메뉴 건너뛰기




Volumn 250, Issue 1, 2005, Pages 111-116

Product and product-independent induction of butane oxidation in Pseudomonas butanovora

Author keywords

Induction of sBMO; Pseudomonas butanovora; sBMO reporter strain; Soluble butane monooxygenase

Indexed keywords

BETA GALACTOSIDASE; BUTANE; BUTANOL; BUTYRALDEHYDE; ETHYLENE OXIDE; OXYGENASE; SOLUBLE BUTANE MONOOXYGENASE; UNCLASSIFIED DRUG; UNSPECIFIC MONOOXYGENASE;

EID: 23844451450     PISSN: 03781097     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.femsle.2005.06.058     Document Type: Article
Times cited : (16)

References (38)
  • 3
    • 0036209594 scopus 로고    scopus 로고
    • Two distinct alcohol dehydrogenases participate in butane metabolism in Pseudomonas butanovora
    • A.S. Vangnai, D.J. Arp, and L.A. Sayavedra-Soto Two distinct alcohol dehydrogenases participate in butane metabolism in Pseudomonas butanovora J. Bacteriol. 184 2002 1916 1924
    • (2002) J. Bacteriol. , vol.184 , pp. 1916-1924
    • Vangnai, A.S.1    Arp, D.J.2    Sayavedra-Soto, L.A.3
  • 4
    • 0036330063 scopus 로고    scopus 로고
    • Roles for the two 1-butanol dehydrogenases of Pseudomonas butanovora in butane and 1-butanol metabolism
    • A.S. Vangnai, L.A. Sayavedra-Soto, and D.J. Arp Roles for the two 1-butanol dehydrogenases of Pseudomonas butanovora in butane and 1-butanol metabolism J. Bacteriol. 184 2002 4343 4350
    • (2002) J. Bacteriol. , vol.184 , pp. 4343-4350
    • Vangnai, A.S.1    Sayavedra-Soto, L.A.2    Arp, D.J.3
  • 5
    • 0032898421 scopus 로고    scopus 로고
    • Butane metabolism by butane-grown Pseudomonas butanovora
    • D.J. Arp Butane metabolism by butane-grown Pseudomonas butanovora Microbiology 145 1999 1173 1180
    • (1999) Microbiology , vol.145 , pp. 1173-1180
    • Arp, D.J.1
  • 6
    • 0036855417 scopus 로고    scopus 로고
    • Molecular analysis of the soluble butane monooxygenase from Pseudomonas butanovora
    • M.K. Sluis, L.A. Sayavedra-Soto, and D.J. Arp Molecular analysis of the soluble butane monooxygenase from Pseudomonas butanovora Microbiology 148 2002 3617 3629
    • (2002) Microbiology , vol.148 , pp. 3617-3629
    • Sluis, M.K.1    Sayavedra-Soto, L.A.2    Arp, D.J.3
  • 7
    • 0026522509 scopus 로고
    • Genetic, biochemical and immunological evidence for the involvement of two alcohol dehydrogenases in the metabolism of propane by Rhodococcus rhodochrous PNKb1
    • W. Ashraf, and J.C. Murrell Genetic, biochemical and immunological evidence for the involvement of two alcohol dehydrogenases in the metabolism of propane by Rhodococcus rhodochrous PNKb1 Arch. Microbiol. 157 1992 488 492
    • (1992) Arch. Microbiol. , vol.157 , pp. 488-492
    • Ashraf, W.1    Murrell, J.C.2
  • 8
    • 0029031697 scopus 로고
    • Three distinct quinoprotein alcohol dehydrogenases are expressed when Pseudomonas putida is grown on different alcohols
    • H. Toyama, A. Fujii, K. Matsushita, E. Shinagawa, M. Ameyama, and O. Adachi Three distinct quinoprotein alcohol dehydrogenases are expressed when Pseudomonas putida is grown on different alcohols J. Bacteriol. 177 1995 2442 2450
    • (1995) J. Bacteriol. , vol.177 , pp. 2442-2450
    • Toyama, H.1    Fujii, A.2    Matsushita, K.3    Shinagawa, E.4    Ameyama, M.5    Adachi, O.6
  • 10
    • 0002187879 scopus 로고
    • Propane utilization by microorganisms
    • J.J. Perry Propane utilization by microorganisms Adv. Appl. Microbiol. 26 1980 89 115
