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Volumn 67, Issue 10, 2001, Pages 4817-4827

Cloning and Genetic Characterization of dca Genes Required for β-Oxidation of Straight-Chain Dicarboxylic Acids in Acinetobacter sp. Strain ADP1

Author keywords

[No Author keywords available]

Indexed keywords

ADIPIC ACID; ADIPIC ACID DERIVATIVE; BACTERIAL PROTEIN; DICARBOXYLIC ACID;

EID: 0035490405     PISSN: 00992240     EISSN: None     Source Type: Journal    
DOI: 10.1128/AEM.67.10.4817-4827.2001     Document Type: Article
Times cited : (51)

References (46)
  • 3
    • 0026579902 scopus 로고
    • Genetic analysis of supraoperonic clustering by use of natural transformation in Acinetobacter calcoaceticus
    • Averhoff, B., L. Gregg-Jolly, D. Elsemore, and L. N. Ornston. 1992. Genetic analysis of supraoperonic clustering by use of natural transformation in Acinetobacter calcoaceticus. J. Bacteriol. 174:200-204.
    • (1992) J. Bacteriol. , vol.174 , pp. 200-204
    • Averhoff, B.1    Gregg-Jolly, L.2    Elsemore, D.3    Ornston, L.N.4
  • 4
    • 0014289028 scopus 로고
    • A study of the Moraxella group. II. Oxidative-negative species (genus Acinetobacter)
    • Baumann, P., M. Doudoroff, and R. Y. Stanier. 1968. A study of the Moraxella group. II. Oxidative-negative species (genus Acinetobacter). J. Bacteriol. 95:1520-1541.
    • (1968) J. Bacteriol. , vol.95 , pp. 1520-1541
    • Baumann, P.1    Doudoroff, M.2    Stanier, R.Y.3
  • 5
    • 0031920817 scopus 로고    scopus 로고
    • The macromolecular aromatic domain in suberized tissue: A changing paradigm
    • Bernards, M. A., and N. G. Lewis. 1998. The macromolecular aromatic domain in suberized tissue: a changing paradigm. Phytochemistry 47:915-933.
    • (1998) Phytochemistry , vol.47 , pp. 915-933
    • Bernards, M.A.1    Lewis, N.G.2
  • 6
    • 0017859433 scopus 로고
    • The microbial degradation of cyclohexanecarboxylic acid by a β-oxidation pathway with simultaneous induction to the utilization of benzoate
    • Blakely, E. R. 1978. The microbial degradation of cyclohexanecarboxylic acid by a β-oxidation pathway with simultaneous induction to the utilization of benzoate. Can. J. Microbiol. 24:847-855.
    • (1978) Can. J. Microbiol. , vol.24 , pp. 847-855
    • Blakely, E.R.1
  • 7
    • 0014083959 scopus 로고
    • Regulation of the enzymes of the β-ketoadipate pathway in Moraxella calcoacetica. 1. General aspects
    • Canovas, J. L., and R. Y. Stanier. 1697. Regulation of the enzymes of the β-ketoadipate pathway in Moraxella calcoacetica. 1. General aspects. Eur. J. Biochem. 1:289-300.
    • (1697) Eur. J. Biochem. , vol.1 , pp. 289-300
    • Canovas, J.L.1    Stanier, R.Y.2
  • 8
    • 0014075738 scopus 로고
    • Dicarboxylic acid catabolism by bacteria
    • Chapman, P. J., and R. G. Dugglesby. 1967. Dicarboxylic acid catabolism by bacteria. Biochem. J. 103:7c-9c.
    • (1967) Biochem. J. , vol.103
    • Chapman, P.J.1    Dugglesby, R.G.2
  • 9
    • 0033871150 scopus 로고    scopus 로고
    • Genetic analysis of a gene cluster for cyclonexanol oxidation in Acinetobacter sp. strain SE19 by in vitro transposition
    • Cheng, Q., S. M. Thomas, K. Kostichka, J. R. Valentine, and V. Nagarajan. 2000. Genetic analysis of a gene cluster for cyclonexanol oxidation in Acinetobacter sp. strain SE19 by in vitro transposition. J. Bacteriol. 182:4744-4751.
