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Volumn 182, Issue 7, 2000, Pages 1956-1963

Characterization of the gene cluster involved in isoprene metabolism in Rhodococcus sp. strain AD45

Author keywords

[No Author keywords available]

Indexed keywords

1 CHLORO 2,4 DINITROBENZENE; 1 HYDROXY 2 GLUTATHIONYL 2 METHYL 3 BUTENE; 1,2 DICHLORO 4 NITROBENZENE; 1,2 EPOXY 2 METHYL 3 BUTENE; 2 METHYLACYL COENZYME A RACEMASE; BACTERIAL DNA; GLUTATHIONE TRANSFERASE; ISOPRENE; OXIDOREDUCTASE; RACEMASE; UNCLASSIFIED DRUG; UNSPECIFIC MONOOXYGENASE;

EID: 0034020589     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.182.7.1956-1963.2000     Document Type: Article
Times cited : (78)

References (55)
  • 1
    • 0033587753 scopus 로고    scopus 로고
    • A role for coenzyme M 2-mercaptoethanesulfonic acid in a bacterial pathway of aliphatic epoxide carboxylation
    • Allen, J. R., D. D. Clark, J. G. Krum, and S. A. Ensign. 1999. A role for coenzyme M (2-mercaptoethanesulfonic acid in a bacterial pathway of aliphatic epoxide carboxylation. Proc. Natl. Acad. Sci. USA 96:8432-8447.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 8432-8447
    • Allen, J.R.1    Clark, D.D.2    Krum, J.G.3    Ensign, S.A.4
  • 2
    • 0033524404 scopus 로고    scopus 로고
    • Two short-chain dehydrogenases confer stereoselectivity for enantiomers of epoxypropane in the multiprotein epoxide carboxylating systems of Xanthobacter strain Py2 and Nocardia corallina B276
    • Allen, J. R., and S. A. Ensign. 1999. Two short-chain dehydrogenases confer stereoselectivity for enantiomers of epoxypropane in the multiprotein epoxide carboxylating systems of Xanthobacter strain Py2 and Nocardia corallina B276. Biochemistry 38:247-256.
    • (1999) Biochemistry , vol.38 , pp. 247-256
    • Allen, J.R.1    Ensign, S.A.2
  • 4
    • 0031021397 scopus 로고    scopus 로고
    • Structure, catalytic mechanism, and evolution of the glutathione 5-transferases
    • Armstrong, R. N. 1997. Structure, catalytic mechanism, and evolution of the glutathione 5-transferases. Chem. Res. Toxicol. 10:2-18.
    • (1997) Chem. Res. Toxicol. , vol.10 , pp. 2-18
    • Armstrong, R.N.1
  • 5
    • 0342618500 scopus 로고    scopus 로고
    • Fosfomycin resistance protein (FosA) is a manganese metalloglutathione transferase related to glyoxalase 1 and the extradiol dioxygenases
    • Bernat, A. B., L. T. Laughlin, and R. N. Armstrong. 1997. Fosfomycin resistance protein (FosA) is a manganese metalloglutathione transferase related to glyoxalase 1 and the extradiol dioxygenases. Biochemistry 36: 3050-3055.
    • (1997) Biochemistry , vol.36 , pp. 3050-3055
    • Bernat, A.B.1    Laughlin, L.T.2    Armstrong, R.N.3
  • 6
    • 0029101750 scopus 로고
    • Evidence for an essential serine residue in the active site of the theta class glutathione transferases
    • Board, P. G., M. Coggan, M. C. J. Wilce, and M. W. Parker. 1995. Evidence for an essential serine residue in the active site of the theta class glutathione transferases. Biochem. J. 311:247-250.
    • (1995) Biochem. J. , vol.311 , pp. 247-250
    • Board, P.G.1    Coggan, M.2    Wilce, M.C.J.3    Parker, M.W.4
  • 7
    • 0029035314 scopus 로고
    • Stereoselective catalysis of a retro-Michael reaction by mu class glutathione transferases. Consequences for the internal distribution of products in the active site
    • Chen, J., and R. N. Armstrong. 1995. Stereoselective catalysis of a retro-Michael reaction by mu class glutathione transferases. Consequences for the internal distribution of products in the active site. Chem. Res. Toxicol. 8:580-585.
