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Volumn 126, Issue 3, 1999, Pages 624-631

Steroid monooxygenase of Rhodococcus rhodochrous: Sequencing of the genomic DNA, and hyperexpression, purification, and characterization of the recombinant enzyme

Author keywords

Biological Baeyer Villiger reaction; Hyperexpression; Recombinant enzyme; Sequence; Steroid monooxygenase

Indexed keywords

ACETIC ACID; CARBON; OXYGEN; PROGESTERONE; RECOMBINANT ENZYME; STEROID MONOOXYGENASE; TESTOSTERONE DERIVATIVE;

EID: 0032862663     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.jbchem.a022494     Document Type: Article
Times cited : (58)

References (29)
  • 1
    • 0022689290 scopus 로고
    • Studies on steroid monooxygenase from Cylindrocarpon radicicola ATCC 11011. Purification and characterization
    • Itagaki, E. (1986) Studies on steroid monooxygenase from Cylindrocarpon radicicola ATCC 11011. Purification and characterization. J. Biochem. 99, 815-824
    • (1986) J. Biochem. , vol.99 , pp. 815-824
    • Itagaki, E.1
  • 2
    • 0022684918 scopus 로고
    • Studies on steroid monooxygenase from Cylindrocarpon radicicola ATCC11011. Oxygenative lactonization of androstenedione to testololactone
    • Itagaki, E. (1986) Studies on steroid monooxygenase from Cylindrocarpon radicicola ATCC11011. Oxygenative lactonization of androstenedione to testololactone. J. Biochem. 99, 825-832
    • (1986) J. Biochem. , vol.99 , pp. 825-832
    • Itagaki, E.1
  • 3
    • 0345376128 scopus 로고
    • A steroid ketone monooxygenase from Cylindrocarpon radicicola
    • Müller, F., ed. CRC Press, Boca Raton
    • Katagiri, M. and Itagaki, E. (1991) A steroid ketone monooxygenase from Cylindrocarpon radicicola in Chemistry and Biochemistry of Flavoenzymes (Müller, F., ed.) Vol. II, pp. 101-108, CRC Press, Boca Raton
    • (1991) Chemistry and Biochemistry of Flavoenzymes , vol.2 , pp. 101-108
    • Katagiri, M.1    Itagaki, E.2
  • 4
    • 0345376130 scopus 로고
    • Steroid monooxygenase from Cylindrocarpon radicicola. An FAD-containing Baeyer-Villiger type oxygenase
    • Bray, R.C., Engel, P.C., and Mayhew, S.G. eds. Walter de Gruyter, Berlin
    • Itagaki, E. and Katagiri, M. (1984) Steroid monooxygenase from Cylindrocarpon radicicola. An FAD-containing Baeyer-Villiger type oxygenase in Flavins and Flavoproteins (Bray, R.C., Engel, P.C., and Mayhew, S.G. eds.) pp. 639-642, Walter de Gruyter, Berlin
    • (1984) Flavins and Flavoproteins , pp. 639-642
    • Itagaki, E.1    Katagiri, M.2
  • 6
    • 0017227971 scopus 로고
    • The purification and properties of cyclohexanone oxygenase from Nocardia globerula CL1 and Acinetobacter NCIB 9871
    • Donoghue, N.A., Norris, D.B., and Trudgill, P.W. (1976) The purification and properties of cyclohexanone oxygenase from Nocardia globerula CL1 and Acinetobacter NCIB 9871. Eur. J. Biochem. 63, 175-192
    • (1976) Eur. J. Biochem. , vol.63 , pp. 175-192
    • Donoghue, N.A.1    Norris, D.B.2    Trudgill, P.W.3
  • 7
    • 0017283120 scopus 로고
    • Purification and properties of cyclohexanone oxygenase from Pseudomonas NCIB 9872
    • Griffin, M. and Trudgill, P.W. (1976) Purification and properties of cyclohexanone oxygenase from Pseudomonas NCIB 9872. Eur. J. Biochem. 63, 199-209
    • (1976) Eur. J. Biochem. , vol.63 , pp. 199-209
    • Griffin, M.1    Trudgill, P.W.2
  • 8
    • 0020490705 scopus 로고
    • Mechanistic studies on cyclohexanone oxygenase
    • Ryerson, C.C., Ballou, D.P., and Walsh, C.T. (1982) Mechanistic studies on cyclohexanone oxygenase. Biochemistry 21, 2644-2655
    • (1982) Biochemistry , vol.21 , pp. 2644-2655
    • Ryerson, C.C.1    Ballou, D.P.2    Walsh, C.T.3
  • 9
    • 0023958999 scopus 로고
    • Acinetobacter cyclohexanone monooxygenase: Gene cloning and sequence determination
    • Chen, Y.-C.J., People, O.P., and Walsh, C.T. (1988) Acinetobacter cyclohexanone monooxygenase: Gene cloning and sequence determination. J. Bacteriol. 170, 781-789
    • (1988) J. Bacteriol. , vol.170 , pp. 781-789
    • Chen, Y.-C.J.1    People, O.P.2    Walsh, C.T.3
  • 10
    • 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
  • 11
    • 0022650756 scopus 로고
    • A small scale five-hour procedure for isolating multiple samples of CsCl-purified DNA: Application to isolations from mammalian, insect, higher plant, algal, yeast, and bacterial sources