    • (2000) J. Bacteriol. , vol.182 , pp. 4744-4751
    • Cheng, Q.1    Thomas, S.M.2    Kostichka, K.3    Valentine, J.R.4    Nagarajan, V.5
  • 10
    • 0347850682 scopus 로고    scopus 로고
    • Ph.D. thesis. Yale University, New Haven, Conn.
    • D'Argenio, D. A. 1999. Ph.D. thesis. Yale University, New Haven, Conn.
    • (1999)
    • D'Argenio, D.A.1
  • 11
    • 0035838554 scopus 로고    scopus 로고
    • Spontaneous mutations affecting transcriptional regulation by protocatechuate in Acinetobacter
    • D'Argenio, D. A., A. Segura, P. V. Bünz, and L. N. Ornston. 2001. Spontaneous mutations affecting transcriptional regulation by protocatechuate in Acinetobacter. FEMS Microbiol. Lett. 201:15-19.
    • (2001) FEMS Microbiol. Lett. , vol.201 , pp. 15-19
    • D'Argenio, D.A.1    Segura, A.2    Bünz, P.V.3    Ornston, L.N.4
  • 12
    • 0033000387 scopus 로고    scopus 로고
    • The physiological contribution of Acinetobacter PcaK, a transport system that acts upon protocatechuate, can be masked by the overlapping specificity of VanK
    • D'Argenio, D. A., A. Segura, W. M. Coco, P. V. Bünz, and L. N. Ornston. 1999. The physiological contribution of Acinetobacter PcaK, a transport system that acts upon protocatechuate, can be masked by the overlapping specificity of VanK. J. Bacteriol. 181:3505-3515.
    • (1999) J. Bacteriol. , vol.181 , pp. 3505-3515
    • D'Argenio, D.A.1    Segura, A.2    Coco, W.M.3    Bünz, P.V.4    Ornston, L.N.5
  • 13
    • 0032718514 scopus 로고    scopus 로고
    • Substitution, insertion, deletion, suppression, and altered substrate specificity in functional protocatechuate 3,4-dioxygenases
    • D'Argenio, D. A., M. W. Vetting, D. H. Ohlendorf, and L. N. Ornston. 1999. Substitution, insertion, deletion, suppression, and altered substrate specificity in functional protocatechuate 3,4-dioxygenases. J. Bacteriol. 181:6478-6487.
    • (1999) J. Bacteriol. , vol.181 , pp. 6478-6487
    • D'Argenio, D.A.1    Vetting, M.W.2    Ohlendorf, D.H.3    Ornston, L.N.4
  • 14
    • 0016824525 scopus 로고
    • The metabolism of cyclohexanol by Acinetobacter NCIB 9871
    • Donoghue, N. A., and P. W. Trudgill. 1975. The metabolism of cyclohexanol by Acinetobacter NCIB 9871. Eur. J. Biochem. 60:1-7.
    • (1975) Eur. J. Biochem. , vol.60 , pp. 1-7
    • Donoghue, N.A.1    Trudgill, P.W.2
  • 15
    • 0031985785 scopus 로고    scopus 로고
    • Structure of the sucrose-specific porin ScrY from Salmonella typhimurium and its complex with sucrose
    • Forst, D., W. Weite, T. Wacker, and K. Diederichs. 1997. Structure of the sucrose-specific porin ScrY from Salmonella typhimurium and its complex with sucrose. Nat. Struct. Biol. 5:37-46.
    • (1997) Nat. Struct. Biol. , vol.5 , pp. 37-46
    • Forst, D.1    Weite, W.2    Wacker, T.3    Diederichs, K.4
  • 16
    • 0028255967 scopus 로고
    • Anaerobic degradation of pimelate by newly isolated denitrifying bacteria
    • Gallus, C., and B. Schink. 1994. Anaerobic degradation of pimelate by newly isolated denitrifying bacteria. Microbiology 140:404-416.