    • (1995) Chem. Res. Toxicol. , vol.8 , pp. 580-585
    • Chen, J.1    Armstrong, R.N.2
  • 8
    • 0031985852 scopus 로고    scopus 로고
    • Microbial consumption of atmospheric isoprene in a temperate forest soil
    • Cleveland, C. C., and J. B. Yavitt. 1998. Microbial consumption of atmospheric isoprene in a temperate forest soil. Appl. Environ. Microbiol. 64: 172-177.
    • (1998) Appl. Environ. Microbiol. , vol.64 , pp. 172-177
    • Cleveland, C.C.1    Yavitt, J.B.2
  • 9
    • 0028960992 scopus 로고
    • Sequence analysis of a gene cluster involved in metabolism of 2,4,5-trichlorophenoxyacetic acid by Burkholderia cepacia AC1100
    • Daubaras, D. L., C. D. Hershberger, K. Kitano, and A. M. Chakrabarty. 1995. Sequence analysis of a gene cluster involved in metabolism of 2,4,5-trichlorophenoxyacetic acid by Burkholderia cepacia AC1100 . Appl. Environ. Microbiol. 61:1279-1289.
    • (1995) Appl. Environ. Microbiol. , vol.61 , pp. 1279-1289
    • Daubaras, D.L.1    Hershberger, C.D.2    Kitano, K.3    Chakrabarty, A.M.4
  • 10
    • 0028224013 scopus 로고
    • X-ray crystal structures of cytosolic glutathione S-transferases. Implications for protein architecture, substrate recognition and catalytic function
    • Dirr, H., P. Reinemer, and R. Huber. 1994. X-ray crystal structures of cytosolic glutathione S-transferases. Implications for protein architecture, substrate recognition and catalytic function. Eur. J. Biochem. 220:645-661.
    • (1994) Eur. J. Biochem. , vol.220 , pp. 645-661
    • Dirr, H.1    Reinemer, P.2    Huber, R.3
  • 11
  • 12
    • 0028227708 scopus 로고
    • Cloning, nucleotide sequence, and expression of the Esherichia coli gene encoding carnitine dehydratase
    • Eichler, K., W. H. Schunck, H. P. Kleber, and M. A. Mandrand-Berthelot. 1994. Cloning, nucleotide sequence, and expression of the Esherichia coli gene encoding carnitine dehydratase. J. Bacteriol. 176:2970-2975.
    • (1994) J. Bacteriol. , vol.176 , pp. 2970-2975
    • Eichler, K.1    Schunck, W.H.2    Kleber, H.P.3    Mandrand-Berthelot, M.A.4
  • 13
    • 0040685806 scopus 로고
    • Biodegradation of chloroethenes using isoprene as a co-substrate
    • H. Verachtert and W. Verstraete (ed.), Royal Flemish Society of Engineers, Oostende, Belgium
    • Ewers, J. W. C., and H.-J. Knackmuss. 1991. Biodegradation of chloroethenes using isoprene as a co-substrate, p. 77-83. In H. Verachtert and W. Verstraete (ed.), Proceedings of the International Symposium on Environmental Biotechnology. Royal Flemish Society of Engineers, Oostende, Belgium.
    • (1991) Proceedings of the International Symposium on Environmental Biotechnology , pp. 77-83
    • Ewers, J.W.C.1    Knackmuss, H.-J.2
  • 14
    • 0026715272 scopus 로고
    • The biology and genetics of the genus Rhodococcus
    • Finnerty, W. R. 1992. The biology and genetics of the genus Rhodococcus. Annu. Rev. Microbiol. 46:193-218.
    • (1992) Annu. Rev. Microbiol. , vol.46 , pp. 193-218
    • Finnerty, W.R.1
  • 15
    • 0030837904 scopus 로고    scopus 로고
    • Alkene monooxygenase from Nocardia corallina B-276 is a member of the class of dinuclear iron proteins capable of stereospecific epoxygenation reactions
    • Gallagher, S. C., R. Cammack, and H. Dalton. 1997. Alkene monooxygenase from Nocardia corallina B-276 is a member of the class of dinuclear iron proteins capable of stereospecific epoxygenation reactions. Eur. J. Biochem. 247:635-641.
