메뉴 건너뛰기




Volumn 284, Issue 5, 1998, Pages 1323-1339

Gene structures and properties of enzymes of the plasmid-encoded nicotine catabolism of Arthrobacter nicotinovorans

Author keywords

6 Hydroxy D nicotine oxidase; 6 Hydroxy L nicotine oxidase; Ketone dehydrogenase; Sequence homologies; phage library

Indexed keywords

6 HYDROXYNICOTINE OXIDASE; KETONE DEHYDROGENASE; OXIDOREDUCTASE; UNCLASSIFIED DRUG;

EID: 0032545185     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1998.2227     Document Type: Article
Times cited : (50)

References (86)
  • 2
    • 0025143109 scopus 로고
    • 2-dependent type. Amino acid sequence of rat liver xanthine dehydrogenase and identification of the cleavage sites of the enzyme protein during irreversible conversion by trypsin
    • 2-dependent type. Amino acid sequence of rat liver xanthine dehydrogenase and identification of the cleavage sites of the enzyme protein during irreversible conversion by trypsin. J. Biol. Chem. 265, 14170-14175.
    • (1990) J. Biol. Chem. , vol.265 , pp. 14170-14175
    • Amaya, Y.1    Yamazaki, K.2    Sato, M.3    Noda, K.4    Nishino, T.5    Nishino, T.6
  • 4
    • 46149141992 scopus 로고
    • Cloning and analysis of the promoter region of the erythromycin resistance gene (ermE) of Streptomyces erythraeus
    • Bibb, M. J., Janssen, G. R. & Ward, J. M. (1985). Cloning and analysis of the promoter region of the erythromycin resistance gene (ermE) of Streptomyces erythraeus. Gene, 41, E357-E368.
    • (1985) Gene , vol.41
    • Bibb, M.J.1    Janssen, G.R.2    Ward, J.M.3
  • 5
    • 0018800089 scopus 로고
    • A rapid alkaline extraction procedure for screening recombinant plasmid DNA
    • Birnboim, H. C. & Doly, J. (1979). A rapid alkaline extraction procedure for screening recombinant plasmid DNA. Nucl. Acids Res. 7, 1513-1523.
    • (1979) Nucl. Acids Res. , vol.7 , pp. 1513-1523
    • Birnboim, H.C.1    Doly, J.2
  • 6
    • 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
    • Blaese, 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
    • Blaese, M.1    Bruntner, C.2    Tshisuaka, B.3    Fetzner, S.4    Lingens, F.5
  • 7
    • 0021281134 scopus 로고
    • Isolation and partial characterization of plasmid DNA from Arthrobacter oxidans
    • Brandsch, R. & Decker, K. (1984). Isolation and partial characterization of plasmid DNA from Arthrobacter oxidans. Arch. Microbiol. 138, 15-17.
    • (1984) Arch. Microbiol. , vol.138 , pp. 15-17
    • Brandsch, R.1    Decker, K.2
  • 8
    • 0023410567 scopus 로고
    • 6-Hydroxy-D-nicotine oxidase of Arthrobacter oxidans; gene structure of the flavoenzyme and its relationship to 6-hydroxy-L-nicotine oxidase
    • Brandsch, R., Hinkkanen, A., Mauch, L., Nagursky, H. & Decker, K. (1987). 6-Hydroxy-D-nicotine oxidase of Arthrobacter oxidans; gene structure of the flavoenzyme and its relationship to 6-hydroxy-L-nicotine oxidase. Eur. J. Biochem. 167, 315-320.
    • (1987) Eur. J. Biochem. , vol.167 , pp. 315-320
    • Brandsch, R.1    Hinkkanen, A.2    Mauch, L.3    Nagursky, H.4    Decker, K.5
  • 9
    • 0015515033 scopus 로고
    • Covalently bound flavin in 6-hydroxy-D-nicotine oxidase of Arthrobacter oxidans
    • Brühmüller, M., Möhler, H. & Decker, K. (1972). Covalently bound flavin in 6-hydroxy-D-nicotine oxidase of Arthrobacter oxidans. Eur. J. Biochem. 29, 143-151.
    • (1972) Eur. J. Biochem. , vol.29 , pp. 143-151
    • Brühmüller, M.1    Möhler, H.2    Decker, K.3
  • 11
    • 0028559727 scopus 로고
    • Cloning of a novel monoamine oxidase cDNA from trout liver
    • Chen, K., Wu, H. F., Grimsby, J. & Shih, J. C. (1994). Cloning of a novel monoamine oxidase cDNA from trout liver. Mol. Pharmacol. 46, 1226-1233.
    • (1994) Mol. Pharmacol. , vol.46 , pp. 1226-1233
    • Chen, K.1    Wu, H.F.2    Grimsby, J.3    Shih, J.C.4
  • 12
    • 0029914165 scopus 로고    scopus 로고
    • Synonymous substitutions in the Xdh gene of Drosophila: Heterogeneous distribution along the coding region
    • Comeron, J. M. & Aguade, M. (1996). Synonymous substitutions in the Xdh gene of Drosophila: heterogeneous distribution along the coding region. Genetics, 144, 1053-1062.
