The molybdopterin cofactors of quinoline oxidoreductases from Pseudomonas putida 86 and Rhodococcus spec. B1 and of xanthine dehydrogenase from Pseudomonas putida 86
    • Hettrich, D., Peschke, B., Tshisuaka, B. & Lingens, F. (1991) The molybdopterin cofactors of quinoline oxidoreductases from Pseudomonas putida 86 and Rhodococcus spec. B1 and of xanthine dehydrogenase from Pseudomonas putida 86. Biol. Chem. Hoppe-Seyler 372, 513-517.
    • (1991) Biol. Chem. Hoppe-Seyler , vol.372 , pp. 513-517
    • Hettrich, D.1    Peschke, B.2    Tshisuaka, B.3    Lingens, F.4
  • 15
    • 0028286779 scopus 로고
    • Purification and characterization of isoquinoline 1-oxidoreductase from Pseudomonas diminuta 7, a novel molybdenum-containing hydroxylase
    • Lehmann, M., Tshisuaka, B., Fetzner, S., Röger, P. & Lingens, F. (1994) Purification and characterization of isoquinoline 1-oxidoreductase from Pseudomonas diminuta 7, a novel molybdenum-containing hydroxylase. J. Biol. Chem. 269, 11254-11260.
    • (1994) J. Biol. Chem. , vol.269 , pp. 11254-11260
    • Lehmann, M.1    Tshisuaka, B.2    Fetzner, S.3    Röger, P.4    Lingens, F.5
  • 16
    • 0027332213 scopus 로고
    • Catabolism of isonicotinate by Mycobacterium sp. INA1: Extended description of the pathway and purification of the molybdoenzyme isonicotinate dehydrogenase
    • Kretzer, A., Frunzke, K. & Andreesen, J.R. (1993) Catabolism of isonicotinate by Mycobacterium sp. INA1: extended description of the pathway and purification of the molybdoenzyme isonicotinate dehydrogenase. J. Gen. Microbiol. 139, 2763-2772.
    • (1993) J. Gen. Microbiol. , vol.139 , pp. 2763-2772
    • Kretzer, A.1    Frunzke, K.2    Andreesen, J.R.3
  • 17
    • 0345628018 scopus 로고    scopus 로고
    • 2-Hydroxyisonicotinate dehydrogenase isolated from Mycobacterium sp. INAI
    • Schräder, T., Hillebrand, C. & Andreesen, J.R. (1998) 2-Hydroxyisonicotinate dehydrogenase isolated from Mycobacterium sp. INAI. FEMS Microbiol. Lett. 164, 311-316.
    • (1998) FEMS Microbiol. Lett. , vol.164 , pp. 311-316
    • Schräder, T.1    Hillebrand, C.2    Andreesen, J.R.3
  • 18
    • 0000260778 scopus 로고
    • Biochemistry and physiology of aerobic carbon monoxide-utilizing bacteria
    • Meyer, O., Jacobitz, S. & Krüger, B. (1986) Biochemistry and physiology of aerobic carbon monoxide-utilizing bacteria. FEMS Microbiol. Rev. 39, 161-179.
    • (1986) FEMS Microbiol. Rev. , vol.39 , pp. 161-179
    • Meyer, O.1    Jacobitz, S.2    Krüger, B.3
  • 19
    • 0002798821 scopus 로고
    • Biochemistry of the aerobic utilization of carbon monoxide
    • Murrell, J.C. & Kelly, D.P., eds. Intercept Ltd, Andover, Hampshire, UK
    • 1 Compounds (Murrell, J.C. & Kelly, D.P., eds), pp. 433-459. Intercept Ltd, Andover, Hampshire, UK.