    • (1997) Eur. J. Biochem. , vol.247 , pp. 635-641
    • Gallagher, S.C.1    Cammack, R.2    Dalton, H.3
  • 16
    • 0016275313 scopus 로고
    • Glutathione S-transferases. The first enzymatic step in mercapturic acid formation
    • Habig, W. H., M. J. Pabst, and W. B. Jakoby. 1974. Glutathione S-transferases. The first enzymatic step in mercapturic acid formation. J. Biol. Chem. 249:7130-7139.
    • (1974) J. Biol. Chem. , vol.249 , pp. 7130-7139
    • Habig, W.H.1    Pabst, M.J.2    Jakoby, W.B.3
  • 17
    • 0026458378 scopus 로고
    • Amino acid substitution matrices from protein blocks
    • Henikoff, J. G. 1992. Amino acid substitution matrices from protein blocks. Proc. Natl. Acad. Sci. USA 89:10915-10919.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 10915-10919
    • Henikoff, J.G.1
  • 18
    • 0002367719 scopus 로고
    • A guide to methods and amplification
    • M. A. Innis, D. H. Gelfand, J. J. Sninsky, and T. J. White (ed.). Academic Press, San Diego, Calif.
    • Innis, M. A., and D. H. Gelfand. 1990. A guide to methods and amplification, p. 3-11. In M. A. Innis, D. H. Gelfand, J. J. Sninsky, and T. J. White (ed.). PCR protocols. Academic Press, San Diego, Calif.
    • (1990) PCR Protocols , pp. 3-11
    • Innis, M.A.1    Gelfand, D.H.2
  • 19
    • 0026348175 scopus 로고
    • Characterization of the epoxide hydrolase from an epichlorohydrin-degrading Pseudomonas sp.
    • Jacobs, M. H., A. J. van den Wijngaard, M. Pentenga, and D. B. Jamsen. 1991. Characterization of the epoxide hydrolase from an epichlorohydrin-degrading Pseudomonas sp. Eur. J. Biochem. 202:1217-1222.
    • (1991) Eur. J. Biochem. , vol.202 , pp. 1217-1222
    • Jacobs, M.H.1    Van Den Wijngaard, A.J.2    Pentenga, M.3    Jamsen, D.B.4
  • 22
    • 0032512591 scopus 로고    scopus 로고
    • Enantioselectivity of a recombinant epoxide hydrolase from Agrobacterium radiobacter
    • Lutje Spelberg, J. H., R. Rink, R. Kellogg, and D. B. Janssen. 1998. Enantioselectivity of a recombinant epoxide hydrolase from Agrobacterium radiobacter. Tetrahedron Asymmetry 9:459-482.
    • (1998) Tetrahedron Asymmetry , vol.9 , pp. 459-482
    • Lutje Spelberg, J.H.1    Rink, R.2    Kellogg, R.3    Janssen, D.B.4
  • 23
    • 0026340042 scopus 로고
    • Cloning and sequencing of the gene for a Pseudomonas paucimobilis enzyme that cleaves β-aryl ether
    • Masai, E., Y. Katayama, S. Kawai, S. Nishikawa, M. Yamasaki, and N. Morohoshi. 1991. Cloning and sequencing of the gene for a Pseudomonas paucimobilis enzyme that cleaves β-aryl ether. J. Bacteriol. 173:7950-7955.
    • (1991) J. Bacteriol. , vol.173 , pp. 7950-7955
    • Masai, E.1    Katayama, Y.2    Kawai, S.3    Nishikawa, S.4    Yamasaki, M.5    Morohoshi, N.6
  • 24
    • 0027223168 scopus 로고
    • A bacterial enzyme degrading the model lignin compound β-etherase is a member of the glutathione S-transferase superfamily
    • Masai, E., Y. Katayama, S. Kubota, S. Kawai, M. Yamasaki, and N. Morohoshi. 1993. A bacterial enzyme degrading the model lignin compound β-etherase is a member of the glutathione S-transferase superfamily. FEBS Lett. 323:135-140.