    • (1996) Genetics , vol.144 , pp. 1053-1062
    • Comeron, J.M.1    Aguade, M.2
  • 13
    • 0014263350 scopus 로고
    • Purification and properties of L-6-hydroxynicotine oxidase
    • Dai, V. D., Decker, K. & Sund, H. (1968). Purification and properties of L-6-hydroxynicotine oxidase. Eur. J. Biochem. 4, 95-102.
    • (1968) Eur. J. Biochem. , vol.4 , pp. 95-102
    • Dai, V.D.1    Decker, K.2    Sund, H.3
  • 14
    • 0013853329 scopus 로고
    • Induction and purification of stereospecific nicotine oxidizing enzymes from Arthrobacter oxydans
    • Decker, K. & Bleeg, H. (1965). Induction and purification of stereospecific nicotine oxidizing enzymes from Arthrobacter oxydans. Biochim. Biophys. Acta, 105, 313-334.
    • (1965) Biochim. Biophys. Acta , vol.105 , pp. 313-334
    • Decker, K.1    Bleeg, H.2
  • 15
    • 0025903584 scopus 로고
    • Flavoproteins with a covalent histidyl(N3)-8α-riboflavin linkage
    • Decker, K. & Brandsch, R. (1991). Flavoproteins with a covalent histidyl(N3)-8α-riboflavin linkage. Bio-Factors, 3, 69-81.
    • (1991) Bio-Factors , vol.3 , pp. 69-81
    • Decker, K.1    Brandsch, R.2
  • 16
    • 0030013135 scopus 로고    scopus 로고
    • Properties of xanthine dehydrogenase variants from rosy mutant strains of Drosophila melanogaster and their relevance to the enzyme's structure and mechanism
    • Doyle, W. A., Burke, J. F., Chovnick, A., Dutton, F. L., Whittle, R. S. & Bray, R. C. (1996). Properties of xanthine dehydrogenase variants from rosy mutant strains of Drosophila melanogaster and their relevance to the enzyme's structure and mechanism. Eur. J. Biochem. 239, 782-795.
    • (1996) Eur. J. Biochem. , vol.239 , pp. 782-795
    • Doyle, W.A.1    Burke, J.F.2    Chovnick, A.3    Dutton, F.L.4    Whittle, R.S.5    Bray, R.C.6
  • 17
    • 0000468708 scopus 로고
    • Über den Abbau des Nicotins durch Bakterienenzyme II, Isolierung und Charakterisierung eines nicotinabbauenden Bodenbakteriums
    • Eberwein, H., Gries, F. A. & Decker, K. (1961). Über den Abbau des Nicotins durch Bakterienenzyme II, Isolierung und Charakterisierung eines nicotinabbauenden Bodenbakteriums. Hoppe-Seyler's Z. Physiol. Chem. 323, 236-248.
    • (1961) Hoppe-Seyler's Z. Physiol. Chem. , vol.323 , pp. 236-248
    • Eberwein, H.1    Gries, F.A.2    Decker, K.3
  • 18
    • 0027248058 scopus 로고
    • A modified alkaline lysis method for the preparation of highly purified plasmid DNA from Escherichia coli
    • Feliciello, I. & Chinali, G. (1993). A modified alkaline lysis method for the preparation of highly purified plasmid DNA from Escherichia coli. Anal. Biochem. 212, 394-402.
    • (1993) Anal. Biochem. , vol.212 , pp. 394-402
    • Feliciello, I.1    Chinali, G.2
  • 19
    • 0027620339 scopus 로고
    • Microbial metabolism of quinoline and related compounds. XVII. Purification and some properties of the molybdenum- and iron-containing quinaldic acid 4-oxidoreductase from Serratia marcescens 2CC-1
    • Fetzner, S. & Lingens, F. (1993). Microbial metabolism of quinoline and related compounds. XVII. Purification and some properties of the molybdenum- and iron-containing quinaldic acid 4-oxidoreductase from Serratia marcescens 2CC-1. Biol. Chem. Hoppe-Seyler, 374, 363-376.
    • (1993) Biol. Chem. Hoppe-Seyler , vol.374 , pp. 363-376
    • Fetzner, S.1    Lingens, F.2
  • 20
    • 0031033229 scopus 로고    scopus 로고
    • 4-Hydroxybenzoyl-coenzyme a reductase (dehydroxylating) is required for anaerobic degradation of 4-hydroxybenzoate by Khodopseudomonas palustris and shares features with molybdenum-containing hydroxylases
    • Gibson, J., Dispensa, M. & Harwood, C. S. (1997). 4-Hydroxybenzoyl-coenzyme A reductase (dehydroxylating) is required for anaerobic degradation of 4-hydroxybenzoate by Khodopseudomonas palustris and shares features with molybdenum-containing hydroxylases. J. Bacteriol. 179, 634-642.
    • (1997) J. Bacteriol. , vol.179 , pp. 634-642
    • Gibson, J.1    Dispensa, M.2    Harwood, C.S.3
  • 21
    • 0028938642 scopus 로고
    • Cloning and molecular characterization of hxA, the gene coding for the xanthine dehydrogenase (purine hydrolase I) of Aspergillus nidulans
    • Glatigny, A. & Scazzocchio, C. (1995). Cloning and molecular characterization of hxA, the gene coding for the xanthine dehydrogenase (purine hydrolase I) of Aspergillus nidulans. J. Biol. Chem. 270, 3534-3550.