    • (1994) Microbiology , vol.140 , pp. 404-416
    • Gallus, C.1    Schink, B.2
  • 17
    • 0029885370 scopus 로고    scopus 로고
    • IS1236, a newly discovered member of the IS3 family, exhibits varied patterns of insertion into the Acinetobacter calcoaceticus chromosome
    • Gerischer, U., D. A. D'Argenio, and L. N. Ornston. 1996. IS1236, a newly discovered member of the IS3 family, exhibits varied patterns of insertion into the Acinetobacter calcoaceticus chromosome. Microbiology 142:1825-1831.
    • (1996) Microbiology , vol.142 , pp. 1825-1831
    • Gerischer, U.1    D'Argenio, D.A.2    Ornston, L.N.3
  • 18
    • 0028915920 scopus 로고
    • Spontaneous mutations pcaH and -G, structural genes for protocatechuate 3,4-dioxygenase in Acinetobacter calcoaceticus
    • Gerischer, U., and L. N. Ornston. 1995. Spontaneous mutations pcaH and -G, structural genes for protocatechuate 3,4-dioxygenase in Acinetobacter calcoaceticus. J. Bacteriol. 177:1336-1347.
    • (1995) J. Bacteriol. , vol.177 , pp. 1336-1347
    • Gerischer, U.1    Ornston, L.N.2
  • 19
    • 0033662088 scopus 로고    scopus 로고
    • Suberin structure in potato periderm: Glycerol, long-chain monomers, and glyceryl and feruloyl dimers
    • Graca, J., and H. Pereira. 2000. Suberin structure in potato periderm: glycerol, long-chain monomers, and glyceryl and feruloyl dimers. Agric. Food Chem. 48:5476-5483.
    • (2000) Agric. Food Chem. , vol.48 , pp. 5476-5483
    • Graca, J.1    Pereira, H.2
  • 20
    • 0027400782 scopus 로고
    • Purification of glutaryl-CoA dehydrogenase from Pseudomonas sp., an enzyme involved in the anaerobic degradation of benzoate
    • Härtel, U., E. Eckel, J. Koch, G. Fuchs, D. Linder, and W. Buckel. 1993. Purification of glutaryl-CoA dehydrogenase from Pseudomonas sp., an enzyme involved in the anaerobic degradation of benzoate. Arch. Microbiol. 159:174-181.
    • (1993) Arch. Microbiol. , vol.159 , pp. 174-181
    • Härtel, U.1    Eckel, E.2    Koch, J.3    Fuchs, G.4    Linder, D.5    Buckel, W.6
  • 21
    • 0025148587 scopus 로고
    • Selection of Acinetobacter calcoaceticus mutants deficient in the p-hydroxybenzoate hydroxylase gene (poba ) a member of a supraoperonic elusler
    • Hartnett, G.,B. Averhoff, and L. N. Ornston. 1990. Selection of Acinetobacter calcoaceticus mutants deficient in the p-hydroxybenzoate hydroxylase gene (pobA ) a member of a supraoperonic elusler. J. Bacteriol. 172:6160-6161.
    • (1990) J. Bacteriol. , vol.172 , pp. 6160-6161
    • Hartnett, G.1    Averhoff, B.2    Ornston, L.N.3
  • 22
    • 0031024667 scopus 로고    scopus 로고
    • Shedding light on anaerobic benzene ring degradation: A process unique to prokaryotes?
    • Harwood, C. S., and J. Gibson. 1997. Shedding light on anaerobic benzene ring degradation: a process unique to prokaryotes? J. Baeteriol. 179:301-309.
    • (1997) J. Baeteriol. , vol.179 , pp. 301-309
    • Harwood, C.S.1    Gibson, J.2
  • 23
    • 0014753329 scopus 로고
    • The dissimilation of higher dicarboxylic acids by Pseudomonas fluorescens
    • Hoet, P. P., and R. Y. Stanier. 1970. The dissimilation of higher dicarboxylic acids by Pseudomonas fluorescens. Eur. J. Biochem. 13:65-70.
    • (1970) Eur. J. Biochem. , vol.13 , pp. 65-70
    • Hoet, P.P.1    Stanier, R.Y.2
  • 24
    • 0014753578 scopus 로고
    • Existence and functions of two enzymes with β-ketoadipate:succinyl-CoA transferase activity in Pseudomonas fluorescens
    • Hoet, P. P., and R. Y. Stanier. 1970. Existence and functions of two enzymes with β-ketoadipate:succinyl-CoA transferase activity in Pseudomonas fluorescens. Eur. J. Biochem. 13:71-76.
