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Volumn 165, Issue 4, 1996, Pages 258-264

Adaptation of Pseudomonas sp. GJ1 to 2-bromoethanol caused by overexpression of an NAD-dependent aldehyde dehydrogenase with low affinity for halogenated aldehydes

Author keywords

1,2 Dibromoethane; 2 Bromoethanol; 2 Chloroethanol; Aldehyde dehydrogenase; Biodegradation; Dehalogenase; Genetic adaptation

Indexed keywords

1,2 DIBROMOETHANE; 2 BROMOACETALDEHYDE; 2 BROMOETHANOL; 2 CHLOROETHANOL; ALDEHYDE DEHYDROGENASE; DEHALOGENASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE; UNCLASSIFIED DRUG;

EID: 0029991614     PISSN: 03028933     EISSN: None     Source Type: Journal    
DOI: 10.1007/s002030050324     Document Type: Article
Times cited : (8)

References (21)
  • 1
    • 0018642315 scopus 로고
    • Interaction of potential metabolites of the carcinogen ethylene dibromide with protein and DNA in vitro
    • Banerjee S, Van Duuren BL, Kline SS (19791 Interaction of potential metabolites of the carcinogen ethylene dibromide with protein and DNA in vitro. Biochem Biophys Res Commun 90: 1214-1220
    • (1979) Biochem Biophys Res Commun , vol.90 , pp. 1214-1220
    • Banerjee, S.1    Van Duuren, B.L.2    Kline, S.S.3
  • 2
    • 0026539553 scopus 로고
    • Aldehyde dehydrogenase. Covalent intermediate in aldehyde dehydrogenation and ester hydrolysis
    • Blatter EE, Abriota DP, Pietruszko R (1992) Aldehyde dehydrogenase. Covalent intermediate in aldehyde dehydrogenation and ester hydrolysis. Biochem J 282:353-360
    • (1992) Biochem J , vol.282 , pp. 353-360
    • Blatter, E.E.1    Abriota, D.P.2    Pietruszko, R.3
  • 3
    • 0020440016 scopus 로고
    • Isozymes of aldehyde dehydrogenase from horse liver
    • Eckfeldt JH, Yonetani T (1982) Isozymes of aldehyde dehydrogenase from horse liver. Methods Enzymol 89:474-479
    • (1982) Methods Enzymol , vol.89 , pp. 474-479
    • Eckfeldt, J.H.1    Yonetani, T.2
  • 4
    • 0020488533 scopus 로고
    • Identification of a segment containing a reactive cysteine residue in human liver cytoplasmic aldehyde dehydrogenase (isoenzyme E)
    • Hempel J, Pietruszko R, Fietzek P, Jornvall H (1982) Identification of a segment containing a reactive cysteine residue in human liver cytoplasmic aldehyde dehydrogenase (isoenzyme E). Biochemistry 21:6834-6838
    • (1982) Biochemistry , vol.21 , pp. 6834-6838
    • Hempel, J.1    Pietruszko, R.2    Fietzek, P.3    Jornvall, H.4
  • 5
    • 0001310399 scopus 로고
    • Biodegradation of 2-chloroethanol and 1,2-dichloroethane by pure bacterial cultures
    • Janssen DB, Scheper A, Witholt B (1984) Biodegradation of 2-chloroethanol and 1,2-dichloroethane by pure bacterial cultures. Prog Ind Microbiol 20: 169-178
    • (1984) Prog Ind Microbiol , vol.20 , pp. 169-178
    • Janssen, D.B.1    Scheper, A.2    Witholt, B.3
  • 6
    • 0021966251 scopus 로고
    • Degradation of halogenated aliphatic compounds by Xanthobacter autotrophicus GJ10
    • Janssen DB, Scheper A, Dijkhuizen L, Witholt B (1985) Degradation of halogenated aliphatic compounds by Xanthobacter autotrophicus GJ10. Appl Environ Microbiol 49:673-677