    • (1995) J. Biol. Chem. , vol.270 , pp. 3534-3550
    • Glatigny, A.1    Scazzocchio, C.2
  • 22
    • 0014556441 scopus 로고
    • Zum Mechanismus der Induktion nicotinabbauender Enzyme in Arthrobacter oxidans
    • Gloger, M. & Decker, K. (1969). Zum Mechanismus der Induktion nicotinabbauender Enzyme in Arthrobacter oxidans. Naturforsch. 246, 1016-1025.
    • (1969) Naturforsch. , vol.246 , pp. 1016-1025
    • Gloger, M.1    Decker, K.2
  • 24
    • 0000422934 scopus 로고
    • Classification
    • Goodfellow, M., Mordarski, M. & Williams, S. T., eds, Academic Press, London
    • Goodfellow, M. & Cross, T. (1984). Classification. The Biology of the Actinomycetes (Goodfellow, M., Mordarski, M. & Williams, S. T., eds), pp. 7-164, Academic Press, London.
    • (1984) The Biology of the Actinomycetes , pp. 7-164
    • Goodfellow, M.1    Cross, T.2
  • 25
    • 0028021488 scopus 로고
    • Structural analysis and molybdenum dependent expression of the pAO1 encoded nicotine dehydrogenase genes of Arthrobacter nicotinovorans
    • Grether-Beck, S., Igloi, G., Pust, S., Schilz, E., Decker, K. & Brandsch, R. (1994). Structural analysis and molybdenum dependent expression of the pAO1 encoded nicotine dehydrogenase genes of Arthrobacter nicotinovorans. Mol. Microbiol. 13, 929-936.
    • (1994) Mol. Microbiol. , vol.13 , pp. 929-936
    • Grether-Beck, S.1    Igloi, G.2    Pust, S.3    Schilz, E.4    Decker, K.5    Brandsch, R.6
  • 26
    • 11244339859 scopus 로고
    • Über den Abbau des Nicotins durch Bakterienenzyme; V. der Abbau des L-6-Hydroxy-nicotins zu [γ-Methyl-aminopropyl]-[6-hydroxy-pyridyl(3)]-keton
    • Gries, F. A., Decker, K. & Brühmüller, M. (1961). Über den Abbau des Nicotins durch Bakterienenzyme; V. Der Abbau des L-6-Hydroxy-nicotins zu [γ-Methyl-aminopropyl]-[6-hydroxy-pyridyl(3)]-keton. Hoppe-Seyler's Z. Physiol. Chem. 325, 229-241.
    • (1961) Hoppe-Seyler's Z. Physiol. Chem. , vol.325 , pp. 229-241
    • Gries, F.A.1    Decker, K.2    Brühmüller, M.3
  • 27
    • 0020363515 scopus 로고
    • Preferential codon usage in prokaryotic genes: The optimal codon-anticodon interaction energy and the selective codon usage in efficiently expressed genes
    • Grosjean, H. & Friers, W. (1982). Preferential codon usage in prokaryotic genes: the optimal codon-anticodon interaction energy and the selective codon usage in efficiently expressed genes. Gene, 18, 199-209.
    • (1982) Gene , vol.18 , pp. 199-209
    • Grosjean, H.1    Friers, W.2
  • 28
    • 0023650609 scopus 로고
    • Analysis of E. coli promoter sequences
    • Harley, C. B. & Reynolds, R. P. (1987). Analysis of E. coli promoter sequences. Nucl. Acids Res. 15, 2343-2361.
    • (1987) Nucl. Acids Res. , vol.15 , pp. 2343-2361
    • Harley, C.B.1    Reynolds, R.P.2
  • 29
    • 0021111879 scopus 로고
    • Compilation and analysis of Escherichia coli promoter DNA sequences
    • Hawley, D. K. & McClure, W. R. (1983). Compilation and analysis of Escherichia coli promoter DNA sequences. Nucl. Acids Res. 11, 2237-2255.
    • (1983) Nucl. Acids Res. , vol.11 , pp. 2237-2255
    • Hawley, D.K.1    McClure, W.R.2
  • 30
    • 0025370653 scopus 로고
    • A simple method for subcloning DNA fragments from gel slices
    • Heery, D. M., Gannon, F. & Powell, R. (1990). A simple method for subcloning DNA fragments from gel slices. Trends Genet. 6, 173.
    • (1990) Trends Genet. , vol.6 , pp. 173
    • Heery, D.M.1    Gannon, F.2    Powell, R.3
  • 31
    • 85030344460 scopus 로고
    • Dissertation, Faculty of Chemistry and Pharmacy, Albert-Ludwig University, Freiburg, Germany
    • Hinkkanen, A. (1984). Dissertation, Faculty of Chemistry and Pharmacy, Albert-Ludwig University, Freiburg, Germany.
    • (1984)
    • Hinkkanen, A.1
  • 32
    • 0020792024 scopus 로고
    • Purification of the flavoproteins 6-hydroxy-D- and 6-hydroxy-L-nicotine oxidase using hydrophobic affinity chromatography
    • Hinkkanen, A., Lilius, E. M., Nowack, J., Maas, R. & Decker, K. (1983). Purification of the flavoproteins 6-hydroxy-D- and 6-hydroxy-L-nicotine oxidase using hydrophobic affinity chromatography. Anal. Biochem. 132, 202-208.
