메뉴 건너뛰기




Volumn 178, Issue 20, 1996, Pages 6019-6024

Purification and sequence analysis of 4-methyl-5-nitrocatechol oxygenase from Burkholderia sp. strain DNT

Author keywords

[No Author keywords available]

Indexed keywords

4 METHYL 5 NITROCATECHOL OXYGENASE; BACTERIAL ENZYME; OXYGENASE; UNCLASSIFIED DRUG;

EID: 0029820893     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.178.20.6019-6024.1996     Document Type: Article
Times cited : (45)

References (51)
  • 1
    • 0026558894 scopus 로고
    • Construction of a 3-chlorobiphenyl-utilizing recombinant from an intergeneric mating
    • Adams, R. H., C.-M. Huang, F. K. Higson, V. Brenner, and D. D. Focht. 1992. Construction of a 3-chlorobiphenyl-utilizing recombinant from an intergeneric mating. Appl. Environ. Microbiol. 58:647-654.
    • (1992) Appl. Environ. Microbiol. , vol.58 , pp. 647-654
    • Adams, R.H.1    Huang, C.-M.2    Higson, F.K.3    Brenner, V.4    Focht, D.D.5
  • 2
    • 0027971398 scopus 로고
    • Oxidative release of nitrite from 2-nitrotoluene by a three-component enzyme system from Pseudomonas sp. strain JS42
    • An, D., D. T. Gibson, and J. C. Spain. 1994. Oxidative release of nitrite from 2-nitrotoluene by a three-component enzyme system from Pseudomonas sp. strain JS42. J. Bacteriol. 176:7462-7467.
    • (1994) J. Bacteriol. , vol.176 , pp. 7462-7467
    • An, D.1    Gibson, D.T.2    Spain, J.C.3
  • 3
    • 0019994544 scopus 로고
    • The purification and properties of 2,4-dichlorophenol hydroxylase from a strain of Acinetobacter species
    • Beadle, C. A., and A. R. W. Smith. 1982. The purification and properties of 2,4-dichlorophenol hydroxylase from a strain of Acinetobacter species. Eur. J. Biochem. 123:323-332.
    • (1982) Eur. J. Biochem. , vol.123 , pp. 323-332
    • Beadle, C.A.1    Smith, A.R.W.2
  • 4
    • 0027135240 scopus 로고
    • A hydroxylase-like gene product contributes to synthesis of a polyketide spore pigment in Streptomyces halstedii
    • Blanco, G., A. Pereda, P. Brian, C. Mendez, K. F. Chater, and J. A. Salas. 1993. A hydroxylase-like gene product contributes to synthesis of a polyketide spore pigment in Streptomyces halstedii. J. Bacteriol. 175:8043-8048.
    • (1993) J. Bacteriol. , vol.175 , pp. 8043-8048
    • Blanco, G.1    Pereda, A.2    Brian, P.3    Mendez, C.4    Chater, K.F.5    Salas, J.A.6
  • 5
    • 0029310651 scopus 로고
    • Cloning and nucleotide sequence of the gene responsible for chlorination of tetracycline
    • Dairi, T., T. Nakano, K. Aisaka, R. Katsumata, and M. Hasegawa. 1995. Cloning and nucleotide sequence of the gene responsible for chlorination of tetracycline. Biosci. Biotechnol. Biochem. 59:1099-1106.
    • (1995) Biosci. Biotechnol. Biochem. , vol.59 , pp. 1099-1106
    • Dairi, T.1    Nakano, T.2    Aisaka, K.3    Katsumata, R.4    Hasegawa, M.5
  • 6
    • 0027243104 scopus 로고
    • Nucleotide sequences and heterologous expression of tcmG and tcmP, biosynthetic genes for tetracenomycin C in Streptomyces glaucescens
    • Decker, H., H. Motamedi, and C. R. Hutchinson. 1993. Nucleotide sequences and heterologous expression of tcmG and tcmP, biosynthetic genes for tetracenomycin C in Streptomyces glaucescens. J. Bacteriol. 175:3876-3886.
    • (1993) J. Bacteriol. , vol.175 , pp. 3876-3886
    • Decker, H.1    Motamedi, H.2    Hutchinson, C.R.3
  • 7
    • 0024791111 scopus 로고
    • Common denominators of promoter control in Pseudomonas and other bacteria
    • Deretic, V., W. M. Konyecsni, C. D. Mohr, D. W. Martin, and N. S. Hibler. 1989. Common denominators of promoter control in Pseudomonas and other bacteria. Bio/Technology 7:1249-1254.
