메뉴 건너뛰기




Volumn 148, Issue 10, 2002, Pages 3285-3292

Molecular and functional characterization of the kstD2 gene of Rhodococcus erythropolis SQ1 encoding a second 3-ketosteroid Δ1-dehydrogenase isoenzyme

Author keywords

3 ketosteroid dehydrogenase; Isoenzymes; Steroid; Unmarked gene deletion

Indexed keywords

ANDROSTANE DERIVATIVE; ANDROSTENEDIONE; GENOMIC DNA; HYDROXYL GROUP; ISOENZYME; SERINE; STEROID REDUCTASE; THREONINE;

EID: 0036772150     PISSN: 13500872     EISSN: None     Source Type: Journal    
DOI: 10.1099/00221287-148-10-3285     Document Type: Article
Times cited : (85)

References (22)
  • 3
    • 0027257316 scopus 로고
    • Improved purification of steroid 1:2-dehydrogenase from Nocardia opaca and partial characterization of its cloned gene sequence
    • Drobnic, K., Križaj, L., Gubenšek, F. & Komel, R. (1993). Improved purification of steroid 1:2-dehydrogenase from Nocardia opaca and partial characterization of its cloned gene sequence, Biochem Biophys Res Commun 190, 509-515.
    • (1993) Biochem. Biophys. Res. Commun , vol.190 , pp. 509-515
    • Drobnic, K.1    Križaj, L.2    Gubenšek, F.3    Komel, R.4
  • 4
    • 0032248628 scopus 로고    scopus 로고
    • Cloning, sequencing and characterization of a downstream region of ksdDI operon of Arthrobacter simplex
    • Dziadek, J., Yamashita, M. & Murooka, Y. (1998). Cloning, sequencing and characterization of a downstream region of ksdDI operon of Arthrobacter simplex. Acta Microbiol Pol 47, 345-353.
    • (1998) Acta Microbiol. Pol , vol.47 , pp. 345-353
    • Dziadek, J.1    Yamashita, M.2    Murooka, Y.3
  • 7
    • 0026779136 scopus 로고
    • Steroid-1-dehydrogenase of Rhodococcus erythropolis: Purification and N-terminal amino acid sequence
    • Kaufmann, G., Thole, H., Kraft, R. & Atrat, P. (1992). Steroid-1-dehydrogenase of Rhodococcus erythropolis: purification and N-terminal amino acid sequence. J Steroid Biochem Mol Biol 43, 297-301.
    • (1992) J. Steroid. Biochem. Mol. Biol , vol.43 , pp. 297-301
    • Kaufmann, G.1    Thole, H.2    Kraft, R.3    Atrat, P.4
  • 9
    • 0032198828 scopus 로고    scopus 로고
    • 1-dehydrogenase of Rhodococcus rhodochrous: Sequencing of the genomic DNA and hyperexpression, purification, and characterization of the recombinant enzyme
    • 1-dehydrogenase of Rhodococcus rhodochrous: sequencing of the genomic DNA and hyperexpression, purification, and characterization of the recombinant enzyme. J Biochem 124, 1026-1032.
    • (1998) J. Biochem , vol.124 , pp. 1026-1032
    • Morii, S.1    Fujii, C.2    Miyoshi, T.3    Iwami, M.4    Itagaki, E.5
  • 10
    • 0039001059 scopus 로고
    • Improved double-stranded DNA sequencing using the linear polymerase chain reaction
    • Murray, V. (1989). Improved double-stranded DNA sequencing using the linear polymerase chain reaction. Nucleic Acids Res 17, 8889.
    • (1989) Nucleic Acids Res , vol.17 , pp. 8889
    • Murray, V.1
  • 12
    • 0027406801 scopus 로고
    • Nocardioform arsenic resistance plasmid characterization and improved Rhodococcus cloning vectors
    • Quan, S. & Dabbs, E. R. (1993). Nocardioform arsenic resistance plasmid characterization and improved Rhodococcus cloning vectors. Plasmid 29, 74-79.
    • (1993) Plasmid , vol.29 , pp. 74-79
    • Quan, S.1    Dabbs, E.R.2
  • 13
    • 0028289983 scopus 로고
    • Small mobilizable multi-purpose cloning vectors derived from the Escherichia coli plasmids pK18 and pK19: Selection of defined deletions in the chromosome of Corynebacterium glutamicum