    • (1983) Anal. Biochem. , vol.132 , pp. 202-208
    • Hinkkanen, A.1    Lilius, E.M.2    Nowack, J.3    Maas, R.4    Decker, K.5
  • 33
    • 0013508426 scopus 로고
    • The bacterial oxidation of nicotine. II. The isolation of the first oxidative product and its identification as (l)-6-hydroxynicotine
    • Hochstein, L. I. & Rittenberg, C. S. (1959). The bacterial oxidation of nicotine. II. The isolation of the first oxidative product and its identification as (l)-6-hydroxynicotine. J. Biol. Chem. 234, 156-162.
    • (1959) J. Biol. Chem. , vol.234 , pp. 156-162
    • Hochstein, L.I.1    Rittenberg, C.S.2
  • 35
    • 0026740865 scopus 로고
    • Xanthine dehydrogenase from Drosophila melanogaster: Purification and properties of the wild-type enzyme and of a variant lacking iron-sulfur centers
    • Hughes, R. K. (1992). Xanthine dehydrogenase from Drosophila melanogaster: purification and properties of the wild-type enzyme and of a variant lacking iron-sulfur centers. Biochemistry, 31, 3073-3083.
    • (1992) Biochemistry , vol.31 , pp. 3073-3083
    • Hughes, R.K.1
  • 36
    • 0027438935 scopus 로고
    • Cloning of the cDNA encoding human xanthine dehydrogenase (oxidase): Structural analysis of the protein and chromosomal location of the gene
    • Ichida, K., Amaya, Y., Noda, K., Minoshima, S., Hosoya, T., Sakai, O., Shimizu, N. & Nishino, T. (1993). Cloning of the cDNA encoding human xanthine dehydrogenase (oxidase): structural analysis of the protein and chromosomal location of the gene. Gene, 133, 279-284.
    • (1993) Gene , vol.133 , pp. 279-284
    • Ichida, K.1    Amaya, Y.2    Noda, K.3    Minoshima, S.4    Hosoya, T.5    Sakai, O.6    Shimizu, N.7    Nishino, T.8
  • 37
    • 0019824131 scopus 로고
    • Correlation between the abundance of E. coli transfer RNAs and the occurence of the respective codons in its protein genes: A proposal for a synonymous codon choice that is optimal for the E. coli translational system
    • Ikemura, T. (1981). Correlation between the abundance of E. coli transfer RNAs and the occurence of the respective codons in its protein genes: a proposal for a synonymous codon choice that is optimal for the E. coli translational system. J. Mol. Biol. 151, 389-409.
    • (1981) J. Mol. Biol. , vol.151 , pp. 389-409
    • Ikemura, T.1
  • 39
    • 0001450075 scopus 로고
    • The genus Arthrobacter
    • (Balows, A., Truper, H. G., Dwarkin, M., Harder, W. & Schleifer, K. H., eds), Springer Verlag, Heidelberg, New York
    • Jones, D. & Keddie, R. M. (1992). The genus Arthrobacter. The Prokaryotes (Balows, A., Truper, H. G., Dwarkin, M., Harder, W. & Schleifer, K. H., eds), vol. 2, pp. 1283-1299, Springer Verlag, Heidelberg, New York.
    • (1992) The Prokaryotes , vol.2 , pp. 1283-1299
    • Jones, D.1    Keddie, R.M.2
  • 40
    • 0000550040 scopus 로고
    • Phytochemical studies on the tobacco alkaloids. I. Optical rotatory power of nornicotine
    • Kisaki, T. & Tamaki, E. (1961). Phytochemical studies on the tobacco alkaloids. I. Optical rotatory power of nornicotine. Arch. Biochem. Biophys. 92, 351-355.
    • (1961) Arch. Biochem. Biophys. , vol.92 , pp. 351-355
    • Kisaki, T.1    Tamaki, E.2
  • 41
    • 0026600935 scopus 로고
    • Reclassification of two strains of Arthrobacter oxydans and proposal of Arthrobacter nicotinovorans sp. nov
    • Kodama, Y., Yamamoto, H., Amano, N. & Amchi, T. (1992). Reclassification of two strains of Arthrobacter oxydans and proposal of Arthrobacter nicotinovorans sp. nov. Int. J. Syst. Bacteriol. 42, 234-239.
    • (1992) Int. J. Syst. Bacteriol. , vol.42 , pp. 234-239
    • Kodama, Y.1    Yamamoto, H.2    Amano, N.3    Amchi, T.4
  • 42
    • 0023334182 scopus 로고
    • Mutations affecting expression of the rosy locus in Drosophila melanogaster
    • Lee, C. S., Curtis, D., McCarron, M., Love, C., Gray, M., Bender, W. & Chovnick, A. (1987). Mutations affecting expression of the rosy locus in Drosophila melanogaster. Genetics, 116, 55-66.
    • (1987) Genetics , vol.116 , pp. 55-66
    • Lee, C.S.1    Curtis, D.2    McCarron, M.3    Love, C.4    Gray, M.5    Bender, W.6    Chovnick, A.7
  • 43
    • 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., Roger, P. & Lingens, F. (1994). Purification and characterization of isoquinoline 1-oxidoreductase from Pseudomonas diminuta 7, a novel molybdenum-containing hydroxylase. J. Biol. Biochem. 269, 11254-11260.