    • (1989) Bio/Technology , vol.7 , pp. 1249-1254
    • Deretic, V.1    Konyecsni, W.M.2    Mohr, C.D.3    Martin, D.W.4    Hibler, N.S.5
  • 8
    • 0025265852 scopus 로고
    • Rubredoxin reductase of Pseudomonas oleovorans: Structure relationship to other flavoprotein oxidoreductases based on one NAD and two FAD finger prints
    • Eggink, G., H. Engel, G. Vriend, P. Terpstra, and B. Witholt. 1990. Rubredoxin reductase of Pseudomonas oleovorans: structure relationship to other flavoprotein oxidoreductases based on one NAD and two FAD finger prints. J. Mol. Biol. 212:135-142.
    • (1990) J. Mol. Biol. , vol.212 , pp. 135-142
    • Eggink, G.1    Engel, H.2    Vriend, G.3    Terpstra, P.4    Witholt, B.5
  • 9
    • 0024261763 scopus 로고
    • Sequence and organization of pobA, the gene coding for p-hydroxybenzoate hydroxylase, an inducible enzyme from Pseudomonas aeruginosa
    • Entsch, B., Y. Nan, K. Weaich, and K. F. Scott. 1988. Sequence and organization of pobA, the gene coding for p-hydroxybenzoate hydroxylase, an inducible enzyme from Pseudomonas aeruginosa. Gene 171:279-291.
    • (1988) Gene , vol.171 , pp. 279-291
    • Entsch, B.1    Nan, Y.2    Weaich, K.3    Scott, K.F.4
  • 10
    • 0026766452 scopus 로고
    • Nucleotide sequencing and transcription mapping of the genes encoding biphenyl dioxygenase, a multicomponent polychlorinated-biphenyl-degrading enzyme in Pseudomonas strain LB400
    • Erikson, B. D., and F. J. Mondello. 1992. Nucleotide sequencing and transcription mapping of the genes encoding biphenyl dioxygenase, a multicomponent polychlorinated-biphenyl-degrading enzyme in Pseudomonas strain LB400. J. Bacteriol. 174:2903-2912.
    • (1992) J. Bacteriol. , vol.174 , pp. 2903-2912
    • Erikson, B.D.1    Mondello, F.J.2
  • 11
    • 0015236352 scopus 로고
    • Electrophoretic analysis of the major polypeptides of the human erythrocyte membrane
    • Fairbanks, G., T. L. Steck, and D. F. H. Wallach. 1971. Electrophoretic analysis of the major polypeptides of the human erythrocyte membrane. Biochemistry 10:2606-2617.
    • (1971) Biochemistry , vol.10 , pp. 2606-2617
    • Fairbanks, G.1    Steck, T.L.2    Wallach, D.F.H.3
  • 13
    • 0028241454 scopus 로고
    • Biodegradation of 4-methyl-5-nitrocatechol by Pseudomonas sp. strain DNT
    • Haigler, B. E., S. F. Nishino, and J. C. Spain. 1994. Biodegradation of 4-methyl-5-nitrocatechol by Pseudomonas sp. strain DNT. J. Bacteriol. 176:3433-3437.
    • (1994) J. Bacteriol. , vol.176 , pp. 3433-3437
    • Haigler, B.E.1    Nishino, S.F.2    Spain, J.C.3
  • 14
    • 10144226506 scopus 로고
    • Purification and characterization of 4-methyl-5-nitrocatechol oxygenase from Pseudomonas sp. strain DNT, abstr. Q-172
    • American Society for Microbiology, Washington, D.C.
    • Haigler, B. E., and J. C. Spain. 1995. Purification and characterization of 4-methyl-5-nitrocatechol oxygenase from Pseudomonas sp. strain DNT, abstr. Q-172, p. 430. In Abstracts of the 95th General Meeting of the American Society for Microbiology 1995. American Society for Microbiology, Washington, D.C.