    • (1993) 1 Compounds , pp. 433-459
    • Meyer, O.1    Frunzke, K.2    Mörsdorf, G.3
  • 20
    • 0037059062 scopus 로고    scopus 로고
    • Catalysis at a dinuclear [CuSMo (=O) OH] cluster in a CO dehydrogenase resolved at 1.1-Å resolution
    • Dobbek, H., Gremer, L., Kiefersauer, R., Huber, R. & Meyer, O. (2002) Catalysis at a dinuclear [CuSMo (=O) OH] cluster in a CO dehydrogenase resolved at 1.1-Å resolution. Proc. Natl Acad. Sci. USA 99, 15971-15976.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 15971-15976
    • Dobbek, H.1    Gremer, L.2    Kiefersauer, R.3    Huber, R.4    Meyer, O.5
  • 22
    • 0035161477 scopus 로고    scopus 로고
    • Structure refinement of the aldehyde oxidoreductase from Desulfovibrio gigas (MOP) at 1.28 Å
    • Rebelo, J.M., Dias, J.M., Huber, R., Moura, J.J.G. & Romão, M.J. (2001) Structure refinement of the aldehyde oxidoreductase from Desulfovibrio gigas (MOP) at 1.28 Å. J. Biol. Inorg. Chem. 6, 791-800.
    • (2001) J. Biol. Inorg. Chem. , vol.6 , pp. 791-800
    • Rebelo, J.M.1    Dias, J.M.2    Huber, R.3    Moura, J.J.G.4    Romão, M.J.5
  • 23
    • 0029840683 scopus 로고    scopus 로고
    • Cloning, expression, and sequence analysis of the three genes encoding quinoline 2-oxidoreductase, a molybdenum-containing hydroxylase from Pseudomonas putida 86
    • Bläse, M., Bruntner, C., Tshisuaka, B., Fetzner, S. & Lingens, F. (1996) Cloning, expression, and sequence analysis of the three genes encoding quinoline 2-oxidoreductase, a molybdenum-containing hydroxylase from Pseudomonas putida 86. J. Biol. Chem. 271, 23068-23079.
    • (1996) J. Biol. Chem. , vol.271 , pp. 23068-23079
    • Bläse, M.1    Bruntner, C.2    Tshisuaka, B.3    Fetzner, S.4    Lingens, F.5
  • 24
    • 0030857695 scopus 로고    scopus 로고
    • Comparative EPR and redox studies of three prokaryotic enzymes of the xanthine oxidase family: Quinoline 2-oxidoreductase, quinaldine 4-oxidase, and isoquinoline 1-oxidoreductase
    • Canne, C., Stephan, I., Finsterbusch, J., Lingens, F., Kappl, R., Fetzner, S. & Hüttermann, J. (1997) Comparative EPR and redox studies of three prokaryotic enzymes of the xanthine oxidase family: quinoline 2-oxidoreductase, quinaldine 4-oxidase, and isoquinoline 1-oxidoreductase. Biochemistry 36, 9780-9790.
    • (1997) Biochemistry , vol.36 , pp. 9780-9790
    • Canne, C.1    Stephan, I.2    Finsterbusch, J.3    Lingens, F.4    Kappl, R.5    Fetzner, S.6    Hüttermann, J.7
  • 25
    • 0345624496 scopus 로고    scopus 로고
    • Kinetics and interactions of molybdenum and iron-sulfur centers in bacterial enzymes of the xanthine oxidase family: Mechanistic implications
    • Canne, C., Lowe, D.J., Fetzner, S., Adams, B., Smith, A.T., Kappl, R., Bray, R.C. & Hiittermann, J. (1999) Kinetics and interactions of molybdenum and iron-sulfur centers in bacterial enzymes of the xanthine oxidase family: mechanistic implications. Biochemistry 38, 14077-14087.
    • (1999) Biochemistry , vol.38 , pp. 14077-14087
    • Canne, C.1    Lowe, D.J.2    Fetzner, S.3    Adams, B.4    Smith, A.T.5    Kappl, R.6    Bray, R.C.7    Hiittermann, J.8
  • 26
    • 0028140249 scopus 로고
    • Molecular cloning of rat liver sulfite oxidase. Expression of a eukaryotic Mo-pterin-containing enzyme in Escherichia coli
    • Garrett, R.M. & Rajagopalan, K.V. (1994) Molecular cloning of rat liver sulfite oxidase. Expression of a eukaryotic Mo-pterin-containing enzyme in Escherichia coli. J. Biol. Chem. 269, 272-276.