    • (1994) J. Biol. Biochem. , vol.269 , pp. 11254-11260
    • Lehmann, M.1    Tshisuaka, B.2    Fetzner, S.3    Roger, P.4    Lingens, F.5
  • 44
    • 0029055501 scopus 로고
    • Molecular cloning of isoquinoline 1-oxidoreductase genes from Pseudomonas diminuta 7, structural analysis of iorA and iorB, and sequence comparisons with other molybdenum-containing hydroxylases
    • Lehmann, M., Tshisuaka, B., Fetzner, S. & Lingens, F. (1995). Molecular cloning of isoquinoline 1-oxidoreductase genes from Pseudomonas diminuta 7, structural analysis of iorA and iorB, and sequence comparisons with other molybdenum-containing hydroxylases. J. Biol. Chem. 270, 14420-14429.
    • (1995) J. Biol. Chem. , vol.270 , pp. 14420-14429
    • Lehmann, M.1    Tshisuaka, B.2    Fetzner, S.3    Lingens, F.4
  • 45
    • 0031940235 scopus 로고    scopus 로고
    • Xanthine dehydrogenase from the phototrophic purple bacterium Rhodobacter capsulata is more similar to its eukaryotic counterparts than to molybdopterin enzymes
    • Leimkuehler, S., Kern, M., Solomon, P., McEwan, A., Schwarz, G., Mendahl, R. R. & Klipp, W. (1998). Xanthine dehydrogenase from the phototrophic purple bacterium Rhodobacter capsulata is more similar to its eukaryotic counterparts than to molybdopterin enzymes. J. Microbiol. 27, 853-869.
    • (1998) J. Microbiol. , vol.27 , pp. 853-869
    • Leimkuehler, S.1    Kern, M.2    Solomon, P.3    McEwan, A.4    Schwarz, G.5    Mendahl, R.R.6    Klipp, W.7
  • 46
    • 0025203824 scopus 로고
    • A procedure for DNA and RNA transfer to membrane filters avoiding weight-induced gel flattening
    • Lichtenstein, A. V., Moiseev, V. L. & Zaboikin, M. M. (1990). A procedure for DNA and RNA transfer to membrane filters avoiding weight-induced gel flattening. Anal. Biochem. 191, 187-191.
    • (1990) Anal. Biochem. , vol.191 , pp. 187-191
    • Lichtenstein, A.V.1    Moiseev, V.L.2    Zaboikin, M.M.3
  • 47
    • 0025982062 scopus 로고
    • Construction of T-vectors, a rapid and general system for direct cloning of unmodified PCR products
    • Marchuk, D., Drumm, M., Saulino, A. & Collins, F. S. (1990). Construction of T-vectors, a rapid and general system for direct cloning of unmodified PCR products. Nucl. Acids Res. 19, 1154.
    • (1990) Nucl. Acids Res. , vol.19 , pp. 1154
    • Marchuk, D.1    Drumm, M.2    Saulino, A.3    Collins, F.S.4
  • 48
    • 0013481910 scopus 로고
    • Growth stage-dependent expression of 6-hydroxy-D-nicotine oxidase of the nicotine regulon of Arthrobacter oxidans
    • Mauch, L., Krauß, B. & Brandsch, R. (1989). Growth stage-dependent expression of 6-hydroxy-D-nicotine oxidase of the nicotine regulon of Arthrobacter oxidans. Arch. Microbiol. 152, 95-99.
    • (1989) Arch. Microbiol. , vol.152 , pp. 95-99
    • Mauch, L.1    Krauß, B.2    Brandsch, R.3
  • 49
    • 0019811426 scopus 로고
    • Unique features in the ribosome binding site sequence of the Gram-positive Staphylococcus aureus β-lactamase gene
    • McLaughlin, J. R., Murray, C. L. & Rabinowitz, J. C. (1981). Unique features in the ribosome binding site sequence of the Gram-positive Staphylococcus aureus β-lactamase gene. J. Biol. Chem. 256, 11283-11291.
    • (1981) J. Biol. Chem. , vol.256 , pp. 11283-11291
    • McLaughlin, J.R.1    Murray, C.L.2    Rabinowitz, J.C.3
  • 50
    • 0028982741 scopus 로고
    • A pAO1-encoded molybdopterin cofactor gene (moaA) of Arthrobacter nicotinovorans: Characterization and site-directed mutagenesis of the encoded protein
    • Menéndez, C., Igloi, G. L., Henninger, H. & Brandsch, R. (1995). A pAO1-encoded molybdopterin cofactor gene (moaA) of Arthrobacter nicotinovorans: characterization and site-directed mutagenesis of the encoded protein. Arch. Microbiol. 164, 142-151.
    • (1995) Arch. Microbiol. , vol.164 , pp. 142-151
    • Menéndez, C.1    Igloi, G.L.2    Henninger, H.3    Brandsch, R.4
  • 51
    • 0030900624 scopus 로고    scopus 로고
    • IS 1473, a putative insertion sequence identified in the plasmid pAO1 from Arthrobacter nicotinovorans: Isolation, characterization, and distribution among Arthrobacter species
    • Menéndez, C., Igloi, G. L. & Brandsch, R. (1997). IS 1473, a putative insertion sequence identified in the plasmid pAO1 from Arthrobacter nicotinovorans: isolation, characterization, and distribution among Arthrobacter species. Plasmid, 37, 35-41.