    • (1995) Abstracts of the 95th General Meeting of the American Society for Microbiology 1995 , pp. 430
    • Haigler, B.E.1    Spain, J.C.2
  • 15
    • 0028022845 scopus 로고
    • Biodegradation of 2-nitrotoluene by Pseudomonas sp. strain JS42
    • Haigler, B. E., W. H. Wallace, and J. C. Spain. 1994. Biodegradation of 2-nitrotoluene by Pseudomonas sp. strain JS42. Appl. Environ. Microbiol. 60:3466-3469.
    • (1994) Appl. Environ. Microbiol. , vol.60 , pp. 3466-3469
    • Haigler, B.E.1    Wallace, W.H.2    Spain, J.C.3
  • 16
    • 0019321006 scopus 로고
    • Fluoride elimination from substrates in hydroxylation reactions catalyzed by p-hydroxybenzoate hydroxylase
    • Husain, M., B. Entsch, D. P. Ballou, V. Massey, and P. J. Chapman. 1980. Fluoride elimination from substrates in hydroxylation reactions catalyzed by p-hydroxybenzoate hydroxylase. J. Biol. Chem. 255:4189-4197.
    • (1980) J. Biol. Chem. , vol.255 , pp. 4189-4197
    • Husain, M.1    Entsch, B.2    Ballou, D.P.3    Massey, V.4    Chapman, P.J.5
  • 17
    • 0026564238 scopus 로고
    • Phenol hydroxylase from Trichosporon cutaneum: Gene cloning, sequence analysis, and functional expression in Escherichia coli
    • Kalin, M., H. Y. Neujahr, R. N. Weissmahr, T. Sejlitz, R. Johl, A. Rechter, and J. Reiser. 1992. Phenol hydroxylase from Trichosporon cutaneum: gene cloning, sequence analysis, and functional expression in Escherichia coli. J. Bacteriol. 174:7112-7120.
    • (1992) J. Bacteriol. , vol.174 , pp. 7112-7120
    • Kalin, M.1    Neujahr, H.Y.2    Weissmahr, R.N.3    Sejlitz, T.4    Johl, R.5    Rechter, A.6    Reiser, J.7
  • 18
    • 0026661977 scopus 로고
    • Complete nucleotide sequence of tbuD, the gene encoding phenol/cresol hydroxylase from Pseudomonas pickettii PKO1, and functional analysis of the encoded enzyme
    • Kukor, J. J., and R. H. Olsen. 1992. Complete nucleotide sequence of tbuD, the gene encoding phenol/cresol hydroxylase from Pseudomonas pickettii PKO1, and functional analysis of the encoded enzyme. J. Bacteriol. 174:6518-6526.
    • (1992) J. Bacteriol. , vol.174 , pp. 6518-6526
    • Kukor, J.J.1    Olsen, R.H.2
  • 19
    • 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 (London) 227:680-685.
    • (1970) Nature (London) , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 20
    • 39749187675 scopus 로고
    • A theory of gel filtration and its experimental verification
    • Laurent, T. C., and J. Killander. 1964. A theory of gel filtration and its experimental verification. J. Chromatogr. 14:317-330.
    • (1964) J. Chromatogr. , vol.14 , pp. 317-330
    • Laurent, T.C.1    Killander, J.2
  • 21
    • 0028801863 scopus 로고
    • Bacterial degradation of m-nitrobenzoic acid
    • Nadeau, L. J., and J. C. Spain, 1995. Bacterial degradation of m-nitrobenzoic acid. Appl. Environ. Microbiol. 61:840-843.
    • (1995) Appl. Environ. Microbiol. , vol.61 , pp. 840-843
    • Nadeau, L.J.1    Spain, J.C.2
  • 22
    • 0026017943 scopus 로고
    • Nucleotide sequence of the Acinetobacter calcoaceticus benABC genes for benzoate 1,2-dioxygenase reveal evolutionary relationships among oxygenases
    • Neidle, E. L., C. Hartnett, L. N. Ornston, A. Bairoch, M. Rekik, and S. Harayama. 1991. Nucleotide sequence of the Acinetobacter calcoaceticus benABC genes for benzoate 1,2-dioxygenase reveal evolutionary relationships among oxygenases. J. Bacteriol. 173:5385-5395.
    • (1991) J. Bacteriol. , vol.173 , pp. 5385-5395
    • Neidle, E.L.1    Hartnett, C.2    Ornston, L.N.3    Bairoch, A.4    Rekik, M.5    Harayama, S.6
  • 23
    • 0015790898 scopus 로고
    • Phenol hydroxylase from yeast. Purification and properties of the enzyme from Trichosporon cutaneum
    • Neujahr, H. Y., and A. Gaal. 1973. Phenol hydroxylase from yeast. Purification and properties of the enzyme from Trichosporon cutaneum. Eur. J. Biochem. 35:386-400.