    • (1994) J. Biol. Chem. , vol.269 , pp. 272-276
    • Garrett, R.M.1    Rajagopalan, K.V.2
  • 27
    • 0031022332 scopus 로고    scopus 로고
    • Biotin sulfoxide reductase. Heterologous expression and characterization of a functional molybdopterin guanine dinucleotide-containing enzyme
    • Pollock, V.V. & Barber, M.J. (1997) Biotin sulfoxide reductase. Heterologous expression and characterization of a functional molybdopterin guanine dinucleotide-containing enzyme. J. Biol. Chem. 272, 3355-3362.
    • (1997) J. Biol. Chem. , vol.272 , pp. 3355-3362
    • Pollock, V.V.1    Barber, M.J.2
  • 28
    • 0034669320 scopus 로고    scopus 로고
    • Optimization of expression of human sulfite oxidase and its molybdenum domain
    • Temple, C.A., Graf, T.N. & Rajagopalan, K.V. (2000) Optimization of expression of human sulfite oxidase and its molybdenum domain. Arch. Biochem. Biophys. 383, 281-287.
    • (2000) Arch. Biochem. Biophys. , vol.383 , pp. 281-287
    • Temple, C.A.1    Graf, T.N.2    Rajagopalan, K.V.3
  • 29
    • 0025345938 scopus 로고
    • Cloning and expression of the carbon monoxide dehydrogenase genes from Pseudomonas thermocarboxydovorans strain C2
    • Black, G.W., Lyons, C.M., Williams, E., Colby, J., Kehoe, M. & O'Reilly, C. (1990) Cloning and expression of the carbon monoxide dehydrogenase genes from Pseudomonas thermocarboxydovorans strain C2. FEMS Microbiol. Lett. 70, 249-254.
    • (1990) FEMS Microbiol. Lett. , vol.70 , pp. 249-254
    • Black, G.W.1    Lyons, C.M.2    Williams, E.3    Colby, J.4    Kehoe, M.5    O'Reilly, C.6
  • 30
    • 0025835008 scopus 로고
    • Molybdenum cofactor biosynthesis in Escherichia coli. Requirement of the chlB gene product for the formation of molybdopterin guanine dinucleotide
    • Johnson, J.L., Indermaur, L.W. & Rajagopalan, K.V. (1991) Molybdenum cofactor biosynthesis in Escherichia coli. Requirement of the chlB gene product for the formation of molybdopterin guanine dinucleotide. J. Biol. Chem. 266, 12140-12145.
    • (1991) J. Biol. Chem. , vol.266 , pp. 12140-12145
    • Johnson, J.L.1    Indermaur, L.W.2    Rajagopalan, K.V.3
  • 31
    • 0028338273 scopus 로고
    • Isolation of protein FA, a product of the mob locus required for molybdenum cofactor biosynthesis in Escherichia coll
    • Palmer, T., Vasishta, A., Whitty, P.W. & Boxer, D.H. (1994) Isolation of protein FA, a product of the mob locus required for molybdenum cofactor biosynthesis in Escherichia coll. Eur. J. Biochem. 222, 687-692.
    • (1994) Eur. J. Biochem. , vol.222 , pp. 687-692
    • Palmer, T.1    Vasishta, A.2    Whitty, P.W.3    Boxer, D.H.4
  • 32
    • 16744365314 scopus 로고    scopus 로고
    • The molybdenum cofactor biosynthesis protein MobA from Rhodobacter capsulatus is required for the activity of molybdenum enzymes containing MGD, but not for xanthine dehydrogenase harboring the MPT cofactor
    • Leimkühler, S. & Klipp, W. (1999) The molybdenum cofactor biosynthesis protein MobA from Rhodobacter capsulatus is required for the activity of molybdenum enzymes containing MGD, but not for xanthine dehydrogenase harboring the MPT cofactor. FEMS Microbiol. Lett. 174, 239-246.
    • (1999) FEMS Microbiol. Lett. , vol.174 , pp. 239-246
    • Leimkühler, S.1    Klipp, W.2
  • 33
    • 0034435586 scopus 로고    scopus 로고
    • Crystal structure of the molybdenum cofactor biosynthesis protein MobA from Escherichia coli at near-atomic resolution
    • Stevenson, C.E.M., Sargent, F., Buchanan, G., Palmer, T. & Lawson, D.M. (2000) Crystal structure of the molybdenum cofactor biosynthesis protein MobA from Escherichia coli at near-atomic resolution. Structure Fold. Res. 8, 1115-1125.