    • (1993) FEBS Lett. , vol.323 , pp. 135-140
    • Masai, E.1    Katayama, Y.2    Kubota, S.3    Kawai, S.4    Yamasaki, M.5    Morohoshi, N.6
  • 25
    • 0017163169 scopus 로고
    • Branched-chain amino acid catabolism in bacteria
    • Massey, L. K., J. R. Sokatch, and R. S. Conrad. 1976. Branched-chain amino acid catabolism in bacteria. Bacteriol. Rev. 40:42-54.
    • (1976) Bacteriol. Rev. , vol.40 , pp. 42-54
    • Massey, L.K.1    Sokatch, J.R.2    Conrad, R.S.3
  • 26
    • 0039001059 scopus 로고
    • Improved double-stranded DNA sequencing using the linear polymerase chain reaction
    • Murray, V. 1989. Improved double-stranded DNA sequencing using the linear polymerase chain reaction. Nucleic Acids Res. 17:8889.
    • (1989) Nucleic Acids Res. , vol.17 , pp. 8889
    • Murray, V.1
  • 27
    • 0030678622 scopus 로고    scopus 로고
    • Indigo formation by microorganisms expressing styrene monooxygenase activity
    • O'Connor, K. E., A. D. Dobson, and S. Hartmans. 1997. Indigo formation by microorganisms expressing styrene monooxygenase activity. Appl. Environ. Microbiol. 63:4287-4291.
    • (1997) Appl. Environ. Microbiol. , vol.63 , pp. 4287-4291
    • O'Connor, K.E.1    Dobson, A.D.2    Hartmans, S.3
  • 28
    • 0029942829 scopus 로고    scopus 로고
    • Recombinant toluene-4-monooxygenase: Catalytic and Mössbauer studies of the purified diiron and Rieske components of a four-protein complex
    • Pikus, J. D., J. M. Studs, C. Achim, K. E. Kauffmann, E. Münck, R. J. Steffan, K. McClay, and G. Fox. 1996. Recombinant toluene-4-monooxygenase: catalytic and Mössbauer studies of the purified diiron and Rieske components of a four-protein complex. Biochemistry 35:9106-9119.
    • (1996) Biochemistry , vol.35 , pp. 9106-9119
    • Pikus, J.D.1    Studs, J.M.2    Achim, C.3    Kauffmann, K.E.4    Münck, E.5    Steffan, R.J.6    McClay, K.7    Fox, G.8
  • 29
    • 0022555852 scopus 로고
    • Transcription termination and the regulation of gene expression
    • Platt, T. 1986. Transcription termination and the regulation of gene expression. Annu. Rev. Biochem. 55:339-372.
    • (1986) Annu. Rev. Biochem. , vol.55 , pp. 339-372
    • Platt, T.1
  • 30
    • 0028585853 scopus 로고
    • Cloning and characterization of a Nocardia corallina B-276 gene cluster encoding alkene monooxygenase
    • Saeki, H., and K. Furuhashi. 1994. Cloning and characterization of a Nocardia corallina B-276 gene cluster encoding alkene monooxygenase. J. Ferment. Bioeng. 78:339-406.
    • (1994) J. Ferment. Bioeng. , vol.78 , pp. 339-406
    • Saeki, H.1    Furuhashi, K.2
  • 32
    • 0027674250 scopus 로고
    • Construction of an expression and site-directed mutagenesis system of haloalkane dehalogenase in Escherichia coli
    • Schanstra, J. P., R. Rink, F. Pries, and D. B. Janssen. 1993. Construction of an expression and site-directed mutagenesis system of haloalkane dehalogenase in Escherichia coli. Protein Expr. Purif. 4:479-489.
    • (1993) Protein Expr. Purif. , vol.4 , pp. 479-489
    • Schanstra, J.P.1    Rink, R.2    Pries, F.3    Janssen, D.B.4
  • 33
    • 0028176487 scopus 로고
    • Purification and properties of α-methylacyl-CoA racemase from rat liver
    • Schmitz, W., R. Fingerhut, and E. Conzelmann. 1994. Purification and properties of α-methylacyl-CoA racemase from rat liver. Eur. J. Biochem. 222: 313-323.