    • (1973) Eur. J. Biochem. , vol.35 , pp. 386-400
    • Neujahr, H.Y.1    Gaal, A.2
  • 24
    • 0029044853 scopus 로고
    • Nucleotide sequences and expression of genes from Streptomyces purpurascens that cause the production of new anthracyclines in Streptomyces galilaeus
    • Niemi, J., and P. Mäntsälä. 1995. Nucleotide sequences and expression of genes from Streptomyces purpurascens that cause the production of new anthracyclines in Streptomyces galilaeus. J. Bacteriol. 177:2942-2945.
    • (1995) J. Bacteriol. , vol.177 , pp. 2942-2945
    • Niemi, J.1    Mäntsälä, P.2
  • 25
    • 85035171633 scopus 로고    scopus 로고
    • Personal communication
    • 24a.Nishino, S. Personal communication.
    • Nishino, S.1
  • 26
    • 0029070669 scopus 로고
    • Oxidative pathway for the biodegradation of nitrobenzene by Comamonas sp. strain JS765
    • Nishino, S. F., and J. C. Spain. 1995. Oxidative pathway for the biodegradation of nitrobenzene by Comamonas sp. strain JS765. Appl. Environ. Microbiol. 61:2308-2313.
    • (1995) Appl. Environ. Microbiol. , vol.61 , pp. 2308-2313
    • Nishino, S.F.1    Spain, J.C.2
  • 28
    • 0025815712 scopus 로고
    • Sequence of the gene (pheA) encoding phenol monooxygenase from Pseudomonas sp. EST1001: Expression in Escherichia coli and Pseudomonas putida
    • Nurk, A., L. Kasak, and M. Kivisaar. 1991. Sequence of the gene (pheA) encoding phenol monooxygenase from Pseudomonas sp. EST1001: expression in Escherichia coli and Pseudomonas putida. Gene (Amsterdam) 102:13-18.
    • (1991) Gene (Amsterdam) , vol.102 , pp. 13-18
    • Nurk, A.1    Kasak, L.2    Kivisaar, M.3
  • 29
    • 0027476196 scopus 로고
    • Cloning, sequence analysis, and expression of the Flavobacterium pentachlorophenol-4-monooxygenase gene in Escherichia coli
    • Orser, C. S., C. C. Lange, L. Xun, T. C. Zahrt, and B. J. Schneider. 1993. Cloning, sequence analysis, and expression of the Flavobacterium pentachlorophenol-4-monooxygenase gene in Escherichia coli. J. Bacteriol. 175:411-416.
    • (1993) J. Bacteriol. , vol.175 , pp. 411-416
    • Orser, C.S.1    Lange, C.C.2    Xun, L.3    Zahrt, T.C.4    Schneider, B.J.5
  • 30
    • 0025357079 scopus 로고
    • Organization and sequence analysis of the 2,4-dichlorophenol hydroxylase and dichlorocatechol oxidative operons of plasmid pJP4
    • Perkins, E. J., M. P. Gordon, O. Caceres, and P. F. Lurquin. 1990. Organization and sequence analysis of the 2,4-dichlorophenol hydroxylase and dichlorocatechol oxidative operons of plasmid pJP4. J. Bacteriol. 172:2351-2359.
    • (1990) J. Bacteriol. , vol.172 , pp. 2351-2359
    • Perkins, E.J.1    Gordon, M.P.2    Caceres, O.3    Lurquin, P.F.4
  • 31
    • 0023883241 scopus 로고
    • Sequence of thioredoxin reductase from Escherichia coli: Relationship to other flavoprotein disulfide oxidoreductases
    • Russel, M., and P. Model. 1988. Sequence of thioredoxin reductase from Escherichia coli: relationship to other flavoprotein disulfide oxidoreductases. J. Biol. Chem. 263:9015-9019.
