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Volumn 180, Issue 17, 1998, Pages 4387-4391

Purification and characterization of the coniferyl aldehyde dehydrogenase from Pseudomonas sp. strain HR199 and molecular characterization of the gene

Author keywords

[No Author keywords available]

Indexed keywords

ALDEHYDE; ALDEHYDE DEHYDROGENASE; CONIFERYLALDEHYDE; CONIFERYLALDEHYDE DEHYDROGENASE; GENE PRODUCT; UNCLASSIFIED DRUG;

EID: 0031750997     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.180.17.4387-4391.1998     Document Type: Article
Times cited : (42)

References (38)
  • 1
    • 0021710537 scopus 로고
    • The relationship between base composition and codon usage in bacterial genes and its use for the simple and reliable identification of protein-coding sequences
    • Bibb, M. J., P. R. Findlay, and M. W. Johnson. 1984. The relationship between base composition and codon usage in bacterial genes and its use for the simple and reliable identification of protein-coding sequences. Gene 30:157-166.
    • (1984) Gene , vol.30 , pp. 157-166
    • Bibb, M.J.1    Findlay, P.R.2    Johnson, M.W.3
  • 2
    • 0025883547 scopus 로고
    • Characterization of an Escherichia coli gene encoding betaine aldehyde dehydrogenase (BADH): Structural similarity to mammalian ALDHs and plant BADH
    • Boyed, L. A., L. Adam, L. E. Pelcher, A. McHughen, R. Hirji, and G. Selvaraj. 1991. Characterization of an Escherichia coli gene encoding betaine aldehyde dehydrogenase (BADH): structural similarity to mammalian ALDHs and plant BADH. Gene 103:45-52.
    • (1991) Gene , vol.103 , pp. 45-52
    • Boyed, L.A.1    Adam, L.2    Pelcher, L.E.3    McHughen, A.4    Hirji, R.5    Selvaraj, G.6
  • 3
    • 0000182975 scopus 로고
    • XL1-Blue: A high efficiency plasmid transforming recA Escherichia coli strain with beta-galactosidase selection
    • Bullock, W. O., J. M. Fernandez, and J. M. Stuart. 1987. XL1-Blue: a high efficiency plasmid transforming recA Escherichia coli strain with beta-galactosidase selection. BioTechniques 5:376-379.
    • (1987) BioTechniques , vol.5 , pp. 376-379
    • Bullock, W.O.1    Fernandez, J.M.2    Stuart, J.M.3
  • 4
    • 0027386075 scopus 로고
    • Metabolism of dibenzothiophene and naphthalene in Pseudomonas strains: Complete DNA sequence of an upper naphthalene catabolic pathway
    • Denome, S. A., D. C. Stanley, E. S. Olson, and K. D. Young. 1993. Metabolism of dibenzothiophene and naphthalene in Pseudomonas strains: complete DNA sequence of an upper naphthalene catabolic pathway. J. Bacteriol. 175:6890-6901.
    • (1993) J. Bacteriol. , vol.175 , pp. 6890-6901
    • Denome, S.A.1    Stanley, D.C.2    Olson, E.S.3    Young, K.D.4
  • 5
    • 0021760092 scopus 로고
    • A comprehensive set of sequence analysis programs for the VAX
    • Devereux, J., P. Haeberli, and O. Smithies. 1984. A comprehensive set of sequence analysis programs for the VAX. Nucleic Acids Res. 12:387-395.
    • (1984) Nucleic Acids Res. , vol.12 , pp. 387-395
    • Devereux, J.1    Haeberli, P.2    Smithies, O.3
  • 6
    • 0018928658 scopus 로고
    • Degradation of coniferyl alcohol and other lignin-related aromatic compounds by Nocardia sp. DSM 1069
    • Eggeling, L., and H. Sahm. 1980. Degradation of coniferyl alcohol and other lignin-related aromatic compounds by Nocardia sp. DSM 1069. Arch. Microbiol. 126:141-148.
    • (1980) Arch. Microbiol. , vol.126 , pp. 141-148
    • Eggeling, L.1    Sahm, H.2
  • 7
    • 0028961395 scopus 로고
    • Investigation of the active site cysteine residue of rat liver mitochondrial aldehyde dehydrogenase by site-directed mutagenesis