    • (1997) Plasmid , vol.37 , pp. 35-41
    • Menéndez, C.1    Igloi, G.L.2    Brandsch, R.3
  • 52
    • 0018572714 scopus 로고
    • DNA sequence of the gene for the outer membrane lipoprotein of E. coli: An extremely AT-rich promoter
    • Nakamura, K. & Inouye, M. (1979). DNA sequence of the gene for the outer membrane lipoprotein of E. coli: an extremely AT-rich promoter. Cell, 18, 1109-1117.
    • (1979) Cell , vol.18 , pp. 1109-1117
    • Nakamura, K.1    Inouye, M.2
  • 53
    • 0028603529 scopus 로고
    • DNA sequence of the cut A, B and C genes, encoding the molybdenum containing hydroxylase carbon monoxide dehydrogenase, from Pseudomonas thermocarboxydovorans strain C2
    • Pearson, D. M., O'Reilly, C. O., Colby, J. & Black, G. W. (1994). DNA sequence of the cut A, B and C genes, encoding the molybdenum containing hydroxylase carbon monoxide dehydrogenase, from Pseudomonas thermocarboxydovorans strain C2. Biochim. Biophys. Acta, 1188, 432-438.
    • (1994) Biochim. Biophys. Acta , vol.1188 , pp. 432-438
    • Pearson, D.M.1    O'Reilly, C.O.2    Colby, J.3    Black, G.W.4
  • 54
    • 0025950944 scopus 로고
    • Searching protein sequence libraries: Comparison of the sensitivity and selectivity of the Smith-Waterman and FASTA algorithms
    • Pearson, W. R. (1991). Searching protein sequence libraries: comparison of the sensitivity and selectivity of the Smith-Waterman and FASTA algorithms. Genomics, 11, 635-650.
    • (1991) Genomics , vol.11 , pp. 635-650
    • Pearson, W.R.1
  • 56
    • 0019874713 scopus 로고
    • In vitro synthesis of the respiratory NADH dehydrogenase of Escherichia coli. Role of UUG as initiation codon
    • Poulis, M. I., Shaw, D. C., Campbell, H. D. & Young, I. G. (1981). In vitro synthesis of the respiratory NADH dehydrogenase of Escherichia coli. Role of UUG as initiation codon. Biochemistry, 20, 4178-4185.
    • (1981) Biochemistry , vol.20 , pp. 4178-4185
    • Poulis, M.I.1    Shaw, D.C.2    Campbell, H.D.3    Young, I.G.4
  • 57
    • 0016629024 scopus 로고
    • Bacteriophage T7 early promoters: Nucleotide sequence of two RNA polymerase binding sites
    • Pribnow, D. (1975). Bacteriophage T7 early promoters: nucleotide sequence of two RNA polymerase binding sites. J. Mol. Biol. 99, 419-443.
    • (1975) J. Mol. Biol. , vol.99 , pp. 419-443
    • Pribnow, D.1
  • 58
    • 85030341550 scopus 로고
    • Dissertation, Faculty of Chemistry and Pharmacy. Albert Ludwig University, Freiburg, Germany
    • Pust, S. (1990). Dissertation, Faculty of Chemistry and Pharmacy. Albert Ludwig University, Freiburg, Germany.
    • (1990)
    • Pust, S.1
  • 59
    • 0013477376 scopus 로고
    • The bacterial oxidation of nicotine V. Identification of 2,6-dihydroxypseudooxynicotine as the third oxidative product
    • Richardson, S. H. & Rittenberg, S. C. (1961). The bacterial oxidation of nicotine V. Identification of 2,6-dihydroxypseudooxynicotine as the third oxidative product. J. Biol. Chem. 236, 964-967.
    • (1961) J. Biol. Chem. , vol.236 , pp. 964-967
    • Richardson, S.H.1    Rittenberg, S.C.2
  • 60
    • 0024567840 scopus 로고
    • Nucleotide sequence of the Xdh region in Drosophila pseudoobscura and an analysis of the evolution of synonymous codons
    • Riley, M. A. (1989). Nucleotide sequence of the Xdh region in Drosophila pseudoobscura and an analysis of the evolution of synonymous codons. Mol. Biol. Evol. 6, 33-52.
    • (1989) Mol. Biol. Evol. , vol.6 , pp. 33-52
    • Riley, M.A.1
  • 61
    • 0030761340 scopus 로고    scopus 로고
    • Crystal structure and mechanism of action of the xanthine oxidase-related aldehyde oxidoreductase from Desulfovibrio gigas
    • Romão, M. J. & Huber, R. (1997). Crystal structure and mechanism of action of the xanthine oxidase-related aldehyde oxidoreductase from Desulfovibrio gigas. Biochem. Soc. Trans. 25, 755-757.
    • (1997) Biochem. Soc. Trans. , vol.25 , pp. 755-757
    • Romão, M.J.1    Huber, R.2
  • 64
    • 0028893185 scopus 로고
    • The structure of chicken liver xanthine dehydrogenase. cDNA cloning and the domain structure
    • Sato, A., Nishino, T., Noda, K., Amaya, Y. & Nishino, T. (1995). The structure of chicken liver xanthine dehydrogenase. cDNA cloning and the domain structure. J. Biol. Chem. 270, 2818-2826.
    • (1995) J. Biol. Chem. , vol.270 , pp. 2818-2826
    • Sato, A.1    Nishino, T.2    Noda, K.3    Amaya, Y.4    Nishino, T.5
  • 65
    • 0016658183 scopus 로고
    • Nucleotide sequence of RNA polymerase binding site from the DNA of bacteriophage fd
    • Schaller, H., Gray, C. & Herrmann, K. (1975). Nucleotide sequence of RNA polymerase binding site from the DNA of bacteriophage fd. Proc. Natl Acad. Sci. USA, 72, 737-741.