    • (1988) J. Biol. Chem. , vol.263 , pp. 9015-9019
    • Russel, M.1    Model, P.2
  • 33
    • 0029007418 scopus 로고
    • Purification and characterization of nitrobenzene nitroreductase from Pseudomonas pseudoalcaligenes JS45
    • Somerville, C. C., S. F. Nishino, and J. C. Spain. 1995. Purification and characterization of nitrobenzene nitroreductase from Pseudomonas pseudoalcaligenes JS45. J. Bacteriol. 177:3837-3842.
    • (1995) J. Bacteriol. , vol.177 , pp. 3837-3842
    • Somerville, C.C.1    Nishino, S.F.2    Spain, J.C.3
  • 34
    • 0002883224 scopus 로고
    • Bacterial degradation of nitroaromatic compounds under aerobic conditions
    • J. C. Spain (ed.), Plenum Press, New York
    • Spain, J. C. 1994. Bacterial degradation of nitroaromatic compounds under aerobic conditions, p. 19-35. In J. C. Spain (ed.), Biodegradation of nitroaromatic compounds. Plenum Press, New York.
    • (1994) Biodegradation of Nitroaromatic Compounds , pp. 19-35
    • Spain, J.C.1
  • 35
    • 0025777419 scopus 로고
    • Pathway for biodegradation of p-nitrophenol in a Moraxella sp
    • Spain, J. C., and D. T. Gibson. 1991. Pathway for biodegradation of p-nitrophenol in a Moraxella sp. Appl. Environ. Microbiol. 57:812-819.
    • (1991) Appl. Environ. Microbiol. , vol.57 , pp. 812-819
    • Spain, J.C.1    Gibson, D.T.2
  • 36
    • 0023240899 scopus 로고
    • Degradation of 1,4-dichlorobenzene by a Pseudomonas sp
    • Spain, J. C., and S. F. Nishino. 1987. Degradation of 1,4-dichlorobenzene by a Pseudomonas sp. Appl. Environ. Microbiol. 53:1010-1019.
    • (1987) Appl. Environ. Microbiol. , vol.53 , pp. 1010-1019
    • Spain, J.C.1    Nishino, S.F.2
  • 41
    • 0029779548 scopus 로고    scopus 로고
    • 2,4-Dinitrotoluene dioxygenase from Burkholderia sp. strain DNT: Similarity to naphthalene dioxygenase
    • Suen, W.-C., B. E. Haigler, and J. C. Spain. 1996. 2,4-Dinitrotoluene dioxygenase from Burkholderia sp. strain DNT: similarity to naphthalene dioxygenase. J. Bacteriol. 178:4926-4934.
    • (1996) J. Bacteriol. , vol.178 , pp. 4926-4934
    • Suen, W.-C.1    Haigler, B.E.2    Spain, J.C.3
  • 42
    • 85035179746 scopus 로고
    • 4-Methyl-5-nitrocatechol oxygenase catalyzes the oxidative removal of nitrite from an intermediate in 2,4-dinitrotoluene degradation by Pseudomonas sp. strain DNT
    • National Institute of Environmental Health Sciences. Superfund Basic Research Program. Research Triangle Park, North Carolina
    • Suen, W.-C., and J. C. Spain. 1993. 4-Methyl-5-nitrocatechol oxygenase catalyzes the oxidative removal of nitrite from an intermediate in 2,4-dinitrotoluene degradation by Pseudomonas sp. strain DNT, p. 51. In Symposium on biodegradation: its role in reducing toxicity and exposure to environmental contaminants. National Institute of Environmental Health Sciences. Superfund Basic Research Program. Research Triangle Park, North Carolina.
    • (1993) Symposium on Biodegradation: Its Role in Reducing Toxicity and Exposure to Environmental Contaminants , pp. 51
    • Suen, W.-C.1    Spain, J.C.2
  • 43
    • 10144257305 scopus 로고
    • Nucleotide sequence and overexpression of 2,4,5-trihydroxytoluene oxygenase gene from Pseudomonas sp. strain DNT in Escherichia coli, abstr. Q-318
    • American Society for Microbiology, Washington, D.C.
    • Suen, W.-C., and J. C. Spain. 1993. Nucleotide sequence and overexpression of 2,4,5-trihydroxytoluene oxygenase gene from Pseudomonas sp. strain DNT in Escherichia coli, abstr. Q-318, p. 404. In Abstracts of the 93rd General Meeting of the American Society for Microbiology 1993. American Society for Microbiology, Washington, D.C.