    • (2000) Structure Fold. Res. , vol.8 , pp. 1115-1125
    • Stevenson, C.E.M.1    Sargent, F.2    Buchanan, G.3    Palmer, T.4    Lawson, D.M.5
  • 34
    • 0034704163 scopus 로고    scopus 로고
    • The crystal structure of the Escherichia coli MobA protein provides insight into molybdopterin guanine dinucleotide biosynthesis
    • Lake, M.W., Temple, C.A., Rajagopalan, K.V. & Schindelin, H. (2000) The crystal structure of the Escherichia coli MobA protein provides insight into molybdopterin guanine dinucleotide biosynthesis. J. Biol. Chem. 275, 40211-40217.
    • (2000) J. Biol. Chem. , vol.275 , pp. 40211-40217
    • Lake, M.W.1    Temple, C.A.2    Rajagopalan, K.V.3    Schindelin, H.4
  • 35
    • 0034704126 scopus 로고    scopus 로고
    • Mechanism of assembly of the bis (molybdopterin guanine dinucleotide) molybdenum cofactor in Rhodobacter sphaeroides dimethyl sulfoxide reductase
    • Temple, C.A. & Rajagopalan, K.V. (2000) Mechanism of assembly of the bis (molybdopterin guanine dinucleotide) molybdenum cofactor in Rhodobacter sphaeroides dimethyl sulfoxide reductase. J. Biol. Chem. 275, 40202-40210.
    • (2000) J. Biol. Chem. , vol.275 , pp. 40202-40210
    • Temple, C.A.1    Rajagopalan, K.V.2
  • 36
    • 0034928544 scopus 로고    scopus 로고
    • Characterization of the mob locus of Rhodobacter sphaeroides WS8: mobA is the only gene required for molybdopterin guanine dinucleotide synthesis
    • Buchanan, G., Kuper, J., Mendel, R.R., Schwarz, G. & Palmer, T. (2001) Characterization of the mob locus of Rhodobacter sphaeroides WS8: mobA is the only gene required for molybdopterin guanine dinucleotide synthesis. Arch. Microbiol. 176, 62-68.
    • (2001) Arch. Microbiol. , vol.176 , pp. 62-68
    • Buchanan, G.1    Kuper, J.2    Mendel, R.R.3    Schwarz, G.4    Palmer, T.5
  • 37
    • 0037161198 scopus 로고    scopus 로고
    • Expression of the ior AB genes from Brevundimonas diminuta 7 encoding the molybdenum hydroxylase isoquinoline 1-oxidoreductase in Pseudomonas putida
    • Israel, I., Sohni, M. & Fetzner, S. (2002) Expression of the ior AB genes from Brevundimonas diminuta 7 encoding the molybdenum hydroxylase isoquinoline 1-oxidoreductase in Pseudomonas putida. FEMS Microbiol. Lett. 210, 123-127.
    • (2002) FEMS Microbiol. Lett. , vol.210 , pp. 123-127
    • Israel, I.1    Sohni, M.2    Fetzner, S.3
  • 40
    • 0023948010 scopus 로고
    • High efficiency transformation of E. coli by high voltage electroporation
    • Dower, W.J., Miller, J.F. & Ragsdale, C.W. (1988) High efficiency transformation of E. coli by high voltage electroporation. Nucleic Acids Res. 16, 6127-6145.
    • (1988) Nucleic Acids Res. , vol.16 , pp. 6127-6145
    • Dower, W.J.1    Miller, J.F.2    Ragsdale, C.W.3
  • 42
    • 0020442864 scopus 로고
    • The pUC plasmids, an M13mp7-derived system for insertion mutagenesis and sequencing with synthetic universal primers
    • Vieira, J. & Messing, J. (1982) The pUC plasmids, an M13mp7-derived system for insertion mutagenesis and sequencing with synthetic universal primers. Gene 19, 259-268.
