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Volumn 367, Issue 2, 2002, Pages 483-489

Cloning, sequencing and heterologous expression of the gene for lupanine hydroxylase, a quinocytochrome c from a Pseudomonas sp.

Author keywords

Cytochrome c; Pyrroloquinoline quinone (PQQ); Quinohaemoprotein; Renaturation; Signal sequence

Indexed keywords

CLONING; DNA; ENZYMES; ESCHERICHIA COLI; GENES; PROTEINS;

EID: 0037108773     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20020729     Document Type: Article
Times cited : (16)

References (25)
  • 1
    • 0000031568 scopus 로고
    • Microbial degradation of lupanine. V. Identification of 17-hydroxylupanine
    • Toczko, M., Brzeski, W. and Kakolewska-Baniuk, A. (1963) Microbial degradation of lupanine. V. Identification of 17-hydroxylupanine. Bull. Acad. Pol. Sci., CI. II, 11, 161-164
    • (1963) Bull. Acad. Pol. Sci., Cl. II , vol.11 , pp. 161-164
    • Toczko, M.1    Brzeski, W.2    Kakolewska-Baniuk, A.3
  • 2
    • 0016607102 scopus 로고
    • Molecular properties of the inducible lupanine hydroxylase from growing cultures of Pseudomonas lupanine
    • Rogozinski, J. (1975) Molecular properties of the inducible lupanine hydroxylase from growing cultures of Pseudomonas lupanine. Acta Biochim. Pol. 32, 57-66
    • (1975) Acta Biochim. Pol. , vol.32 , pp. 57-66
    • Rogozinski, J.1
  • 3
    • 0025812570 scopus 로고
    • Lupanine hydroxylase, a quinocytochrome c from an alkaloid-degrading Pseudomonas sp.
    • Hopper, D. J. Rogozinski, J. and Toczko, M. (1991) Lupanine hydroxylase, a quinocytochrome c from an alkaloid-degrading Pseudomonas sp. Biochem. J. 279, 105-109
    • (1991) Biochem. J. , vol.279 , pp. 105-109
    • Hopper, D.J.1    Rogozinski, J.2    Toczko, M.3
  • 4
    • 0032478046 scopus 로고    scopus 로고
    • Redox potential of the haem c group in the quinocytochrome, lupanine hydroxylase, an enzyme located in the periplasm of a Pseudomonas sp.
    • Hopper, D. J. and Rogozinski, J. (1998) Redox potential of the haem c group in the quinocytochrome, lupanine hydroxylase, an enzyme located in the periplasm of a Pseudomonas sp. Biochim. Biophys. Acta 1383, 160-164
    • (1998) Biochim. Biophys. Acta , vol.1383 , pp. 160-164
    • Hopper, D.J.1    Rogozinski, J.2
  • 5
    • 0029081986 scopus 로고
    • Characterization of the interaction between PQQ and heine c in the quinohemoprotein ethanol dehydrogenase from Comamonas testosteroni
    • de Jong, G. A. H., Caldeira, J., Sun, J., Jongejan, J. A., de Vries, S., Loehr, T. M., Moura, I. and Duine, J. A. (1995) Characterization of the interaction between PQQ and heine c in the quinohemoprotein ethanol dehydrogenase from Comamonas testosteroni. Biochemistry 34, 9451-9458
    • (1995) Biochemistry , vol.34 , pp. 9451-9458
    • De Jong, G.A.H.1    Caldeira, J.2    Sun, J.3    Jongejan, J.A.4    De Vries, S.5    Loehr, T.M.6    Moura, I.7    Duine, J.A.8
  • 6
    • 0030032506 scopus 로고    scopus 로고
    • Characterization of the gene encoding quinohaemoprotein ethanol dehydrogenase of Comamonas testosteroni
    • Stoorvogel, J., Kraayveld, D. E., van Sluis, C. A., Jongejan, J. A., de Vries, S. and Duine, J. A. (1996) Characterization of the gene encoding quinohaemoprotein ethanol dehydrogenase of Comamonas testosteroni. Eur. J. Biochem. 235, 690-698
    • (1996) Eur. J. Biochem. , vol.235 , pp. 690-698
    • Stoorvogel, J.1    Kraayveld, D.E.2    Van Sluis, C.A.3    Jongejan, J.A.4    De Vries, S.5    Duine, J.A.6
