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Volumn 88, Issue 1, 1999, Pages 7-11

Gene cloning and characterization of aldehyde dehydrogenase from a petroleum-degrading bacterium, strain HD-1

Author keywords

Aldehyde dehydrogenase; Gene cloning; Kinetics; Petroleum degrading bacterium; Substrate specificity

Indexed keywords

ACETALDEHYDE; ALDEHYDE; ALDEHYDE DEHYDROGENASE; DECANOIC ACID DERIVATIVE; HEXANOIC ACID DERIVATIVE; NICOTINAMIDE ADENINE DINUCLEOTIDE; OCTANOIC ACID DERIVATIVE; PETROLEUM; RECOMBINANT ENZYME; TETRAMER;

EID: 0032866859     PISSN: 13891723     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1389-1723(99)80167-4     Document Type: Article
Times cited : (17)

References (41)
  • 1
    • 0027481986 scopus 로고
    • 2 and assimilate aliphatic and aromatic hydrocarbons anaerobically
    • 2 and assimilate aliphatic and aromatic hydrocarbons anaerobically. J. Ferment. Bioeng., 76, 280-283 (1993).
    • (1993) J. Ferment. Bioeng. , vol.76 , pp. 280-283
    • Morikawa, M.1    Imanaka, T.2
  • 2
    • 0029969093 scopus 로고    scopus 로고
    • Biological oxidation of alkane to alkene under anaerobic conditions
    • 2. Morikawa, M., Kanemoto, M., and Imanaka, T.: Biological oxidation of alkane to alkene under anaerobic conditions. J. Ferment. Bioeng., 82, 309-311 (1996).
    • (1996) J. Ferment. Bioeng. , vol.82 , pp. 309-311
    • Morikawa, M.1    Kanemoto, M.2    Imanaka, T.3
  • 3
    • 0009688593 scopus 로고
    • Diterminal oxidation of long-chain alkanes by bacteria
    • 3. Kester, A. S. and Foster, J. W.: Diterminal oxidation of long-chain alkanes by bacteria. J. Bacteriol., 85, 859-869 (1962).
    • (1962) J. Bacteriol. , vol.85 , pp. 859-869
    • Kester, A.S.1    Foster, J.W.2
  • 4
    • 0028672044 scopus 로고
    • Genetics of alkane oxidation by Pseudomonas oleovolans
    • 4. van Beilen, J. B., Wubbolts, M. G., and Witholt, B.: Genetics of alkane oxidation by Pseudomonas oleovolans. Biodegradation, 5, 161-174 (1994).
    • (1994) Biodegradation , vol.5 , pp. 161-174
    • Van Beilen, J.B.1    Wubbolts, M.G.2    Witholt, B.3
  • 5
    • 0024556880 scopus 로고
    • The Pseudomonas oleovorans alkBAC operon encodes two structurally related rubredoxins and an aldehyde dehydrogenase
    • 5. Kok, M., Oldenhuis, R., van der Linden, M. P. G., Meulenberg, C. H. C., Kingma, J., and Witholt, B.: The Pseudomonas oleovorans alkBAC operon encodes two structurally related rubredoxins and an aldehyde dehydrogenase. J. Biol. Chem., 264, 5442-5451 (1989).
    • (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
  • 6
    • 0025273823 scopus 로고
    • Enzymatic oxidation of xenobiotic chemicals
    • 6. Guengerich, F. P.: Enzymatic oxidation of xenobiotic chemicals. Crit. Rev. Biochem. Mol. Biol., 25, 97-153 (1990).
    • (1990) Crit. Rev. Biochem. Mol. Biol. , vol.25 , pp. 97-153
    • Guengerich, F.P.1
  • 7
    • 0023104891 scopus 로고
    • Involvement of a quinoprotein alcohol dehydrogenase and an NAD-dependent aldehyde dehydrogenase in 2-chloroethanol metabolism in Xanthobacter autotrophicus GJ10
    • 7. Janssen, D. B., Keuning, S., and Witholt, B.: Involvement of a quinoprotein alcohol dehydrogenase and an NAD-dependent aldehyde dehydrogenase in 2-chloroethanol metabolism in Xanthobacter autotrophicus GJ10. J. Gen. Microbiol., 133, 85-92 (1987).