    • (1982) Gene , vol.19 , pp. 259-268
    • Vieira, J.1    Messing, J.2
  • 43
    • 0020371498 scopus 로고
    • Nucleotide sequence and exact localization of the neomycin phosphotransferase gene from transposon Tn5
    • Beck, E., Ludwig, G., Auerswald, E.A., Reiss, B. & Schaller, H. (1982) Nucleotide sequence and exact localization of the neomycin phosphotransferase gene from transposon Tn5. Gene 19, 327-336.
    • (1982) Gene , vol.19 , pp. 327-336
    • Beck, E.1    Ludwig, G.2    Auerswald, E.A.3    Reiss, B.4    Schaller, H.5
  • 44
    • 0021027842 scopus 로고
    • A broad host range mobilization system for in vivo genetic engineering: Transposon mutagenesis in Gram negative bacteria
    • Simon, R., Priefer, U. & Pühler, A. (1983) A broad host range mobilization system for in vivo genetic engineering: transposon mutagenesis in Gram negative bacteria. Biol/Technology 1, 784-791.
    • (1983) Biol/Technology , vol.1 , pp. 784-791
    • Simon, R.1    Priefer, U.2    Pühler, A.3
  • 45
    • 0023952240 scopus 로고
    • Genetic characterization and sequence analysis of the duplicated nifA/nifB gene region of Rhodobacter capsulatus
    • Masepohl, B., Klipp, W. & Pühler, A. (1988) Genetic characterization and sequence analysis of the duplicated nifA/nifB gene region of Rhodobacter capsulatus. Mol. Gen. Genet. 212, 27-37.
    • (1988) Mol. Gen. Genet , vol.212 , pp. 27-37
    • Masepohl, B.1    Klipp, W.2    Pühler, A.3
  • 46
    • 0021286821 scopus 로고
    • A physical map of pPH1JI and pJB4JI
    • Hirsch, P.R. & Beringer, J.E. (1984) A physical map of pPH1JI and pJB4JI. Plasmid 12, 39-141.
    • (1984) Plasmid , vol.12 , pp. 39-141
    • Hirsch, P.R.1    Beringer, J.E.2
  • 47
    • 0000925040 scopus 로고
    • Colony hybridization: A method for the isolation of cloned DNAs that contain a specific gene
    • Grunstein, M. & Hogness, D.S. (1975) Colony hybridization: a method for the isolation of cloned DNAs that contain a specific gene. Proc. Natl Acad. Sci. USA 72, 3961-3965.
    • (1975) Proc. Natl. Acad. Sci. USA , vol.72 , pp. 3961-3965
    • Grunstein, M.1    Hogness, D.S.2
  • 48
    • 0001232852 scopus 로고
    • One-dimensional polyacrylamide gel electrophoresis
    • (Hames, B.D. & Rickwood, D., eds), 2nd edn. IRL Press (Oxford University Press), Oxford
    • Hames, B.D. (1990) One-dimensional polyacrylamide gel electrophoresis. In Gel Electrophoresis of Proteins - a Practical Approach (Hames, B.D. & Rickwood, D., eds), 2nd edn, pp. 1-147 IRL Press (Oxford University Press), Oxford.
    • (1990) Gel Electrophoresis of Proteins - A Practical Approach , pp. 1-147
    • Hames, B.D.1
  • 49
    • 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
  • 50
    • 0345144158 scopus 로고    scopus 로고
    • Immunoblotting
    • Caponi, L. & Migliorini, P., eds. Springer, Berlin, Heidelberg, New York
    • Caponi, L. & Migliorini, P. (1999) Immunoblotting. In Antibody Usage in the Laboratory (Caponi, L. & Migliorini, P., eds), p. 42. Springer, Berlin, Heidelberg, New York.
    • (1999) Antibody Usage in the Laboratory , pp. 42
    • Caponi, L.1    Migliorini, P.2
  • 51
    • 0029917011 scopus 로고    scopus 로고
    • Linearization of the Bradford protein assay increases its sensitivity: Theoretical and experimental studies
    • Zor, T. & Selinger, Z. (1996) Linearization of the Bradford protein assay increases its sensitivity: theoretical and experimental studies. Anal. Biochem. 236, 302-308.