    • (1994) Eur. J. Biochem. , vol.222 , pp. 313-323
    • Schmitz, W.1    Fingerhut, R.2    Conzelmann, E.3
  • 34
    • 0030821703 scopus 로고    scopus 로고
    • Molecular cloning of cDNA species for rat and mouse liver-methylacyl-CoA racemases
    • Schmitz, W., H. M. Helander, J. K. Hiltunen, and E. Conzelmann. 1997 Molecular cloning of cDNA species for rat and mouse liver-methylacyl-CoA racemases. Biochem. J. 326:883-889.
    • (1997) Biochem. J. , vol.326 , pp. 883-889
    • Schmitz, W.1    Helander, H.M.2    Hiltunen, J.K.3    Conzelmann, E.4
  • 35
    • 0030512257 scopus 로고    scopus 로고
    • Isoprene synthesis by plants and animals
    • Sharkey, T. D. 1996. Isoprene synthesis by plants and animals. Endeavour (Oxford) 20:74-78.
    • (1996) Endeavour (Oxford) , vol.20 , pp. 74-78
    • Sharkey, T.D.1
  • 36
    • 0030995329 scopus 로고    scopus 로고
    • DNA sequencing and expression of the formyl coenzyme A transferase gene, frc, from Oxalobacter fonnigenes
    • Sidhu, H., S. D. Ogden, H. Y. Lung, B. G. Luttge, A. L. Baetz, and A. B. Peck. 1997. DNA sequencing and expression of the formyl coenzyme A transferase gene, frc, from Oxalobacter fonnigenes. J. Bacteriol. 179:3378-3381.
    • (1997) J. Bacteriol. , vol.179 , pp. 3378-3381
    • Sidhu, H.1    Ogden, S.D.2    Lung, H.Y.3    Luttge, B.G.4    Baetz, A.L.5    Peck, A.B.6
  • 37
    • 0030803666 scopus 로고    scopus 로고
    • Alkene monooxygenase from Xanthobacter strain Py2. Purification and characterization of a four-component system central to the bacterial metabolism of aliphatic alkenes
    • Small, F. J., and S. A. Ensign. 1997. Alkene monooxygenase from Xanthobacter strain Py2. Purification and characterization of a four-component system central to the bacterial metabolism of aliphatic alkenes. J. Biol. Chem. 272:24913-24920.
    • (1997) J. Biol. Chem. , vol.272 , pp. 24913-24920
    • Small, F.J.1    Ensign, S.A.2
  • 38
    • 0025006802 scopus 로고
    • The methane monooxygenase gene cluster of Methylococcus capsulatus (Bath)
    • Stainthorpe, A. C., V. Lees, G. P. Salmond, H. Dalton, and J. C. Murrell. 1990. The methane monooxygenase gene cluster of Methylococcus capsulatus (Bath). Gene 91:27-34.
    • (1990) Gene , vol.91 , pp. 27-34
    • Stainthorpe, A.C.1    Lees, V.2    Salmond, G.P.3    Dalton, H.4    Murrell, J.C.5
  • 39
    • 0023506006 scopus 로고
    • Molecular characterization of cloned avirulence genes from race 0 and race 1 of Pseudomonas syringae pv. glycinea
    • Staskawicz, B., D. Dahlbeck, N. Keen, and C. Napoli. 1987. Molecular characterization of cloned avirulence genes from race 0 and race 1 of Pseudomonas syringae pv. glycinea. J. Bacteriol. 169:5789-5794.
    • (1987) J. Bacteriol. , vol.169 , pp. 5789-5794
    • Staskawicz, B.1    Dahlbeck, D.2    Keen, N.3    Napoli, C.4
  • 40
    • 0028960645 scopus 로고
    • Complementation of Xanthobacter Py2 mutants defective in epoxyalkane degradation, and expression and nucleotide sequence of the complementing DNA fragment
    • Swaving, J., C. A. Webers, A. J. van Ooyen, and J. A. M. de Bont. 1995. Complementation of Xanthobacter Py2 mutants defective in epoxyalkane degradation, and expression and nucleotide sequence of the complementing DNA fragment. Microbiology 141:477-484.