  • 7
    • 0036479218 scopus 로고    scopus 로고
    • Crystal structure of quinohemoprotein alcohol dehydrogenase from Comamonas testosteroni
    • Oubrie, A., Rozeboom, H. J., Kalk, K. H., Huizinga, E. G. and Dijkstra, B. W. (2002) Crystal structure of quinohemoprotein alcohol dehydrogenase from Comamonas testosteroni. J. Biol. Chem. 277, 3727-3732
    • (2002) J. Biol. Chem. , vol.277 , pp. 3727-3732
    • Oubrie, A.1    Rozeboom, H.J.2    Kalk, K.H.3    Huizinga, E.G.4    Dijkstra, B.W.5
  • 8
    • 0029643953 scopus 로고
    • The refined structure of the quinoprotein methanol dehydrogenase from Methylobacterium extorquens at 1.94 Å
    • Ghosh, M., Anthony, C., Harlos, K., Goodwin, M. G. and Blake, C. C. F. (1995) The refined structure of the quinoprotein methanol dehydrogenase from Methylobacterium extorquens at 1.94 Å. Structure 3, 177-187
    • (1995) Structure , vol.3 , pp. 177-187
    • Ghosh, M.1    Anthony, C.2    Harlos, K.3    Goodwin, M.G.4    Blake, C.C.F.5
  • 9
    • 0030000290 scopus 로고    scopus 로고
    • Determination of the gene sequence and the three-dimensional structure at a 2.4 Å resolution of methanol dehydrogenase from Methylophilus W3A1
    • Xia, Z., Dai, W., Zhang, Y., White, S. A., Boyd, G. D. and Mathews, F. S. (1996) Determination of the gene sequence and the three-dimensional structure at a 2.4 Å resolution of methanol dehydrogenase from Methylophilus W3A1. J. Mol. Biol. 259, 480-501
    • (1996) J. Mol. Biol. , vol.259 , pp. 480-501
    • Xia, Z.1    Dai, W.2    Zhang, Y.3    White, S.A.4    Boyd, G.D.5    Mathews, F.S.6
  • 10
    • 0001279038 scopus 로고
    • Preparation of genomic DNA from bacteria
    • (Ausubel, F. M., Brent, R., Kingston, R. E., Moore, D. D., Seidman, J. G., Smith, J. A. and Struhl, K., eds.), Greene Publishing Associates & Wiley, New York
    • Wilson, K. (1993) Preparation of genomic DNA from bacteria. In Current Protocols in Molecular Biology, vol. 1 (Ausubel, F. M., Brent, R., Kingston, R. E., Moore, D. D., Seidman, J. G., Smith, J. A. and Struhl, K., eds.), pp: 1-5, Greene Publishing Associates & Wiley, New York
    • (1993) Current Protocols in Molecular Biology , vol.1 , pp. 1-5
    • Wilson, K.1
  • 11
    • 0025276591 scopus 로고
    • A simple single-step procedure for small-scale preparation of Escherichia coli plasmids
    • He, M. Y., Wilde, A. and Kaderbhai, M. A. (1990) A simple single-step procedure for small-scale preparation of Escherichia coli plasmids. Nucleic Acids Res. 8, 1660-1661
    • (1990) Nucleic Acids Res. , vol.8 , pp. 1660-1661
    • He, M.Y.1    Wilde, A.2    Kaderbhai, M.A.3
  • 13
    • 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
  • 14
    • 0023708084 scopus 로고
    • The PMTL NIC-cloning vectors.1. Improved pUC polylinker regions to facilitate the use of sonicated DNA for nucleotide sequencing
    • Chambers, S. P., Prior, S. E., Barstow, D. A. and Minton, N. P. (1988) The PMTL NIC-cloning vectors.1. Improved pUC polylinker regions to facilitate the use of sonicated DNA for nucleotide sequencing Gene 68, 139-149
    • (1988) Gene , vol.68 , pp. 139-149
    • Chambers, S.P.1    Prior, S.E.2    Barstow, D.A.3    Minton, N.P.4
  • 15
    • 0030614959 scopus 로고    scopus 로고
    • Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites
    • Nielsen, H., Engelbrecht, J., Brunak, S. and von Heijne, G. (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
  • 16