    • (1985) Appl Environ Microbiol , vol.49 , pp. 673-677
    • Janssen, D.B.1    Scheper, A.2    Dijkhuizen, L.3    Witholt, B.4
  • 7
    • 1542574275 scopus 로고
    • Degradation of n-alkanes and α,ω-dihaloalkanes by wild-type and mutants of Acinetobacter sp. strain GJ70
    • Janssen DB, Jager D, Witholt B (1987) Degradation of n-alkanes and α,ω-dihaloalkanes by wild-type and mutants of Acinetobacter sp. strain GJ70. Appl Environ Microbiol 133:85-92
    • (1987) Appl Environ Microbiol , vol.133 , pp. 85-92
    • Janssen, D.B.1    Jager, D.2    Witholt, B.3
  • 8
    • 0023656153 scopus 로고
    • Three different proteins exhibiting NAD-dependent acetaldehyde dehydrogenase activities from Alcaligenes eutrophus
    • Jendrossek D, Steinbüchel A, Schlegel HG (1988) Three different proteins exhibiting NAD-dependent acetaldehyde dehydrogenase activities from Alcaligenes eutrophus. Eur J Biochem 167:541-548
    • (1988) Eur J Biochem , vol.167 , pp. 541-548
    • Jendrossek, D.1    Steinbüchel, A.2    Schlegel, H.G.3
  • 9
    • 0021798672 scopus 로고
    • Purification and characterization of hydrolytic haloalkane dehalogenase from Xanthobacter autotrophicus GJ10
    • Keuning S, Janssen DB, Witholt B (1985) Purification and characterization of hydrolytic haloalkane dehalogenase from Xanthobacter autotrophicus GJ10. J Bacteriol 163:635-639
    • (1985) J Bacteriol , vol.163 , pp. 635-639
    • Keuning, S.1    Janssen, D.B.2    Witholt, B.3
  • 10
    • 0017726418 scopus 로고
    • Pre-steady state kinetic studies on cytoplasmic sheep liver aldehyde dehydrogenase
    • MacGibbon AKH, Blackwell LF, Buckly PD (1977) Pre-steady state kinetic studies on cytoplasmic sheep liver aldehyde dehydrogenase. Biochem J 167:469-477
    • (1977) Biochem J , vol.167 , pp. 469-477
    • MacGibbon, A.K.H.1    Blackwell, L.F.2    Buckly, P.D.3
  • 11
    • 0023651262 scopus 로고
    • Reaction conditions affect the specificity of bromoacetaldehyde as a probe for DNA cruciforms and B-Z junctions
    • McLean MJ, Larson JE, Wohlrab F, Wells RD (1987) Reaction conditions affect the specificity of bromoacetaldehyde as a probe for DNA cruciforms and B-Z junctions. Nucleic Acids Res 15:6917-6935
    • (1987) Nucleic Acids Res , vol.15 , pp. 6917-6935
    • McLean, M.J.1    Larson, J.E.2    Wohlrab, F.3    Wells, R.D.4
  • 12
    • 0025774602 scopus 로고
    • Expression of the Vibrio cholerae gene encoding aldehyde dehydrogenase is under control of ToxR, the cholera toxin transcriptional activator
    • Parsot C, Mekalanos JJ (1991) Expression of the Vibrio cholerae gene encoding aldehyde dehydrogenase is under control of ToxR, the cholera toxin transcriptional activator. J Bacteriol 173:2842-2851
    • (1991) J Bacteriol , vol.173 , pp. 2842-2851
    • Parsot, C.1    Mekalanos, J.J.2
  • 13
    • 0026508776 scopus 로고
    • Identification and molecular characterization of the gene coding for acetaldehyde dehydrogenase II (acoD) of Alcaligenes eutrophus
    • Priefert H, Krüger N, Jendrossek D, Schmidt B, Steinbüchel A (1992) Identification and molecular characterization of the gene coding for acetaldehyde dehydrogenase II (acoD) of Alcaligenes eutrophus. J Bacteriol 174:899-907