    • (1980) Adv. Appl. Microbiol. , vol.26 , pp. 89-115
    • Perry, J.J.1
  • 11
    • 0015383749 scopus 로고
    • Isolation and characterization of n-butane-utilizing microorganisms
    • A.G. McLee, A.C. Kormendy, and M. Wayman Isolation and characterization of n-butane-utilizing microorganisms Can. J. Microbiol. 18 1972 1191 1195
    • (1972) Can. J. Microbiol. , vol.18 , pp. 1191-1195
    • McLee, A.G.1    Kormendy, A.C.2    Wayman, M.3
  • 12
    • 0034086965 scopus 로고    scopus 로고
    • Molecular biology and regulation of methane monooxygenase
    • J.C. Murrell, B. Gilbert, and I.R. McDonald Molecular biology and regulation of methane monooxygenase Arch. Microbiol. 173 2000 325 332
    • (2000) Arch. Microbiol. , vol.173 , pp. 325-332
    • Murrell, J.C.1    Gilbert, B.2    McDonald, I.R.3
  • 13
    • 50549177801 scopus 로고
    • Hydrocarbon oxidation by a bacterial enzyme system. I. Products of octane oxidation
    • J.N. Baptist, R.K. Gholson, and M.J. Coon Hydrocarbon oxidation by a bacterial enzyme system. I. Products of octane oxidation Biochim. Biophys. Acta 69 1963 40 47
    • (1963) Biochim. Biophys. Acta , vol.69 , pp. 40-47
    • Baptist, J.N.1    Gholson, R.K.2    Coon, M.J.3
  • 14
    • 0020559210 scopus 로고
    • Copper stress underlines the fundamental change in intracellular location of methane mono-oxygenase in methane utilizing organisms: Studies in batch and continuous cultures
    • S.H. Stanley, D.J. Prior, D.J. Leak, and H. Dalton Copper stress underlines the fundamental change in intracellular location of methane mono-oxygenase in methane utilizing organisms: studies in batch and continuous cultures Biotechnol. Lett. 5 1983 487 492
    • (1983) Biotechnol. Lett. , vol.5 , pp. 487-492
    • Stanley, S.H.1    Prior, D.J.2    Leak, D.J.3    Dalton, H.4
  • 15
    • 0024978652 scopus 로고
    • Substrate specificity of soluble methane monooxygenase. Mechanistic implications
    • J. Green, and H. Dalton Substrate specificity of soluble methane monooxygenase. Mechanistic implications J. Biol. Chem. 264 1989 17698 17703
    • (1989) J. Biol. Chem. , vol.264 , pp. 17698-17703
    • Green, J.1    Dalton, H.2
  • 16
    • 0034192166 scopus 로고    scopus 로고
    • Regulation of expression of methane monooxygenases by copper ions
    • J.C. Murrell, I.R. McDonald, and B. Gilbert Regulation of expression of methane monooxygenases by copper ions Trends Microbiol. 8 2000 221 225
    • (2000) Trends Microbiol. , vol.8 , pp. 221-225
    • Murrell, J.C.1    McDonald, I.R.2    Gilbert, B.3
  • 17
    • 0034969905 scopus 로고    scopus 로고
    • Analysis of Pseudomonas putida alkane-degradation gene clusters and flanking insertion sequences: Evolution and regulation of the alk genes
    • J.B. van Beilen, S. Panke, S. Lucchini, A.G. Franchini, M. Rothlisberger, and B. Witholt Analysis of Pseudomonas putida alkane-degradation gene clusters and flanking insertion sequences: evolution and regulation of the alk genes Microbiology 147 2001 1621 1630
    • (2001) Microbiology , vol.147 , pp. 1621-1630
    • Van Beilen, J.B.1    Panke, S.2    Lucchini, S.3    Franchini, A.G.4    Rothlisberger, M.5    Witholt, B.6
  • 18
    • 0028672044 scopus 로고
    • Genetics of alkane oxidation by Pseudomonas oleovorans
    • J.B. van Beilen, M.G. Wubbolts, and B. Witholt Genetics of alkane oxidation by Pseudomonas oleovorans Biodegradation 5 1994 161 174
    • (1994) Biodegradation , vol.5 , pp. 161-174