    • 0029829590 scopus 로고    scopus 로고
    • A common export pathway for proteins binding complex redox cofactors
    • Berks, B. C. (1996) A common export pathway for proteins binding complex redox cofactors. Mol. Microbiol. 22, 393-404
    • (1996) Mol. Microbiol. , vol.22 , pp. 393-404
    • Berks, B.C.1
  • 17
    • 0037990786 scopus 로고    scopus 로고
    • Biogenesis of respiratory cytochromes in bacteria
    • Thony-Meyer, L. (1997) Biogenesis of respiratory cytochromes in bacteria. Microbiol. Mol. Biol. Rev. 61, 337-376
    • (1997) Microbiol. Mol. Biol. Rev. , vol.61 , pp. 337-376
    • Thony-Meyer, L.1
  • 20
    • 0031833103 scopus 로고    scopus 로고
    • The structure and function of the PQQ-containing quinoprotein dehydrogenases
    • Anthony, C. and Ghosh, M. (1998) The structure and function of the PQQ-containing quinoprotein dehydrogenases. Progr. Biophys. Mol. Biol. 69, 1-21
    • (1998) Progr. Biophys. Mol. Biol. , vol.69 , pp. 1-21
    • Anthony, C.1    Ghosh, M.2
  • 21
    • 0034615786 scopus 로고    scopus 로고
    • X-ray structure of the quinoprotein ethanol dehydrogenase from Pseudomonas aeruginosa: Basis of substrate specificity
    • Keitel, T., Diehl, A., Knaute, T., Stezowski, J. J., Höhne, W and Görisch, H. (2000) X-ray structure of the quinoprotein ethanol dehydrogenase from Pseudomonas aeruginosa: Basis of substrate specificity. J. Mol. Biol. 297, 961-974
    • (2000) J. Mol. Biol. , vol.297 , pp. 961-974
    • Keitel, T.1    Diehl, A.2    Knaute, T.3    Stezowski, J.J.4    Höhne, W.5    Görisch, H.6
  • 22
    • 0032945593 scopus 로고    scopus 로고
    • DIALIGN 2: Improvement of the segment-to-segment approach to multiple sequence alignment
    • Morgenstern, B. (1999) DIALIGN 2: Improvement of the segment-to-segment approach to multiple sequence alignment Bioinformatics 15, 211-218
    • (1999) Bioinformatics , vol.15 , pp. 211-218
    • Morgenstern, B.1
  • 23
    • 0033522648 scopus 로고    scopus 로고
    • The 1.7 Å crystal structure of the apo form of the quinoprotein glucose dehydrogenase from Acinetobacter calcoaceticus reveals a novel internal conserved sequence repeat
    • Oubrie, A., Rozeboom, H. J., Kalk, K. H., Duine, J. A. and Dijkstra, B. W. (1999) The 1.7 Å crystal structure of the apo form of the quinoprotein glucose dehydrogenase from Acinetobacter calcoaceticus reveals a novel internal conserved sequence repeat. J. Mol. Biol. 289, 319-333
    • (1999) J. Mol. Biol. , vol.289 , pp. 319-333
    • Oubrie, A.1    Rozeboom, H.J.2    Kalk, K.H.3    Duine, J.A.4    Dijkstra, B.W.5
  • 24
    • 0033858629 scopus 로고    scopus 로고
    • Structural requirements of pyrroloquinoline quinone dependent enzymatic reactions
    • Oubrie, A. and Dijkstra, B. W. (2000) Structural requirements of pyrroloquinoline quinone dependent enzymatic reactions. Protein Sci, 97, 1265-1273
    • (2000) Protein Sci. , vol.97 , pp. 1265-1273
    • Oubrie, A.1    Dijkstra, B.W.2
  • 25
    • 0029609904 scopus 로고
    • Structure of the quinoprotein glucose dehydrogenase of Escherichia coli modelled on that of methanol dehydrogenase from Methylobacterium extorquens
    • Cozier, G. E. and Anthony, C. (1995) Structure of the quinoprotein glucose dehydrogenase of Escherichia coli modelled on that of methanol dehydrogenase from Methylobacterium extorquens. Biochem. J. 312, 679-685
    • (1995) Biochem. J. , vol.312 , pp. 679-685
    • Cozier, G.E.1    Anthony, C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.