    • Farrés, J., T. T. Y. Wang, S. J. Cunningham, and H. Weiner. 1995. Investigation of the active site cysteine residue of rat liver mitochondrial aldehyde dehydrogenase by site-directed mutagenesis. Biochemistry 34:2592-2598.
    • (1995) Biochemistry , vol.34 , pp. 2592-2598
    • Farrés, J.1    Wang, T.T.Y.2    Cunningham, S.J.3    Weiner, H.4
  • 8
    • 0020959710 scopus 로고
    • Studies on transformation of Escherichia coli with plasmids
    • Hanahan, D. 1983. Studies on transformation of Escherichia coli with plasmids. J. Mol. Biol. 166:557-580.
    • (1983) J. Mol. Biol. , vol.166 , pp. 557-580
    • Hanahan, D.1
  • 9
    • 0022341743 scopus 로고
    • Mitochondrial aldehyde dehydrogenase from human liver. Primary structure, differences in relation to the cytosolic enzyme, and functional correlations
    • Hempel, J., R. Kaiser, and H. Jörnvall. 1985. Mitochondrial aldehyde dehydrogenase from human liver. Primary structure, differences in relation to the cytosolic enzyme, and functional correlations. Eur. J. Biochem. 153:13-28.
    • (1985) Eur. J. Biochem. , vol.153 , pp. 13-28
    • Hempel, J.1    Kaiser, R.2    Jörnvall, H.3
  • 10
    • 0027525666 scopus 로고
    • Aldehyde dehydrogenases: Widespread structural and functional diversity within a shared framework
    • Hempel, J., H. Nicholas, and R. Lindahl. 1993. Aldehyde dehydrogenases: widespread structural and functional diversity within a shared framework. Protein Sci. 2:1890-1900.
    • (1993) Protein Sci. , vol.2 , pp. 1890-1900
    • Hempel, J.1    Nicholas, H.2    Lindahl, R.3
  • 11
    • 0028958160 scopus 로고
    • Overlapping substrate specificities of benzaldehyde dehydrogenase (the xylC gene product) and 2-hydroxymuconic semialdehyde dehydrogenase (the xylG gene product) encoded by TOL plasmid pWW0 of Pseudomonas putida
    • Inoue, J., J. P. Shaw, M. Rekik, and S. Harayama. 1995. Overlapping substrate specificities of benzaldehyde dehydrogenase (the xylC gene product) and 2-hydroxymuconic semialdehyde dehydrogenase (the xylG gene product) encoded by TOL plasmid pWW0 of Pseudomonas putida. J. Bacteriol. 177: 1196-1201.
    • (1995) J. Bacteriol. , vol.177 , pp. 1196-1201
    • Inoue, J.1    Shaw, J.P.2    Rekik, M.3    Harayama, S.4
  • 12
    • 0023656153 scopus 로고
    • Three different proteins exhibiting NAD-dependent acetaldehyde dehydrogenase activity from Alcaligenes eutrophus
    • Jendrossek, D., A. Steinbüchel, and H. G. Schlegel. 1987. Three different proteins exhibiting NAD-dependent acetaldehyde dehydrogenase activity from Alcaligenes eutrophus. Eur. J. Biochem. 167:541-548.
    • (1987) Eur. J. Biochem. , vol.167 , pp. 541-548
    • Jendrossek, D.1    Steinbüchel, A.2    Schlegel, H.G.3
  • 13
    • 0021746513 scopus 로고
    • Characterization of a ligninolytic bacterial isolate: Taxonomic relatedness and oxidation of some lignin related compounds
    • Kern, H. W., L. E. Webb, and L. Eggeling. 1984. Characterization of a ligninolytic bacterial isolate: taxonomic relatedness and oxidation of some lignin related compounds. Syst. Appl. Microbiol. 5:433-447.
    • (1984) Syst. Appl. Microbiol. , vol.5 , pp. 433-447
    • Kern, H.W.1    Webb, L.E.2    Eggeling, L.3
  • 14
    • 0019904249 scopus 로고
    • Wide host range cloning vectors: A cosmid clone bank of an Agrobacterium Ti plasmid
    • Knauf, V. C., and E. W. Nester. 1982. Wide host range cloning vectors: a cosmid clone bank of an Agrobacterium Ti plasmid. Plasmid 8:45-54.
    • (1982) Plasmid , vol.8 , pp. 45-54
    • Knauf, V.C.1    Nester, E.W.2
  • 15
    • 0024556880 scopus 로고