    • (1996) Anal. Biochem. , vol.236 , pp. 302-308
    • Zor, T.1    Selinger, Z.2
  • 52
    • 0030942268 scopus 로고    scopus 로고
    • Construction and use of a versatile set of broad-host-range cloning and expression vectors based on the RK2 replicon
    • Blatny, J.M., Brautaset, T., Winther-Larsen, H.C., Haugan, K. & Valla, S. (1997) Construction and use of a versatile set of broad-host-range cloning and expression vectors based on the RK2 replicon. Appl. Environ. Microbiol. 63, 370-379.
    • (1997) Appl. Environ. Microbiol. , vol.63 , pp. 370-379
    • Blatny, J.M.1    Brautaset, T.2    Winther-Larsen, H.C.3    Haugan, K.4    Valla, S.5
  • 55
    • 0036083835 scopus 로고    scopus 로고
    • AraC-Xy1S database: A family of positive transcriptional regulators in bacteria
    • Tobes, R. & Ramos, J.L. (2002) AraC-Xy1S database: a family of positive transcriptional regulators in bacteria. Nucleic Acids Res. 30, 318-321.
    • (2002) Nucleic Acids Res. , vol.30 , pp. 318-321
    • Tobes, R.1    Ramos, J.L.2
  • 56
    • 0036190750 scopus 로고    scopus 로고
    • Specific and global regulation of genes associated with the degradation of aromatic compounds in bacteria
    • Gerischer, U. (2002) Specific and global regulation of genes associated with the degradation of aromatic compounds in bacteria. J. Mol. Microbiol. Biotechnol. 4, 111-121.
    • (2002) J. Mol. Microbiol. Biotechnol. , vol.4 , pp. 111-121
    • Gerischer, U.1
  • 57
    • 0030977557 scopus 로고    scopus 로고
    • 2-Oxo-1,2-dihydroquinoline 8-monooxygenase: Phylogenetic relationship to other multicomponent nonheme iron oxygenases
    • Rosche, B., Tshisuaka, B., Hauer, B., Lingens, F. & Fetzner, S. (1997) 2-Oxo-1,2-dihydroquinoline 8-monooxygenase: phylogenetic relationship to other multicomponent nonheme iron oxygenases. J. Bacteriol. 179, 3549-3554.
    • (1997) J. Bacteriol. , vol.179 , pp. 3549-3554
    • Rosche, B.1    Tshisuaka, B.2    Hauer, B.3    Lingens, F.4    Fetzner, S.5
  • 58
    • 0036364864 scopus 로고    scopus 로고
    • Biosynthesis and molecular biology of the molybdenum cofactor (Moco)
    • Sigel, A. & Sigel, H., eds. of Met. Ions Biol. Syst. Marcel Dekker, NY, USA
    • Mendel, R.R. & Schwarz, G. (2002) Biosynthesis and molecular biology of the molybdenum cofactor (Moco). In: Molybdenum and Tungsten. Their Roles in Biological Processes (Sigel, A. & Sigel, H., eds), pp. 317-368, Vol. 39 of Met. Ions Biol. Syst. Marcel Dekker, NY, USA.
    • (2002) Molybdenum and Tungsten. Their Roles in Biological Processes , vol.39 , pp. 317-368
    • Mendel, R.R.1    Schwarz, G.2
  • 59
    • 0002626094 scopus 로고
    • Enzymatic hydroxylations in industrial application
    • Kulla, H.G. (1991) Enzymatic hydroxylations in industrial application. Chimia 45, 81-85.
    • (1991) Chimia , vol.45 , pp. 81-85
    • Kulla, H.G.1
  • 60
    • 24444470309 scopus 로고
    • Manufacture of carbostyril and/or 6-hydroxycarbostyril with Pseudomonas species
    • Japanese Patent 05 304 973 [93 304 973]
    • Kawashima, H., Sueyoshi, H. & (Nippon Steel Corp, Japan) (1993) Manufacture of carbostyril and/or 6-hydroxycarbostyril with Pseudomonas species. Japanese Patent 05 304 973 [93 304 973], Chem. Abstract. (1994), 120, 132464K.