    • (1987) J. Gen. Microbiol. , vol.133 , pp. 85-92
    • Janssen, D.B.1    Keuning, S.2    Witholt, B.3
  • 8
    • 0032545706 scopus 로고    scopus 로고
    • Cloning, sequence and expression of a linear plasmid-based and a chromosomal homolog of chloroacetaldehyde dehydrogenase-encoding genes in Xanthobacter autotrophicus GJ10
    • 8. Bergeron, H., Labbe, D., Turmel, C., and Lau, P. C. K.: Cloning, sequence and expression of a linear plasmid-based and a chromosomal homolog of chloroacetaldehyde dehydrogenase-encoding genes in Xanthobacter autotrophicus GJ10. Gene, 207, 9-18 (1998).
    • (1998) Gene , vol.207 , pp. 9-18
    • Bergeron, H.1    Labbe, D.2    Turmel, C.3    Lau, P.C.K.4
  • 9
    • 0028950304 scopus 로고
    • Degradation of the thiocarbamate herbicide EPTC (S-ethyl dipropyl-carbamothioate) and biosafening by Rhodococcus sp. strain NI86/21 involve an inducible cytochrome P-450 system and aldehyde dehydrogenase
    • 9. Nagy, I., Schoofs, G., Compernolle, F., Proost, P., Vanderleyden, J., and de Mot, R.: Degradation of the thiocarbamate herbicide EPTC (S-ethyl dipropyl-carbamothioate) and biosafening by Rhodococcus sp. strain NI86/21 involve an inducible cytochrome P-450 system and aldehyde dehydrogenase. J. Bacteriol., 177, 676-687 (1995).
    • (1995) J. Bacteriol. , vol.177 , pp. 676-687
    • Nagy, I.1    Schoofs, G.2    Compernolle, F.3    Proost, P.4    Vanderleyden, J.5    De Mot, R.6
  • 10
    • 0019838194 scopus 로고
    • Cloning of the genes for penicillinase, penP and penI, of Bacillus licheniformis in some vector plasmids and their expression in Escherichia coli, Bacillus subtilis, and Bacillus licheniformis
    • 10. Imanaka, T., Tanaka, T., Tsunekawa, H., and Aiba, S.: Cloning of the genes for penicillinase, penP and penI, of Bacillus licheniformis in some vector plasmids and their expression in Escherichia coli, Bacillus subtilis, and Bacillus licheniformis. J. Bacteriol., 147, 776-786 (1981).
    • (1981) J. Bacteriol. , vol.147 , pp. 776-786
    • Imanaka, T.1    Tanaka, T.2    Tsunekawa, H.3    Aiba, S.4
  • 11
    • 0029010741 scopus 로고
    • AldB, an RpoS-dependent gene in Escherichia coli encoding an aldehyde dehydrogenase that is repressed by Fis and activated by Crp
    • 11. Xu, J. and Johnson, R. C.: aldB, an RpoS-dependent gene in Escherichia coli encoding an aldehyde dehydrogenase that is repressed by Fis and activated by Crp. J. Bacteriol., 177, 3166-3175 (1995).
    • (1995) J. Bacteriol. , vol.177 , pp. 3166-3175
    • Xu, J.1    Johnson, R.C.2
  • 12
  • 13
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • 13. Laemmli, U. K.: Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227, 680-685 (1970).
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 14
    • 0002453859 scopus 로고
    • Yeast aldehyde dehydrogenase
    • 14. Black, S.: Yeast aldehyde dehydrogenase. Arch. Biochem. Biophys., 34, 86-97 (1951).
    • (1951) Arch. Biochem. Biophys. , vol.34 , pp. 86-97
    • Black, S.1
  • 15
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • 15. Bradford, M. M.: A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem., 72, 248-254 (1976).