    • The Pseudomonas oleovorans alkBAC operon encodes two structurally related rubredoxins and an aldehyde dehydroge-nase
    • Kok, M., R. Oldenhuis, M. P. G. van der Linden, C. H. C. Meulenberg, J. Kingma, and B. Witholt. 1989. The Pseudomonas oleovorans alkBAC operon encodes two structurally related rubredoxins and an aldehyde dehydroge-nase. J. Biol. Chem. 264:5442-5451.
    • (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
  • 17
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (London) 227:680-685.
    • (1970) Nature (London) , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 20
    • 0024287195 scopus 로고
    • Benzyl alcohol dehydrogenase and benzaldehyde dehydrogenase II from Acinetobacter calcoaceticus
    • MacKintosh, R. W., and C. A. Fewson. 1988. Benzyl alcohol dehydrogenase and benzaldehyde dehydrogenase II from Acinetobacter calcoaceticus. Biochem. J. 250:743-751.
    • (1988) Biochem. J. , vol.250 , pp. 743-751
    • MacKintosh, R.W.1    Fewson, C.A.2
  • 21
    • 0025935386 scopus 로고
    • Molecular cloning, sequencing, and expression of cDNA for rat liver microsomal aldehyde dehydrogenase
    • Miyauchi, K., R. Masaki, S. Taketani, A. Yamamoto, M. Akayama, and Y. Tashiro. 1991. Molecular cloning, sequencing, and expression of cDNA for rat liver microsomal aldehyde dehydrogenase. J. Biol. Chem. 266:19536-19542.
    • (1991) J. Biol. Chem. , vol.266 , pp. 19536-19542
    • Miyauchi, K.1    Masaki, R.2    Taketani, S.3    Yamamoto, A.4    Akayama, M.5    Tashiro, Y.6
  • 22
    • 0027429443 scopus 로고
    • Molecular organization of the Escherichia coli gab cluster: Nucleotide sequence of the structural genes gabD and gubP and expression of the GABA permease gene
    • Niegemann, E., A. Schulz, and K. Bartsch. 1993. Molecular organization of the Escherichia coli gab cluster: nucleotide sequence of the structural genes gabD and gubP and expression of the GABA permease gene. Arch. Microbiol. 160:454-460.
    • (1993) Arch. Microbiol. , vol.160 , pp. 454-460
    • Niegemann, E.1    Schulz, A.2    Bartsch, K.3
  • 24
    • 0025913664 scopus 로고
    • Identification and molecular characterization of the Alcaligenes eutrophus H16 aco operon genes involved in acetoin catabolism
    • Priefert, H., S. Hein, N. Krüger, K. Zeh, B. Schmidt, and A. Steinbüchel. 1991. Identification and molecular characterization of the Alcaligenes eutrophus H16 aco operon genes involved in acetoin catabolism. J. Bacteriol. 173:4056-4071.
    • (1991) J. Bacteriol. , vol.173 , pp. 4056-4071
    • Priefert, H.1    Hein, S.2    Krüger, N.3    Zeh, K.4    Schmidt, B.5    Steinbüchel, A.6
  • 25
    • 0026508776 scopus 로고
    • Identification and molecular characterization of the gene coding for acetaldehyde dehydrogenase II (acoD) of Alcaligenes eutrophus
    • Priefert, H., N. Krüger, D. Jendrossek, B. Schmidt, and A. Steinbüchel. 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
  • 26
    • 0030981938 scopus 로고    scopus 로고
    • Molecular characterization of genes of Pseudomonas sp. strain HR199 involved in bioconversion of vanillin to protocatechuate
    • Priefert, H., J. Rabenhorst, and A. Steinbüchel. 1997. Molecular characterization of genes of Pseudomonas sp. strain HR199 involved in bioconversion of vanillin to protocatechuate. J. Bacteriol. 179:2595-2607.
    • (1997) J. Bacteriol. , vol.179 , pp. 2595-2607
    • Priefert, H.1    Rabenhorst, J.2    Steinbüchel, A.3
  • 27
    • 0030466186 scopus 로고    scopus 로고
    • Production of methoxyphenol type natural aroma chemicals by biotransformation of eugenol with a new Pseudomonas sp