    • (1993) Abstracts of the 93rd General Meeting of the American Society for Microbiology 1993 , pp. 404
    • Suen, W.-C.1    Spain, J.C.2
  • 44
    • 0027404666 scopus 로고
    • Cloning and characterization of Pseudomonas sp. strain DNT genes for 2,4-dinitrotoluene degradation
    • Suen, W.-C., and J. C. Spain. 1993. Cloning and characterization of Pseudomonas sp. strain DNT genes for 2,4-dinitrotoluene degradation. J. Bacteriol. 175:1831-1837.
    • (1993) J. Bacteriol. , vol.175 , pp. 1831-1837
    • Suen, W.-C.1    Spain, J.C.2
  • 45
    • 0026088644 scopus 로고
    • Hydroxylation of o-halogenophenol and o-nitrophenol by salicylate hydroxylase
    • Suzuki, K., T. Gomi, T. Kaidoh, and E. Itagaki. 1991. Hydroxylation of o-halogenophenol and o-nitrophenol by salicylate hydroxylase. J. Biochem. 109:348-353.
    • (1991) J. Biochem. , vol.109 , pp. 348-353
    • Suzuki, K.1    Gomi, T.2    Kaidoh, T.3    Itagaki, E.4
  • 46
    • 0004135644 scopus 로고
    • W. H. Freeman and Company, San Francisco
    • Walsh, C. 1979. Enzymatic reaction mechanisms, p. 417. W. H. Freeman and Company, San Francisco.
    • (1979) Enzymatic Reaction Mechanisms , pp. 417
    • Walsh, C.1
  • 47
    • 0023041821 scopus 로고
    • Prediction of the occurrence of the ADP-binding βαβ-fold in proteins, using an amino acid sequence fingerprint
    • Wierenga, R. K., P. Terpstra, and W. G. J. Hol. 1986. Prediction of the occurrence of the ADP-binding βαβ-fold in proteins, using an amino acid sequence fingerprint. J. Mol. Biol. 187:101-107.
    • (1986) J. Mol. Biol. , vol.187 , pp. 101-107
    • Wierenga, R.K.1    Terpstra, P.2    Hol, W.G.J.3
  • 48
    • 0026770524 scopus 로고
    • Diverse substrate range of a Flavobacterium pentachlorophenol hydroxylase and reaction stoichiometries
    • Xun, L., E. Topp, and C. S. Orser. 1992. Diverse substrate range of a Flavobacterium pentachlorophenol hydroxylase and reaction stoichiometries. J. Bacteriol. 174:2898-2902.
    • (1992) J. Bacteriol. , vol.174 , pp. 2898-2902
    • Xun, L.1    Topp, E.2    Orser, C.S.3
  • 49
    • 0025801743 scopus 로고
    • Nucleotide sequence analysis of the Pseudomonas putida PpG7 salicylate hydroxylase gene (nahG) and its 3′-flanking region
    • You, I. S., D. Ghosal, and I. C. Gunsalus. 1991. Nucleotide sequence analysis of the Pseudomonas putida PpG7 salicylate hydroxylase gene (nahG) and its 3′-flanking region. Biochemistry 30:1635-1641.
    • (1991) Biochemistry , vol.30 , pp. 1635-1641
    • You, I.S.1    Ghosal, D.2    Gunsalus, I.C.3
  • 50
    • 0023896389 scopus 로고
    • Purification and characterization of a bacterial nitrophenol oxygenase which converts ortho-nitrophenol to catechol and nitrite
    • Zeyer, J., and H. P. Kocher. 1988. Purification and characterization of a bacterial nitrophenol oxygenase which converts ortho-nitrophenol to catechol and nitrite. J. Bacteriol. 170:1789-1794.
    • (1988) J. Bacteriol. , vol.170 , pp. 1789-1794
    • Zeyer, J.1    Kocher, H.P.2
  • 51
    • 0024427069 scopus 로고
    • Toluene degradation by Pseudomonas putida F1: Nucleotide sequence of the todC1C2BADE genes and their expression in Escherichia coli
    • Zylstra, G. J., and D. T. Gibson. 1989. Toluene degradation by Pseudomonas putida F1: nucleotide sequence of the todC1C2BADE genes and their expression in Escherichia coli. J. Biol. Chem. 264:14940-14946.
    • (1989) J. Biol. Chem. , vol.264 , pp. 14940-14946
    • Zylstra, G.J.1    Gibson, D.T.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.