    • (1970) Eur. J. Biochem. , vol.13 , pp. 71-76
    • Hoet, P.P.1    Stanier, R.Y.2
  • 26
    • 0025675856 scopus 로고
    • High efficiency transformation of Escherichia coli with plasmids
    • Inoue, H., H. Nojima, and H. Okayama. 1990. High efficiency transformation of Escherichia coli with plasmids. Gene 96:23-28.
    • (1990) Gene , vol.96 , pp. 23-28
    • Inoue, H.1    Nojima, H.2    Okayama, H.3
  • 27
    • 0015425823 scopus 로고
    • Interspecies transformation of Acinetobacter, genetic evidence for a ubiquitous genus
    • Juni, E. 1972. Interspecies transformation of Acinetobacter, genetic evidence for a ubiquitous genus. J. Bacteriol. 112:417-431.
    • (1972) J. Bacteriol. , vol.112 , pp. 417-431
    • Juni, E.1
  • 28
    • 0014503154 scopus 로고
    • Transformation of Acinetobacter calco-aceticus (Bacterium anitratum)
    • Juni, E., and A. Janick. 1969. Transformation of Acinetobacter calco-aceticus (Bacterium anitratum). J. Bacteriol. 98:281-288.
    • (1969) J. Bacteriol. , vol.98 , pp. 281-288
    • Juni, E.1    Janick, A.2
  • 29
    • 0009688593 scopus 로고
    • Diterminal oxidation of long-chain alkanes by bacteria
    • Kester, A. S., and J. W. Foster. 1963. Diterminal oxidation of long-chain alkanes by bacteria. J. Bacteriol. 85:859-869.
    • (1963) J. Bacteriol. , vol.85 , pp. 859-869
    • Kester, A.S.1    Foster, J.W.2
  • 31
    • 0006665591 scopus 로고
    • Enzymatic ω-oxidation of fatty acids. I. Products of octanoate, decanoate, and laurate oxidation
    • Kusunose, M., E. Kusunose, and M. J. Coon. 1964. Enzymatic ω-oxidation of fatty acids. I. Products of octanoate, decanoate, and laurate oxidation. J. Biol. Chem. 239:1374-1380.
    • (1964) J. Biol. Chem. , vol.239 , pp. 1374-1380
    • Kusunose, M.1    Kusunose, E.2    Coon, M.J.3
  • 32
    • 0032770496 scopus 로고    scopus 로고
    • Glycerol is a suberin monomer. New experimental evidence for an old hypothesis
    • Moire, L., A. Schmutz, A. Buchala, B. Van, R. E. Stark, and U. Ryser. 1999. Glycerol is a suberin monomer. New experimental evidence for an old hypothesis. Plant Physiol. 119:1137-1146.
    • (1999) Plant Physiol. , vol.119 , pp. 1137-1146
    • Moire, L.1    Schmutz, A.2    Buchala, A.3    Van, B.4    Stark, R.E.5    Ryser, U.6
  • 33
    • 0030614959 scopus 로고    scopus 로고
    • Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites
    • Nielsen, H., J. Engelbrecht, S. Brunak, and G. von Heijne. 1997. Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites. Protein Eng. 10:1-6.
    • (1997) Protein Eng. , vol.10 , pp. 1-6
    • Nielsen, H.1    Engelbrecht, J.2    Brunak, S.3    Von Heijne, G.4
  • 35
    • 0033987616 scopus 로고    scopus 로고
    • Bacteria are not what they eat: That is why they are so diverse
    • Parke, D., D. A. D'Argenio, and L. N. Ornston. 2000. Bacteria are not what they eat: that is why they are so diverse. J. Bacteriol. 182:257-263.
    • (2000) J. Bacteriol. , vol.182 , pp. 257-263
    • Parke, D.1    D'Argenio, D.A.2    Ornston, L.N.3
  • 36
    • 0021133441 scopus 로고
    • Nutritional diversity of Rhizobiaceae revealed by auxanography
    • Parke, D., and L. N. Ornston. 1984. Nutritional diversity of Rhizobiaceae revealed by auxanography. J. Gen. Microbiol. 130:1743-1750.