    • (1995) Microbiology , vol.141 , pp. 477-484
    • Swaving, J.1    Webers, C.A.2    Van Ooyen, A.J.3    De Bont, J.A.M.4
  • 41
    • 0030000879 scopus 로고    scopus 로고
    • Crystal structures of the binary and ternary complexes of 7alpha-hydroxysteroid dehydrogenase from Escherichia coli
    • Tanaka, N., T. Nonaka, T. Tanabe, T. Yoshimoto, D. Tsuru, and Y. Mitsui. 1996. Crystal structures of the binary and ternary complexes of 7alpha-hydroxysteroid dehydrogenase from Escherichia coli. Biochemistry 35:7715-7730.
    • (1996) Biochemistry , vol.35 , pp. 7715-7730
    • Tanaka, N.1    Nonaka, T.2    Tanabe, T.3    Yoshimoto, T.4    Tsuru, D.5    Mitsui, Y.6
  • 42
    • 0026611538 scopus 로고
    • The oxidizing capacity of earth's atmosphere; probable past and future changes
    • Thompson, A. M. 1992. The oxidizing capacity of earth's atmosphere; probable past and future changes. Science 256:1157-1165.
    • (1992) Science , vol.256 , pp. 1157-1165
    • Thompson, A.M.1
  • 43
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson, J. D., D. G. Higgins, and T. J. Gibson. 1994. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22:4673-4680.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 44
    • 0006922045 scopus 로고
    • Microbial oxidation of isoprene, a biogenic foliage volatile, and of 1,3-butadiene, an anthropogenic gas
    • van Ginkel, C. G., E. de Jong, J. W. R. Tilanus, and J. A. M. de Bont. 1987. Microbial oxidation of isoprene, a biogenic foliage volatile, and of 1,3-butadiene, an anthropogenic gas. FEMS Microbiol. Ecol. 45:275-279.
    • (1987) FEMS Microbiol. Ecol. , vol.45 , pp. 275-279
    • Van Ginkel, C.G.1    De Jong, E.2    Tilanus, J.W.R.3    De Bont, J.A.M.4
  • 45
    • 0031879205 scopus 로고    scopus 로고
    • A glutathione S-transferase with activity towards cis-1,2-dichloroepoxyethane is involved in isoprene utilization by Rhodococcus sp. strain AD45
    • van Hylckama Vlieg, J. E. T., J. Kingma, A. J. van den Wijngaard, and D. B. Janssen. 1998. A glutathione S-transferase with activity towards cis-1,2-dichloroepoxyethane is involved in isoprene utilization by Rhodococcus sp. strain AD45. Appl. Environ. Microbiol. 64:2800-2805.
    • (1998) Appl. Environ. Microbiol. , vol.64 , pp. 2800-2805
    • Van Hylckama Vlieg, J.E.T.1    Kingma, J.2    Van Den Wijngaard, A.J.3    Janssen, D.B.4
  • 46
    • 0032956206 scopus 로고    scopus 로고
    • Purification of a glutathione S-transferase and dehydrogenase involved in isoprene metabolism in Rhodococcus sp. strain AD45
    • van Hylckama Vlieg, J. E. T., J. Kingma, W. Kruizinga, and D. B. Janssen. 1999. Purification of a glutathione S-transferase and dehydrogenase involved in isoprene metabolism in Rhodococcus sp. strain AD45. J. Bacteriol. 181: 2094-2101.
    • (1999) J. Bacteriol. , vol.181 , pp. 2094-2101
    • Van Hylckama Vlieg, J.E.T.1    Kingma, J.2    Kruizinga, W.3    Janssen, D.B.4
  • 47
    • 0030844081 scopus 로고    scopus 로고
    • Effect of chlorinated ethene conversion on viability and activity of Methylosinus trichosporium OB3b
    • van Hylckama Vlieg, J. E. T., W. de Koning, and D. B. Janssen. 1997. Effect of chlorinated ethene conversion on viability and activity of Methylosinus trichosporium OB3b. Appl. Environ. Microbiol. 63:4961-4964.