    • Schäfer, A., Tauch, A., Jäger, W., Kalinowski, J., Thierbach, G. & Pühler, A. (1994). Small mobilizable multi-purpose cloning vectors derived from the Escherichia coli plasmids pK18 and pK19: selection of defined deletions in the chromosome of Corynebacterium glutamicum. Gene 145, 69-73.
    • (1994) Gene , vol.145 , pp. 69-73
    • Schäfer, A.1    Tauch, A.2    Jäger, W.3    Kalinowski, J.4    Thierbach, G.5    Pühler, A.6
  • 14
    • 50549187554 scopus 로고
    • Steroid 1-dehydrogenase of Nocardia restrictus
    • Sih, C. J. & Bennet, R. E. (1962). Steroid 1-dehydrogenase of Nocardia restrictus. Biochim Biophys Acta 56, 587-592.
    • (1962) Biochim. Biophys. Acta , vol.56 , pp. 587-592
    • Sih, C.J.1    Bennet, R.E.2
  • 15
    • 0021027842 scopus 로고
    • A broad host range mobilization system for in vivo genetic engineering: Transposon mutagenesis in gram negative bacteria
    • Simon, R., Priefer, U. & Pühler, A. (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
  • 16
    • 0023042283 scopus 로고
    • Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes
    • Studier, F. W. & Moffatt, B. A. (1986). Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes. J Mol Biol 189, 113-130.
    • (1986) J. Mol. Biol , vol.189 , pp. 113-130
    • Studier, F.W.1    Moffatt, B.A.2
  • 17
    • 0027968068 scopus 로고
    • CLUSTALW: Improving the sensitivity of progressive multiple sequence alignment through sequence weighing, position-specific gap penalties and weight matrix
    • Thompson, J. D., Higgins, D. G. & Gibson, T. J. (1994). CLUSTALW: improving the sensitivity of progressive multiple sequence alignment through sequence weighing, position-specific gap penalties and weight matrix. Nucleic Acids Res 22, 4673-4680.
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 20
    • 0036038941 scopus 로고    scopus 로고
    • Molecular and functional characterization of kshA and kshB, encoding two components of 3-ketosteroid 9α-hydroxylase, a class IA monooxygenase, in Rhodococcus erythropolis strain SQ1
    • Van der Geize, R., Hessels, G. I., Van Gerwen, R., Van der Meijden, P. & Dijkhuizen, L. (2002). Molecular and functional characterization of kshA and kshB, encoding two components of 3-ketosteroid 9α-hydroxylase, a class IA monooxygenase, in Rhodococcus erythropolis strain SQ1. Mol Microbiol 45, 1007-1018.
    • (2002) Mol. Microbiol , vol.45 , pp. 1007-1018
    • Van der Geize, R.1    Hessels, G.I.2    Van Gerwen, R.3    Van der Meijden, P.4    Dijkhuizen, L.5
  • 21
    • 0027031430 scopus 로고
    • Overexpression of a Rhodococcus erythropolis protein in Escherichia coli with immunological identity to the Rhodococcus steroid 1-dehydrogenase. Immunoelectron microscopic localization and electrophoretic studies
    • Wagner, M., Atrat, P. G., Wagner, B., Hanemann, V. & Clark-Curtiss, J. E. (1992). Overexpression of a Rhodococcus erythropolis protein in Escherichia coli with immunological identity to the Rhodococcus steroid 1-dehydrogenase. Immunoelectron microscopic localization and electrophoretic studies. J Basic Microbiol 32, 269-277.
    • (1992) J. Basic Microbiol , vol.32 , pp. 269-277
    • Wagner, M.1    Atrat, P.G.2    Wagner, B.3    Hanemann, V.4    Clark-Curtiss, J.E.5
  • 22
    • 0018700885 scopus 로고
    • Evidence for two steroid 1,2-dehydrogenase activities in Mycobacterium fortuitum
    • Wovcha, M. G., Brooks, K. E. & Kominek, L. A. (1979). Evidence for two steroid 1,2-dehydrogenase activities in Mycobacterium fortuitum. Biochim Biophys Acta 574, 471-479.
    • (1979) Biochim. Biophys. Acta , vol.574 , pp. 471-479
    • Wovcha, M.G.1    Brooks, K.E.2    Kominek, L.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.