    • (1984) J. Gen. Microbiol. , vol.130 , pp. 1743-1750
    • Parke, D.1    Ornston, L.N.2
  • 37
    • 0017895678 scopus 로고
    • Physiological study and taxonomy of Alcaligenes species: A. denitrificans, A. odorans and A. faecalis
    • Pichinoly, F., M. Veron, M. Mandel, M. Durand, C. Job, and J. L. Garcia. 1978. Physiological study and taxonomy of Alcaligenes species: A. denitrificans, A. odorans and A. faecalis. Can. J. Microbiol. 24:743-753.
    • (1978) Can. J. Microbiol. , vol.24 , pp. 743-753
    • Pichinoly, F.1    Veron, M.2    Mandel, M.3    Durand, M.4    Job, C.5    Garcia, J.L.6
  • 38
    • 0002043965 scopus 로고    scopus 로고
    • Rearrangements of the bacterial chromosome: Formation and applications
    • F. C. Neidhart, R. Curtiss III, J. L. Ingraham, H. C. C. Lin, K. B. Low, B. Magasanik, W. S. Reznikoff, M. Riley, M. Schaechter, and H. E. Umbarger (ed.), American Society for Microbiology, Washington, D. C.
    • Roth, J. R., N. Benson, T. Galitski, K. Haack, J. G. Lawrence, and L. Miesel. 1996. Rearrangements of the bacterial chromosome: formation and applications, p. 2256-2276. In F. C. Neidhart, R. Curtiss III, J. L. Ingraham, H. C. C. Lin, K. B. Low, B. Magasanik, W. S. Reznikoff, M. Riley, M. Schaechter, and H. E. Umbarger (ed.), Escherichia coli and Salmonella: cellular and molecular biology. American Society for Microbiology, Washington, D. C.
    • (1996) Escherichia Coli and Salmonella: Cellular and Molecular Biology , pp. 2256-2276
    • Roth, J.R.1    Benson, N.2    Galitski, T.3    Haack, K.4    Lawrence, J.G.5    Miesel, L.6
  • 40
    • 0028946962 scopus 로고
    • Structural basis for sugar translocation through maltoporin channels at 3.1 a resolution
    • Schirmer, T., T. A. Keller, Y. Wang, and J. P. Rosenbusch. 1995. Structural basis for sugar translocation through maltoporin channels at 3.1 A resolution. Science 267:512-514.
    • (1995) Science , vol.267 , pp. 512-514
    • Schirmer, T.1    Keller, T.A.2    Wang, Y.3    Rosenbusch, J.P.4
  • 44
    • 0030930296 scopus 로고    scopus 로고
    • mucK a gene in Acinetobacter calcoaceticus ADP1 (BD413), encodes the ability to grow on exogenous cis,cis-muconate as the sole carbon source
    • Williams, P. A., and L. E. Shaw. 1997. mucK a gene in Acinetobacter calcoaceticus ADP1 (BD413), encodes the ability to grow on exogenous cis,cis-muconate as the sole carbon source. J. Bacteriol. 179:5935-5942.
    • (1997) J. Bacteriol. , vol.179 , pp. 5935-5942
    • Williams, P.A.1    Shaw, L.E.2
  • 45
    • 0023184331 scopus 로고
    • Bacterial evolution
    • Woese, C. R. 1987. Bacterial evolution. Microbiol. Rev. 51:221-271.
    • (1987) Microbiol. Rev. , vol.51 , pp. 221-271
    • Woese, C.R.1
  • 46
    • 0021943518 scopus 로고
    • Improved M13 phage cloning vectors and host strains: Nucleotide sequences of the M13mp18 and pUC19 vectors
    • Yaniseh-Perron, C., J. Vieira, and J. Messing. 1985. Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mp18 and pUC19 vectors. Gene 33:103-119.
    • (1985) Gene , vol.33 , pp. 103-119
    • Yaniseh-Perron, C.1    Vieira, J.2    Messing, J.3


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