    • (1993) Chem. Abstract. , vol.120
    • Kawashima, H.1    Sueyoshi, H.2
  • 61
    • 0030664822 scopus 로고    scopus 로고
    • Isolation of new 6-methylnicotinic-acid-degrading bacteria, one of which catalyses the regioselective hydroxylation of nicotinic acid at position C2
    • Tinschert, A., Kiener, A., Heinzmann, K. & Tschech, A. (1997) Isolation of new 6-methylnicotinic-acid-degrading bacteria, one of which catalyses the regioselective hydroxylation of nicotinic acid at position C2. Arch. Microbiol. 168, 355-361.
    • (1997) Arch. Microbiol. , vol.168 , pp. 355-361
    • Tinschert, A.1    Kiener, A.2    Heinzmann, K.3    Tschech, A.4
  • 62
    • 0034003090 scopus 로고    scopus 로고
    • Novel regioselective hydroxylations of pyridine carboxylic acids at position C2 and pyrazine carboxylic acids at position C3
    • Tinschert, A., Tschech, A., Heinzmann, K. & Kiener, A. (2000) Novel regioselective hydroxylations of pyridine carboxylic acids at position C2 and pyrazine carboxylic acids at position C3. Appl. Microbiol. Biotechnol. 53, 185-195.
    • (2000) Appl. Microbiol. Biotechnol. , vol.53 , pp. 185-195
    • Tinschert, A.1    Tschech, A.2    Heinzmann, K.3    Kiener, A.4
  • 63
    • 0032516404 scopus 로고    scopus 로고
    • Microbial production of 2-hydroxynicotinic acid from nicotinic acid by intact cells of MCI3289
    • Ueda, M. & Sashida, R. (1998) Microbial production of 2-hydroxynicotinic acid from nicotinic acid by intact cells of MCI3289. J. Mol. Catal. B: Enzym. 4, 199-204.
    • (1998) J. Mol. Catal. B: Enzym. , vol.4 , pp. 199-204
    • Ueda, M.1    Sashida, R.2
  • 64
    • 0001270261 scopus 로고    scopus 로고
    • Design by directed evolution
    • Arnold, F.H. (1998) Design by directed evolution. Acc. Chem. Res. 31, 125-131.
    • (1998) Acc. Chem. Res. , vol.31 , pp. 125-131
    • Arnold, F.H.1
  • 66
    • 0001952918 scopus 로고    scopus 로고
    • Superior biocatalysts by directed evolution
    • Reetz, M.T. & Jaeger, K.-E. (1999) Superior biocatalysts by directed evolution. Topics Curr. Chem. 200, 31-57.
    • (1999) Topics Curr. Chem. , vol.200 , pp. 31-57
    • Reetz, M.T.1    Jaeger, K.-E.2
  • 67
    • 0019805971 scopus 로고
    • Specific-purpose plasmid cloning vectors. II. Broad host range, high copy number, RSF1010-derived vectors, and a host-vector system for gene cloning in Pseudomonas
    • Bagdasarian, M., Lurz, R., Rückert, B., Franklin, F.C.H., Bagdasarian, M.M., Frey, J. & Timmis, K.N. (1981) Specific-purpose plasmid cloning vectors. II. Broad host range, high copy number, RSF1010-derived vectors, and a host-vector system for gene cloning in Pseudomonas. Gene 16, 237-247
    • (1981) Gene , vol.16 , pp. 237-247
    • Bagdasarian, M.1    Lurz, R.2    Rückert, B.3    Franklin, F.C.H.4    Bagdasarian, M.M.5    Frey, J.6    Timmis, K.N.7
  • 68
    • 85005514339 scopus 로고
    • Microbial metabolism of quinoline and related compounds. I. Isolation and characterization of quinoline-degrading bacteria
    • Schwarz, G., Senghas, E., Erben, A., Schäfer, B., Lingens, F. & Höke, H. (1988) Microbial metabolism of quinoline and related compounds. I. Isolation and characterization of quinoline-degrading bacteria. Syst. Appl. Microbiol. 10, 185-190.
    • (1988) Syst. Appl. Microbiol. , vol.10 , pp. 185-190
    • Schwarz, G.1    Senghas, E.2    Erben, A.3    Schäfer, B.4    Lingens, F.5    Höke, H.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.