    • (1997) Appl. Environ. Microbiol. , vol.63 , pp. 4961-4964
    • Van Hylckama Vlieg, J.E.T.1    De Koning, W.2    Janssen, D.B.3
  • 48
    • 0031056720 scopus 로고    scopus 로고
    • Bacterial glutathione S-transferases: What are they good for?
    • Vuilleumier, S. 1997. Bacterial glutathione S-transferases: what are they good for? J. Bacteriol. 179:1431-1441.
    • (1997) J. Bacteriol. , vol.179 , pp. 1431-1441
    • Vuilleumier, S.1
  • 49
    • 0030037613 scopus 로고    scopus 로고
    • Protein engineering studies of dichloromethane dehalogenase/glutathione S-transferase from Methylophilus sp. strain DM11. Ser12 but not Tyr6 is required for enzyme activity
    • Vuilleumier, S., and T. Leisinger. 1996. Protein engineering studies of dichloromethane dehalogenase/glutathione S-transferase from Methylophilus sp. strain DM11. Ser12 but not Tyr6 is required for enzyme activity. Eur. J. Biochem. 239:410-417.
    • (1996) Eur. J. Biochem. , vol.239 , pp. 410-417
    • Vuilleumier, S.1    Leisinger, T.2
  • 50
    • 0032802573 scopus 로고    scopus 로고
    • Three distinct phases of isoprene formation during growth and sporulation of Bacillus subtilis
    • Wagner, W. P., M. Nemecek, and R. Fall. 1999. Three distinct phases of isoprene formation during growth and sporulation of Bacillus subtilis. J. Bacteriol. 181:4700-4703.
    • (1999) J. Bacteriol. , vol.181 , pp. 4700-4703
    • Wagner, W.P.1    Nemecek, M.2    Fall, R.3
  • 51
    • 0028223369 scopus 로고
    • Stereoselectivity of in vitro isoprene metabolism
    • Wistuba, D., K. Weigand, and H. Peter. 1994. Stereoselectivity of in vitro isoprene metabolism. Chem. Res. Toxicol. 7:336-343.
    • (1994) Chem. Res. Toxicol. , vol.7 , pp. 336-343
    • Wistuba, D.1    Weigand, K.2    Peter, H.3
  • 53
    • 0026595293 scopus 로고
    • Identification of a new gene, tmoF, in the Pseudomonas mendocina KR1 gene cluster encoding toluene-4-monooxygenase
    • Yen, K. M., and M. R. Karl. 1992. Identification of a new gene, tmoF, in the Pseudomonas mendocina KR1 gene cluster encoding toluene-4-monooxygenase. J. Bacteriol. 174:7253-7261.
    • (1992) J. Bacteriol. , vol.174 , pp. 7253-7261
    • Yen, K.M.1    Karl, M.R.2
  • 54
    • 9044246676 scopus 로고    scopus 로고
    • Cloning and expression of the genes encoding the propene monooxygenase from Xanthobacter, Py2
    • Zhou, N.-Y., C. K. N. Chan Kwo Chion, and D. J. Leak. 1996. Cloning and expression of the genes encoding the propene monooxygenase from Xanthobacter, Py2. Appl. Microbiol. Biotechnol. 44:582-588.
    • (1996) Appl. Microbiol. Biotechnol. , vol.44 , pp. 582-588
    • Zhou, N.-Y.1    Chan Kwo Chion, C.K.N.2    Leak, D.J.3
  • 55
    • 0032943262 scopus 로고    scopus 로고
    • The alkene monooxygenase from Xanthobacter strain Py2 is closely related to aromatic monooxygenases and catalyzes aromatic monohydroxylation of benzene, toluene, and phenol
    • Zhou, N.-Y., C. K. N. Chan Kwo Chion, and D. J. Leak. 1999. The alkene monooxygenase from Xanthobacter strain Py2 is closely related to aromatic monooxygenases and catalyzes aromatic monohydroxylation of benzene, toluene, and phenol. Appl. Environ. Microbiol. 65:1589-1595.
    • (1999) Appl. Environ. Microbiol. , vol.65 , pp. 1589-1595
    • Zhou, N.-Y.1    Chan Kwo Chion, C.K.N.2    Leak, D.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.