    • Rabenhorst, J. 1996. Production of methoxyphenol type natural aroma chemicals by biotransformation of eugenol with a new Pseudomonas sp. Appl. Microbiol. Biotechnol. 46:470-474.
    • (1996) Appl. Microbiol. Biotechnol. , vol.46 , pp. 470-474
    • Rabenhorst, J.1
  • 28
    • 0025909284 scopus 로고
    • Molecular cloning of the mitochondrial aldehyde dehydrogenase gene of Saccharomyces cerevisiae by genetic complementation
    • Saigal, D., S. J. Cunningham, J. Farrés, and H. Weiner. 1991. Molecular cloning of the mitochondrial aldehyde dehydrogenase gene of Saccharomyces cerevisiae by genetic complementation. J. Bacteriol. 173:3199-3208.
    • (1991) J. Bacteriol. , vol.173 , pp. 3199-3208
    • Saigal, D.1    Cunningham, S.J.2    Farrés, J.3    Weiner, H.4
  • 30
    • 34250969714 scopus 로고
    • Ein Submersverfahren zur Kultur wasserstoffoxidierender Bakterien: Wachstumsphysiologische Untersuchungen
    • Schlegel, H. G., H. Kaltwasser, and G. Gottschalk. 1961. Ein Submersverfahren zur Kultur wasserstoffoxidierender Bakterien: Wachstumsphysiologische Untersuchungen. Arch. Mikrobiol. 38:209-222.
    • (1961) Arch. Mikrobiol. , vol.38 , pp. 209-222
    • Schlegel, H.G.1    Kaltwasser, H.2    Gottschalk, G.3
  • 31
    • 0030811549 scopus 로고    scopus 로고
    • The potential roles of the conserved amino acids in human liver mitochondrial aldehyde dehydrogenase
    • Sheikh, S., L. Ni, T. D. Hurley, and H. Weiner. 1997. The potential roles of the conserved amino acids in human liver mitochondrial aldehyde dehydrogenase. J. Biol. Chem. 272:18817-18822.
    • (1997) J. Biol. Chem. , vol.272 , pp. 18817-18822
    • Sheikh, S.1    Ni, L.2    Hurley, T.D.3    Weiner, H.4
  • 32
    • 0021027842 scopus 로고
    • A broad host range mobilization system for in vivo genetic engineering: Transposon mutagenesis in gram-negative bacteria
    • Simon, R., U. Priefer, and A. Pühler. 1983. A broad host range mobilization system for in vivo genetic engineering: transposon mutagenesis in gram-negative bacteria. Bio/Technology 1:784-791.
    • (1983) Bio/Technology , vol.1 , pp. 784-791
    • Simon, R.1    Priefer, U.2    Pühler, A.3
  • 33
    • 0031570328 scopus 로고    scopus 로고
    • Structure of mitochondrial aldehyde dehydrogenase: The genetic component of ethanol aversion
    • Steinmetz, C. G., P.-G. Xie, H. Weiner, and T. D. Hurley. 1997. Structure of mitochondrial aldehyde dehydrogenase: the genetic component of ethanol aversion. Structure 5:701-711.
    • (1997) Structure , vol.5 , pp. 701-711
    • Steinmetz, C.G.1    Xie, P.-G.2    Weiner, H.3    Hurley, T.D.4
  • 35
    • 0017370171 scopus 로고
    • Degradation of eugenol by a microorganism
    • Tadasa, K. 1977. Degradation of eugenol by a microorganism. Agric. Biol. Chem. 41:925-929.
    • (1977) Agric. Biol. Chem. , vol.41 , pp. 925-929
    • Tadasa, K.1
  • 36
    • 0000015935 scopus 로고
    • Initial steps of eugenol degradation pathway of a microorganism
    • Tadasa, K., and H. Kayahara. 1983. Initial steps of eugenol degradation pathway of a microorganism. Agric. Biol. Chem. 47:2639-2640.
    • (1983) Agric. Biol. Chem. , vol.47 , pp. 2639-2640
    • Tadasa, K.1    Kayahara, H.2
  • 38
    • 0028922730 scopus 로고
    • Involvement of glutamate 268 in the active site of human liver mitochondrial (class 2) aldehyde dehydrogenase as probed by site-directed mutagenesis
    • Wang, X. P., and H. Weiner. 1995. Involvement of glutamate 268 in the active site of human liver mitochondrial (class 2) aldehyde dehydrogenase as probed by site-directed mutagenesis. Biochemistry 34:237-243.
    • (1995) Biochemistry , vol.34 , pp. 237-243
    • Wang, X.P.1    Weiner, H.2


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