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 16
    • 0026508776 scopus 로고
    • Identification and molecular characterization of the gene coding for acetaldehyde dehydrogenase II (acoD) of Alcaligenes eutrophus
    • 16. Priefert, H., Kruger, N., Jendrossek, D., Schmidt, B., and Steinbuchel, A.: Identification and molecular characterization of the gene coding for acetaldehyde dehydrogenase II (acoD) of Alcaligenes eutrophus. J. Bacteriol., 174, 899-907 (1992).
    • (1992) J. Bacteriol. , vol.174 , pp. 899-907
    • Priefert, H.1    Kruger, N.2    Jendrossek, D.3    Schmidt, B.4    Steinbuchel, A.5
  • 17
    • 0025774602 scopus 로고
    • Expression of the Vivrio cholerae toxin transcriptional activator
    • 17. Parsot, C. and Mekalanos, J. J.: Expression of the Vivrio cholerae toxin transcriptional activator. J. Bacteriol., 173, 2842-2851 (1991).
    • (1991) J. Bacteriol. , vol.173 , pp. 2842-2851
    • Parsot, C.1    Mekalanos, J.J.2
  • 18
    • 0024544044 scopus 로고
    • Primary structures of rat and bovine liver mitochondrial aldehyde dehydrogenases deduced from cDNA sequences
    • 18. Ferres, J., Guan, K. L., and Weiner, H.: Primary structures of rat and bovine liver mitochondrial aldehyde dehydrogenases deduced from cDNA sequences. Eur. J. Biochem., 180, 67-74 (1989).
    • (1989) Eur. J. Biochem. , vol.180 , pp. 67-74
    • Ferres, J.1    Guan, K.L.2    Weiner, H.3
  • 20
    • 0022404998 scopus 로고
    • Characterization of the coenzyme binding site of liver aldehyde dehydrogenase: Differential reactivity of coenzyme analogues
    • 20. Von Bahr-Lindstrom, H., Jeck, R., Woenckhaus, C., Sohn, S., Hempel, J., and Jornvall, H.: Characterization of the coenzyme binding site of liver aldehyde dehydrogenase: differential reactivity of coenzyme analogues. Biochemistry, 24, 5847-5851 (1985).
    • (1985) Biochemistry , vol.24 , pp. 5847-5851
    • Von Bahr-Lindstrom, H.1    Jeck, R.2    Woenckhaus, C.3    Sohn, S.4    Hempel, J.5    Jornvall, H.6
  • 21
    • 0021182752 scopus 로고
    • Human liver mitochondrial aldehyde dehydrogenase: A C-terminal segment positions and defines the structure corresponding to the one reported to differ in the Oriental enzyme variant
    • 21. Hempel, J., Kaiser, R., and Jornvall, H.: Human liver mitochondrial aldehyde dehydrogenase: a C-terminal segment positions and defines the structure corresponding to the one reported to differ in the Oriental enzyme variant. FEBS Lett., 173, 367-373 (1984).
    • (1984) FEBS Lett. , vol.173 , pp. 367-373
    • Hempel, J.1    Kaiser, R.2    Jornvall, H.3
  • 22
    • 0021864787 scopus 로고
    • Expression of glnA in Escherichia coli is regulated at tandem promoters
    • 22. Reitzer, L. J. and Magasanik, B.: Expression of glnA in Escherichia coli is regulated at tandem promoters. Proc. Natl. Acad. Sci. USA, 82, 1979-1983 (1985).
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 1979-1983
    • Reitzer, L.J.1    Magasanik, B.2
  • 23
    • 0026719281 scopus 로고
    • Identification of AcoR, a regulatory gene for the expression of genes essential for acetoin catabolism in Alcaligenes eutrophus H16
    • 23. Kruger, N. and Sterinbuchel, A.: Identification of AcoR, a regulatory gene for the expression of genes essential for acetoin catabolism in Alcaligenes eutrophus H16. J. Bacteriol., 174, 4391-4400 (1992).