    • (1975) Proc. Natl Acad. Sci. USA , vol.72 , pp. 737-741
    • Schaller, H.1    Gray, C.2    Herrmann, K.3
  • 66
    • 85030342038 scopus 로고
    • Dissertation, Faculty of Chemistry and Pharmacy. Albert Ludwig University, Freiburg, Germany
    • Schelling, U. (1995). Dissertation, Faculty of Chemistry and Pharmacy. Albert Ludwig University, Freiburg, Germany.
    • (1995)
    • Schelling, U.1
  • 67
    • 85030346525 scopus 로고    scopus 로고
    • Dissertation, Faculty of Chemistry and Pharmacy. Albert Ludwig University, Freiburg, Germany
    • Schenk, S. (1996). Dissertation, Faculty of Chemistry and Pharmacy. Albert Ludwig University, Freiburg, Germany.
    • (1996)
    • Schenk, S.1
  • 68
    • 13144285686 scopus 로고    scopus 로고
    • Molecular and preliminary crystallographic investigation of the enantiomer-specific 6-hydroxy-L-nicotine oxidase
    • (Stevenson, K. J., Massey, V. & Williams, C. H., Jr, eds), University of Calgary Press, Calgary
    • Schenk, S. & Decker, K. (1997). Molecular and preliminary crystallographic investigation of the enantiomer-specific 6-hydroxy-L-nicotine oxidase. In Flavins and Flavoproteins 1996 (Stevenson, K. J., Massey, V. & Williams, C. H., Jr, eds), pp. 269-273, University of Calgary Press, Calgary.
    • (1997) Flavins and Flavoproteins 1996 , pp. 269-273
    • Schenk, S.1    Decker, K.2
  • 69
    • 85030345276 scopus 로고    scopus 로고
    • Horizontal gene transfer involved in the convergent evolution of the plasmid-encoded enantioselective 6-hydroxynicotine oxidases
    • In the press
    • Schenk, S. & Decker, K. (1998). Horizontal gene transfer involved in the convergent evolution of the plasmid-encoded enantioselective 6-hydroxynicotine oxidases. J. Mol. Evol. In the press.
    • (1998) J. Mol. Evol.
    • Schenk, S.1    Decker, K.2
  • 70
    • 0028999344 scopus 로고
    • Cloning, sequencing and heterologous expression of the monoamine oxidase gene from Aspergillus niger
    • Schilling, B. & Lerch, K. (1994). Cloning, sequencing and heterologous expression of the monoamine oxidase gene from Aspergillus niger. Mol. Gen. Genet. 247, 430-438.
    • (1994) Mol. Gen. Genet. , vol.247 , pp. 430-438
    • Schilling, B.1    Lerch, K.2
  • 72
    • 0016610995 scopus 로고
    • Determinant of cistron specificity in bacterial ribosomes
    • Shine, J. & Dalgarno, L. (1975). Determinant of cistron specificity in bacterial ribosomes. Nature, 254, 34-38.
    • (1975) Nature , vol.254 , pp. 34-38
    • Shine, J.1    Dalgarno, L.2
  • 73
    • 0023504973 scopus 로고
    • Purification, specific fragmentation, and separation of large DNA molecules
    • Smith, C. L. & Cantor, C. R. (1987). Purification, specific fragmentation, and separation of large DNA molecules. Methods Enzymol. 155, 449-467.
    • (1987) Methods Enzymol. , vol.155 , pp. 449-467
    • Smith, C.L.1    Cantor, C.R.2
  • 74
    • 0030013766 scopus 로고    scopus 로고
    • BCM search launcher. An integrated interface to molecular biology data base search and analysis services available on the world wide web
    • Smith, R. F., Wiese, B. A., Wojzynski, M. K., Davison, D. B. & Worley, K. C. (1996). BCM search launcher. An integrated interface to molecular biology data base search and analysis services available on the world wide web. Genome Res. 6, 454-462.
    • (1996) Genome Res. , vol.6 , pp. 454-462
    • Smith, R.F.1    Wiese, B.A.2    Wojzynski, M.K.3    Davison, D.B.4    Worley, K.C.5
  • 75
    • 0019887799 scopus 로고
    • Identification of common molecular subsequences
    • Smith, T. F. & Waterman, M. S. (1981). Identification of common molecular subsequences. J. Mol. Biol. 147, 195-197.
    • (1981) J. Mol. Biol. , vol.147 , pp. 195-197
    • Smith, T.F.1    Waterman, M.S.2
  • 76
    • 0001936455 scopus 로고
    • RNA: RNA interactions during polypeptide chain initiation
    • (Chambliss, G., et al., ed.), University Park Press, Baltimore
    • Steitz, J. A. (1979). RNA: RNA interactions during polypeptide chain initiation. In Ribosomes (Chambliss, G., et al., ed.), pp. 479-495, University Park Press, Baltimore.
    • (1979) Ribosomes , pp. 479-495
    • Steitz, J.A.1
  • 77
    • 0020480282 scopus 로고
    • Characterization of translational initiation sites in E. coli
    • Stormo, G. D., Schneider, T. D. & Gold, L. M. (1982). Characterization of translational initiation sites in E. coli. Nucl. Acids Res. 10, 2971-2995.