    • (1992) J Bacteriol , vol.174 , pp. 899-907
    • Priefert, H.1    Krüger, N.2    Jendrossek, D.3    Schmidt, B.4    Steinbüchel, A.5
  • 14
    • 0019258605 scopus 로고
    • Genotoxic effects of 1,2-dibromoethane and 1,2-dichloroethane
    • Rannug U (1980) Genotoxic effects of 1,2-dibromoethane and 1,2-dichloroethane. Mutat Res 76:269-295
    • (1980) Mutat Res , vol.76 , pp. 269-295
    • Rannug, U.1
  • 15
    • 0025071351 scopus 로고
    • Degradation of 2-chloroethanol by wild-type and mutants of Pseudomonas putida US2
    • Strotmann UJ, Pentenga M, Janssen DB (1990) Degradation of 2-chloroethanol by wild-type and mutants of Pseudomonas putida US2. Arch Microbiol 154:294-300
    • (1990) Arch Microbiol , vol.154 , pp. 294-300
    • Strotmann, U.J.1    Pentenga, M.2    Janssen, D.B.3
  • 16
    • 0020611347 scopus 로고
    • Bacterial degradation of 2-chloroethanol proceeds via chloroacetic acid
    • Stucki G, Leisinger T (1983) Bacterial degradation of 2-chloroethanol proceeds via chloroacetic acid. FEMS Microbiol Lett 16:123-126
    • (1983) FEMS Microbiol Lett , vol.16 , pp. 123-126
    • Stucki, G.1    Leisinger, T.2
  • 17
    • 0025774284 scopus 로고
    • Involvement of a large plasmid in the degradation of 1,2-dichloroethane by Xanthobacter autotrophicus
    • Tardif G, Greer CW, Labbé D, Lau PCK (1991) Involvement of a large plasmid in the degradation of 1,2-dichloroethane by Xanthobacter autotrophicus. Appl Environ Microbiol 57:1853-1857
    • (1991) Appl Environ Microbiol , vol.57 , pp. 1853-1857
    • Tardif, G.1    Greer, C.W.2    Labbé, D.3    Lau, P.C.K.4
  • 19
    • 0026330982 scopus 로고
    • Characterization of the haloacid dehalogenase from Xanthobacter autotrophicus GJ10 and sequencing of the dhlB gene
    • Van der Ploeg J, Van Hall G, Janssen DB (1991) Characterization of the haloacid dehalogenase from Xanthobacter autotrophicus GJ10 and sequencing of the dhlB gene. J Bacteriol 173:7925-7933
    • (1991) J Bacteriol , vol.173 , pp. 7925-7933
    • Van Der Ploeg, J.1    Van Hall, G.2    Janssen, D.B.3
  • 20
    • 0028269320 scopus 로고
    • Identification of chloroacetaldehyde dehydrogenase involved in 1,2-dichloroethane degradation
    • Van der Ploeg J, Smidt MP, Landa AS, Janssen DB (1994) Identification of chloroacetaldehyde dehydrogenase involved in 1,2-dichloroethane degradation. Appl Environ Microbiol 60:1599-1605
    • (1994) Appl Environ Microbiol , vol.60 , pp. 1599-1605
    • Van Der Ploeg, J.1    Smidt, M.P.2    Landa, A.S.3    Janssen, D.B.4
  • 21
    • 0028949105 scopus 로고
    • Adaptation of Xanthobacter autotrophicus GJ10 to bromoacetate due to activation and mobilization of the haloacetate dehalogenase gene by insertion element IS1247
    • Van der Ploeg J, Willemsen M, Van Hall G, Janssen DB (1995) Adaptation of Xanthobacter autotrophicus GJ10 to bromoacetate due to activation and mobilization of the haloacetate dehalogenase gene by insertion element IS1247. J Bacteriol 177: 1348-1356
    • (1995) J Bacteriol , vol.177 , pp. 1348-1356
    • Van Der Ploeg, J.1    Willemsen, M.2    Van Hall, G.3    Janssen, D.B.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.