    • Van Beilen, J.B.1    Wubbolts, M.G.2    Witholt, B.3
  • 19
    • 0024556880 scopus 로고
    • The Pseudomonas oleovorans alkBAC operon encodes two structurally related rubredoxins and aldehyde dehydrogenase
    • M. Kok, R. Oldenhuis, M.P.G. van der Linden, C.H.C. Meulenberg, J. Kingma, and B. Witholt The Pseudomonas oleovorans alkBAC operon encodes two structurally related rubredoxins and aldehyde dehydrogenase J. Biol. Chem. 264 1989 5442 5451
    • (1989) J. Biol. Chem. , vol.264 , pp. 5442-5451
    • Kok, M.1    Oldenhuis, R.2    Van Der Linden, M.P.G.3    Meulenberg, C.H.C.4    Kingma, J.5    Witholt, B.6
  • 22
    • 0015500791 scopus 로고
    • Enzymatic ω-oxidation. VI. Isolation of homogeneous reduced diphosphopyrideine nucleotide-rubredoxin reductase
    • T. Ueda, E.T. Lode, and M.J. Coon Enzymatic ω-oxidation. VI. Isolation of homogeneous reduced diphosphopyrideine nucleotide-rubredoxin reductase J. Biol. Chem. 247 1972 2109 2116
    • (1972) J. Biol. Chem. , vol.247 , pp. 2109-2116
    • Ueda, T.1    Lode, E.T.2    Coon, M.J.3
  • 23
    • 0014939950 scopus 로고
    • Enzymatic ω-oxidation. IV. Purification and properties of the ω-hydroxylase of Pseudomonas oleovorans
    • E.V. McKenna, and M.J. Coon Enzymatic ω-oxidation. IV. Purification and properties of the ω-hydroxylase of Pseudomonas oleovorans J. Biol. Chem. 245 1970 3882 3889
    • (1970) J. Biol. Chem. , vol.245 , pp. 3882-3889
    • McKenna, E.V.1    Coon, M.J.2
  • 24
    • 0345451054 scopus 로고    scopus 로고
    • Alkane hydroxylase from Acinetobacter sp. strain ADP1 is encoded by alkM and belongs to a new family of bacterial integral-membrane hydrocarbon hydroxylases
    • A. Ratajczak, W. Geissdorfer, and W. Hillen Alkane hydroxylase from Acinetobacter sp. strain ADP1 is encoded by alkM and belongs to a new family of bacterial integral-membrane hydrocarbon hydroxylases Appl. Environ. Microbiol. 64 1998 1175 1179
    • (1998) Appl. Environ. Microbiol. , vol.64 , pp. 1175-1179
    • Ratajczak, A.1    Geissdorfer, W.2    Hillen, W.3
  • 25
    • 0031791390 scopus 로고    scopus 로고
    • Expression of alkane hydroxylase from Acinetobacter sp. Strain ADP1 is induced by a broad range of n-alkanes and requires the transcriptional activator AlkR
    • A. Ratajczak, W. Geissdörfer, and W. Hillen Expression of alkane hydroxylase from Acinetobacter sp. Strain ADP1 is induced by a broad range of n-alkanes and requires the transcriptional activator AlkR J. Bacteriol. 180 1998 5822 5827
    • (1998) J. Bacteriol. , vol.180 , pp. 5822-5827
    • Ratajczak, A.1    Geissdörfer, W.2    Hillen, W.3
  • 27
    • 0031691310 scopus 로고    scopus 로고
    • Carbon-source-dependent expression of the PalkB promoter from the Pseudomonas oleovorans alkane degradation pathway
    • L. Yuste, I. Canosa, and F. Rojo Carbon-source-dependent expression of the PalkB promoter from the Pseudomonas oleovorans alkane degradation pathway J. Bacteriol. 180 1998 5218 5226
    • (1998) J. Bacteriol. , vol.180 , pp. 5218-5226
    • Yuste, L.1    Canosa, I.2    Rojo, F.3
  • 28
    • 0034920233 scopus 로고    scopus 로고
    • Induction of butane consumption in Pseudomonas butanovora
    • L.A. Sayavedra-Soto, C.M. Byrd, and D.J. Arp Induction of butane consumption in Pseudomonas butanovora Arch. Microbiol. 176 2001 114 120
    • (2001) Arch. Microbiol. , vol.176 , pp. 114-120
    • Sayavedra-Soto, L.A.1    Byrd, C.M.2    Arp, D.J.3
  • 29
    • 0030799165 scopus 로고    scopus 로고