    • (1982) Nucl. Acids Res. , vol.10 , pp. 2971-2995
    • Stormo, G.D.1    Schneider, T.D.2    Gold, L.M.3
  • 78
    • 0026549146 scopus 로고
    • Compilation and analysis of DNA sequences associated with apparent streptomycete promoters
    • Strohl, W. R. (1992). Compilation and analysis of DNA sequences associated with apparent streptomycete promoters. Nucl. Acids Res. 20, 961-974.
    • (1992) Nucl. Acids Res. , vol.20 , pp. 961-974
    • Strohl, W.R.1
  • 79
    • 0028280650 scopus 로고
    • Molecular cloning and sequence analysis of the gene of the molybdenum-containing aldehyde oxidoreductase of Desulfovibrio gigas. The deduced amino acid sequence shows similarity to xanthine dehydrogenase
    • Thoenes, U., Flores, O. L., Neves, A., Devreese, B., Van Beeumen, J. J., Huber, R., Romão, M. J., LeGall, J., Moura, J. J. & Rodrigues-Pousada, C. (1994). Molecular cloning and sequence analysis of the gene of the molybdenum-containing aldehyde oxidoreductase of Desulfovibrio gigas. The deduced amino acid sequence shows similarity to xanthine dehydrogenase. Eur. J. Biochem. 220, 901-910.
    • (1994) Eur. J. Biochem. , vol.220 , pp. 901-910
    • Thoenes, U.1    Flores, O.L.2    Neves, A.3    Devreese, B.4    Van Beeumen, J.J.5    Huber, R.6    Romão, M.J.7    LeGall, J.8    Moura, J.J.9    Rodrigues-Pousada, C.10
  • 80
    • 0030849308 scopus 로고    scopus 로고
    • Biochemical and genetic characterization of the aldehyde dehydrogenase complex from Acetobacter europaeus
    • Thurner, C., Vela, C., Thony-Meyer, L., Meile, L. & Teuber, M. (1997). Biochemical and genetic characterization of the aldehyde dehydrogenase complex from Acetobacter europaeus. Arch. Microbiol 168, 81-91.
    • (1997) Arch. Microbiol , vol.168 , pp. 81-91
    • Thurner, C.1    Vela, C.2    Thony-Meyer, L.3    Meile, L.4    Teuber, M.5
  • 82
    • 0028175748 scopus 로고
    • Simplified large-scale alkaline lysis preparation of plasmid DNA with minimal use of phenol
    • Wang, L. F., Voysey, R. & Yu, M. (1994). Simplified large-scale alkaline lysis preparation of plasmid DNA with minimal use of phenol. BioTechniques, 17, 26-28.
    • (1994) BioTechniques , vol.17 , pp. 26-28
    • Wang, L.F.1    Voysey, R.2    Yu, M.3
  • 83
    • 0026036047 scopus 로고
    • Enzymes depending on the pterin molybdenum cofactor: Sequence families, spectroscopic properties of molybdenum and possible cofactor-binding domains
    • Wootton, J. C., Nicolson, R. E., Cock, J. M., Walters, D. E., Burke, J. F., Doyle, W. A. & Bray, R. C. (1991). Enzymes depending on the pterin molybdenum cofactor: sequence families, spectroscopic properties of molybdenum and possible cofactor-binding domains. Biochim. Biophys. Acta, 1057, 157-185.
    • (1991) Biochim. Biophys. Acta , vol.1057 , pp. 157-185
    • Wootton, J.C.1    Nicolson, R.E.2    Cock, J.M.3    Walters, D.E.4    Burke, J.F.5    Doyle, W.A.6    Bray, R.C.7
  • 84
    • 0027378093 scopus 로고
    • cDNA cloning, characterization, and tissue-specific expression of human xanthine dehydrogenase/ xanthine oxidase
    • Wright, R. M., Vaitaitis, G. M., Wilson, C. M., Repine, T. B., Terada, L. S. & Repine, J. E. (1993). cDNA cloning, characterization, and tissue-specific expression of human xanthine dehydrogenase/ xanthine oxidase. Proc. Natl Acad. Sci. USA, 90, 10690-10694.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 10690-10694
    • Wright, R.M.1    Vaitaitis, G.M.2    Wilson, C.M.3    Repine, T.B.4    Terada, L.S.5    Repine, J.E.6
  • 85
    • 0031832276 scopus 로고    scopus 로고
    • Cloning of two Bombyx homologues of the Drosophila rosy gene and their relationship to larval translucent skin colour mutants
    • Yasukochi, Y., Kanda, T. & Tamura, T. (1998). Cloning of two Bombyx homologues of the Drosophila rosy gene and their relationship to larval translucent skin colour mutants. Genet Res. 71, 11-19.
    • (1998) Genet Res. , vol.71 , pp. 11-19
    • Yasukochi, Y.1    Kanda, T.2    Tamura, T.3
  • 86
    • 0027661582 scopus 로고
    • Fast and economical large-scale preparation of high-quality plasmid DNA
    • Yeung, C. M. & Lau, A. S. (1993). Fast and economical large-scale preparation of high-quality plasmid DNA. BioTechniques, 15, 381-382.
    • (1993) BioTechniques , vol.15 , pp. 381-382
    • Yeung, C.M.1    Lau, A.S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.