    • (1992) J. Bacteriol. , vol.174 , pp. 4391-4400
    • Kruger, N.1    Sterinbuchel, A.2
  • 24
    • 0022545682 scopus 로고
    • Upstream activator sequences are present in the promoters of nitrogen fixation genes
    • 24. Buck, M., Miller, S., Drummond, M., and Dixon, R.: Upstream activator sequences are present in the promoters of nitrogen fixation genes. Nature, 320, 374-378 (1986).
    • (1986) Nature , vol.320 , pp. 374-378
    • Buck, M.1    Miller, S.2    Drummond, M.3    Dixon, R.4
  • 26
    • 0023812828 scopus 로고
    • Role of uhp genes in expression of the Escherichia coli sugar-phosphate transport system
    • 26. Weston, L. A. and Kandner, R. J.: Role of uhp genes in expression of the Escherichia coli sugar-phosphate transport system. J. Bacteriol., 170, 3375-3383 (1988).
    • (1988) J. Bacteriol. , vol.170 , pp. 3375-3383
    • Weston, L.A.1    Kandner, R.J.2
  • 27
    • 0023898663 scopus 로고
    • Purification and properties of the inducible coenzyme A-linked butyraldehyde dehydrogenase from Clostridium acetobutylicum
    • 27. Palosaari, N. R. and Rogers, P.: Purification and properties of the inducible coenzyme A-linked butyraldehyde dehydrogenase from Clostridium acetobutylicum. J. Bacteriol., 170, 2971-2976 (1988).
    • (1988) J. Bacteriol. , vol.170 , pp. 2971-2976
    • Palosaari, N.R.1    Rogers, P.2
  • 28
    • 0023643181 scopus 로고
    • +-independent aldehyde dehydrogenase from Pseudomonas testosteroni
    • +-independent aldehyde dehydrogenase from Pseudomonas testosteroni. Eur. J. Biochem., 166, 575-579 (1987).
    • (1987) Eur. J. Biochem. , vol.166 , pp. 575-579
    • Poels, P.A.1    Groen, B.W.2    Duine, J.A.3
  • 29
    • 0017878807 scopus 로고
    • An induced aliphatic aldehyde dehydrogenase from the bioluminescent bacterium, Beneckea harveri
    • 29. Bognar, A. L. and Meighen, E. A.: An induced aliphatic aldehyde dehydrogenase from the bioluminescent bacterium, Beneckea harveri. J. Biol. Chem., 25, 446-450 (1978).
    • (1978) J. Biol. Chem. , vol.25 , pp. 446-450
    • Bognar, A.L.1    Meighen, E.A.2
  • 30
    • 0025367654 scopus 로고
    • Purification and characterization of osmoregulatory betaine aldehyde dehydrogenase of Escherichia coli
    • 30. Falkenberg, P. and Stom, A. R.: Purification and characterization of osmoregulatory betaine aldehyde dehydrogenase of Escherichia coli. Biochim. Biophys. Acta, 1034, 253-259 (1990).
    • (1990) Biochim. Biophys. Acta , vol.1034 , pp. 253-259
    • Falkenberg, P.1    Stom, A.R.2
  • 31
    • 0023656153 scopus 로고
    • Three different proteins exhibiting NAD-dependent acetaldehyde dehydrogenase activity from Alcaligenes eutrophus
    • 31. Jendrossek, D., Steinbüchel, A., and Schlegel, H. G.: Three different proteins exhibiting NAD-dependent acetaldehyde dehydrogenase activity from Alcaligenes eutrophus. Eur. J. Biochem., 167, 541-548 (1987).
    • (1987) Eur. J. Biochem. , vol.167 , pp. 541-548
    • Jendrossek, D.1    Steinbüchel, A.2    Schlegel, H.G.3
  • 32
    • 0023656597 scopus 로고
    • Involvement of lactaldehyde dehydrogenase in several metabolic pathways of Escherichia coli K12
    • 32. Baldoma, L. and Aguilar, J.: Involvement of lactaldehyde dehydrogenase in several metabolic pathways of Escherichia coli K12. J. Biol. Chem., 262, 13991-13996 (1987).