    • Chloroform cometabolism by butane-grown CF8, Pseudomonas butanovora, and Mycobacterium vaccae JOB5 and methane-grown Methylosinus trichosporium OB3b
    • N. Hamamura, C. Page, T. Long, L. Semprini, and D.J. Arp Chloroform cometabolism by butane-grown CF8, Pseudomonas butanovora, and Mycobacterium vaccae JOB5 and methane-grown Methylosinus trichosporium OB3b Appl. Environ. Microbiol. 63 1997 3607 3613
    • (1997) Appl. Environ. Microbiol. , vol.63 , pp. 3607-3613
    • Hamamura, N.1    Page, C.2    Long, T.3    Semprini, L.4    Arp, D.J.5
  • 30
    • 0019293840 scopus 로고
    • A new route for ethylene glycol metabolism in Mycobacterium E44
    • W.W. Wiegant, and J.A.M.d. Bont A new route for ethylene glycol metabolism in Mycobacterium E44 J. Gen. Microbiol. 120 1980 325 331
    • (1980) J. Gen. Microbiol. , vol.120 , pp. 325-331
    • Wiegant, W.W.1    d Bont, J.A.M.2
  • 31
    • 0024787144 scopus 로고
    • Construction of a lacZ-kanamycin-resistance cassette, useful for site-directed and as a promoter probe
    • W. Kokotek, and W. Lotz Construction of a lacZ-kanamycin-resistance cassette, useful for site-directed and as a promoter probe Gene 84 1989 467 471
    • (1989) Gene , vol.84 , pp. 467-471
    • Kokotek, W.1    Lotz, W.2
  • 33
    • 29744466425 scopus 로고
    • Determination of serum proteins by means of the Biuret reaction
    • A.G. Gornall, C.J. Bardawill, and M.M. David Determination of serum proteins by means of the Biuret reaction J. Biol. Chem. 177 1949 751 766
    • (1949) J. Biol. Chem. , vol.177 , pp. 751-766
    • Gornall, A.G.1    Bardawill, C.J.2    David, M.M.3
  • 34
    • 0001165802 scopus 로고
    • Purification, composition, and molecular weight of the β-galactosidase of Escherichia coli K12
    • G.R. Craven, E. Steers Jr., and C.B. Anfinsen Purification, composition, and molecular weight of the β-galactosidase of Escherichia coli K12 J. Biol. Chem. 240 1965 2468 2477
    • (1965) J. Biol. Chem. , vol.240 , pp. 2468-2477
    • Craven, G.R.1    Steers Jr., E.2    Anfinsen, C.B.3
  • 35
    • 0020645052 scopus 로고
    • Yeast promoters and lacZ fusions designed to study expression of cloned genes in yeast
    • L. Guarente Yeast promoters and lacZ fusions designed to study expression of cloned genes in yeast Methods Enzymol. 101 1983 181 191
    • (1983) Methods Enzymol. , vol.101 , pp. 181-191
    • Guarente, L.1
  • 37
    • 0034966733 scopus 로고    scopus 로고
    • The alkane hydroxylase gene of Burkholderia cepacia RR10 is under catabolite repression control
    • M.M. Marin, T.H. Smits, J.B. van Beilen, and F. Rojo The alkane hydroxylase gene of Burkholderia cepacia RR10 is under catabolite repression control J. Bacteriol. 183 2001 4202 4209
    • (2001) J. Bacteriol. , vol.183 , pp. 4202-4209
    • Marin, M.M.1    Smits, T.H.2    Van Beilen, J.B.3    Rojo, F.4
  • 38
    • 6044239434 scopus 로고    scopus 로고
    • TouR-mediated effector-independent growth phase-dependent activation of the sigma54 Ptou promoter of Pseudomonas stutzeri OX1
    • D. Solera, F.L. Arenghi, T. Woelk, E. Galli, and P. Barbieri TouR-mediated effector-independent growth phase-dependent activation of the sigma54 Ptou promoter of Pseudomonas stutzeri OX1 J. Bacteriol. 186 2004 7353 7363
    • (2004) J. Bacteriol. , vol.186 , pp. 7353-7363
    • Solera, D.1    Arenghi, F.L.2    Woelk, T.3    Galli, E.4    Barbieri, P.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.