    • (1987) J. Biol. Chem. , vol.262 , pp. 13991-13996
    • Baldoma, L.1    Aguilar, J.2
  • 33
    • 0019871847 scopus 로고
    • Ordered conformation of polypeptides and proteins in acidic dodecyl sulfate solution
    • 33. Wu, C. S. C., Ikeda, K., and Yang, J. T.: Ordered conformation of polypeptides and proteins in acidic dodecyl sulfate solution. Biochemistry, 20, 566-570 (1981).
    • (1981) Biochemistry , vol.20 , pp. 566-570
    • Wu, C.S.C.1    Ikeda, K.2    Yang, J.T.3
  • 34
    • 0001236882 scopus 로고
    • Studies on malonic semialdehyde dehydrogenase from Pseudomonas aeruginosa
    • 34. Nakamura, K. and Bernheim, F.: Studies on malonic semialdehyde dehydrogenase from Pseudomonas aeruginosa. Biochim. Biophys. Acta, 50, 147-152 (1961).
    • (1961) Biochim. Biophys. Acta , vol.50 , pp. 147-152
    • Nakamura, K.1    Bernheim, F.2
  • 35
    • 0017166832 scopus 로고
    • Purification and characterization of Betaine Aldehyde Dehydrogenase from Pseudomonas aeruginosa A-16
    • 35. Nagasawa, T., Kawabata, Y., and Tani, Y.: Purification and characterization of Betaine Aldehyde Dehydrogenase from Pseudomonas aeruginosa A-16. Agr. Biol. Chem., 40, 1743-1749 (1976).
    • (1976) Agr. Biol. Chem. , vol.40 , pp. 1743-1749
    • Nagasawa, T.1    Kawabata, Y.2    Tani, Y.3
  • 36
    • 0009723097 scopus 로고
    • Studies on acetic acid bacteria
    • 36. Nakayama, T.: Studies on acetic acid bacteria. J. Biochem., 48, 812-830 (1960).
    • (1960) J. Biochem. , vol.48 , pp. 812-830
    • Nakayama, T.1
  • 37
    • 0014429124 scopus 로고
    • Yeast aldehyde dehydrogenase. II. Properties of the homogeneous enzyme preparations
    • 37. Steinman, C. R. and Jakoby, W.: Yeast aldehyde dehydrogenase. II. Properties of the homogeneous enzyme preparations. J. Biol. Chem., 243, 730-734 (1968).
    • (1968) J. Biol. Chem. , vol.243 , pp. 730-734
    • Steinman, C.R.1    Jakoby, W.2
  • 39
    • 0020435686 scopus 로고
    • Aldehyde dehydrogenase from Pseudomonas aeruginosa
    • 39. Vandecasteele, J. P. and Guerrillot, L.: Aldehyde dehydrogenase from Pseudomonas aeruginosa. Methods Enzymol., 89, 484-490 (1982).
    • (1982) Methods Enzymol. , vol.89 , pp. 484-490
    • Vandecasteele, J.P.1    Guerrillot, L.2
  • 40
    • 0023656153 scopus 로고
    • Three different proteins exhibiting NAD-dependent acetaldehyde dehydrogenase activity from Alcaligenes eutrophus
    • 40. Jendrossek, D., Steinbuchel, A., and Schlegel, H. G.: Three different proteins exhibiting NAD-dependent acetaldehyde dehydrogenase activity from Alcaligenes eutrophus. Eur. J. Biochem., 167, 541-548 (1987).
    • (1987) Eur. J. Biochem. , vol.167 , pp. 541-548
    • Jendrossek, D.1    Steinbuchel, A.2    Schlegel, H.G.3
  • 41
    • 0021185917 scopus 로고
    • Vivrio harveyi aldehyde dehydrogenase
    • 41. Byers, D. and Meighen, E.: Vivrio harveyi aldehyde dehydrogenase. J. Biol. Chem., 259, 7109-7114 (1984).
    • (1984) J. Biol. Chem. , vol.259 , pp. 7109-7114
    • Byers, D.1    Meighen, E.2


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