    • Weeks, D.P., Beerman, N., and Griffith, O.M. (1986) A small scale five-hour procedure for isolating multiple samples of CsCl-purified DNA: application to isolations from mammalian, insect, higher plant, algal, yeast, and bacterial sources. Anal. Biochem. 152, 376-385
    • (1986) Anal. Biochem. , vol.152 , pp. 376-385
    • Weeks, D.P.1    Beerman, N.2    Griffith, O.M.3
  • 12
    • 0030608159 scopus 로고    scopus 로고
    • Structure of chromosomal DNA coding for pseudomonas putida S-1 salicylate hydroxylase
    • Suzuki, K., Mizuguchi, M., Ohnishi, K., and Itagaki, E. (1996) Structure of chromosomal DNA coding for Pseudomonas putida S-1 salicylate hydroxylase. Biochim. Biophys. Acta 1275, 154-156
    • (1996) Biochim. Biophys. Acta , vol.1275 , pp. 154-156
    • Suzuki, K.1    Mizuguchi, M.2    Ohnishi, K.3    Itagaki, E.4
  • 13
    • 0020770873 scopus 로고
    • P-Hydroxybenzoate hydroxylase from Pseudomonas fluorescence. I. Completion of the elucidation of the primary structure
    • Hofsteenge, J., Weijer, W.J., Jekel, P.A., and Beintema, J.J. (1983) p-Hydroxybenzoate hydroxylase from Pseudomonas fluorescence. I. Completion of the elucidation of the primary structure. Eur. J. Biochem. 133, 91-108
    • (1983) Eur. J. Biochem. , vol.133 , pp. 91-108
    • Hofsteenge, J.1    Weijer, W.J.2    Jekel, P.A.3    Beintema, J.J.4
  • 14
    • 0023041821 scopus 로고
    • Prediction of the occurrence of the ADP-binding βαβ-fold in proteins, using an amino acid sequence fingerprint
    • Wierenga, R.K., Terpstra, P., and Hol, W.G.J. (1986) Prediction of the occurrence of the ADP-binding βαβ-fold in proteins, using an amino acid sequence fingerprint. J. Mol. Biol. 187, 101-107
    • (1986) J. Mol. Biol. , vol.187 , pp. 101-107
    • Wierenga, R.K.1    Terpstra, P.2    Hol, W.G.J.3
  • 15
    • 0024516824 scopus 로고
    • cDNA sequence of adrenodoxin reductase. Identification of NADP-binding sites in oxidoreductases
    • Hanukoglu, I. and Gutfinger, T. (1989) cDNA sequence of adrenodoxin reductase. Identification of NADP-binding sites in oxidoreductases. Eur. J. Biochem. 180, 479-484
    • (1989) Eur. J. Biochem. , vol.180 , pp. 479-484
    • Hanukoglu, I.1    Gutfinger, T.2
  • 16
    • 0024296240 scopus 로고
    • A gene from Mycobacterium tuberculosis which is homologous to the DnaJ heat shock protein of E. coli
    • Lathigra, R.B., Young, D.B., Sweetser, D., and Young, R.A. (1988) A gene from Mycobacterium tuberculosis which is homologous to the DnaJ heat shock protein of E. coli. Nucleic Acids Res. 16, 1636
    • (1988) Nucleic Acids Res. , vol.16 , pp. 1636
    • Lathigra, R.B.1    Young, D.B.2    Sweetser, D.3    Young, R.A.4
  • 17
    • 0029984895 scopus 로고    scopus 로고
    • A novel gene cluster including the Rhodococcus rhodochrous J1 nhlBA genes encoding a low molecular mass nitrile hydratase (L-NHase) induced by its reaction product
    • Komeda, H., Kobayashi, M., and Shimizu, S. (1996) A novel gene cluster including the Rhodococcus rhodochrous J1 nhlBA genes encoding a low molecular mass nitrile hydratase (L-NHase) induced by its reaction product. J. Biol. Chem. 271, 15796-15802
    • (1996) J. Biol. Chem. , vol.271 , pp. 15796-15802
    • Komeda, H.1    Kobayashi, M.2    Shimizu, S.3
  • 18
    • 0021147979 scopus 로고
    • Nucleotide sequence of the temperate Bacillus subtilis bacteriophage SP02 DNA polymerase gene L.
    • Raden, B. and Rutberg, L. (1984) Nucleotide sequence of the temperate Bacillus subtilis bacteriophage SP02 DNA polymerase gene L. J. Virol. 52, 9-15
    • (1984) J. Virol. , vol.52 , pp. 9-15
    • Raden, B.1    Rutberg, L.2
  • 19
    • 0020553821 scopus 로고
    • Nucleotide sequence of a Bacillus pumilus gene specifying chloramphenical acetyltransferase
    • Harwood, C.R., Williams, D.M., and Lovett, P.S. (1983) Nucleotide sequence of a Bacillus pumilus gene specifying chloramphenical acetyltransferase. Gene 24, 163-169
    • (1983) Gene , vol.24 , pp. 163-169
    • Harwood, C.R.1    Williams, D.M.2    Lovett, P.S.3
  • 20
    • 0028826046 scopus 로고
    • TTG serves as an initiation codon for the ribosomal protein MvaS7 from the archaeon Methanococcus vannielii
    • Golderer, G., Dlaska, M., Grobner, P., and Piendl, W. (1995) TTG serves as an initiation codon for the ribosomal protein MvaS7 from the archaeon Methanococcus vannielii. J. Bacteriol. 177, 5994-5996
    • (1995) J. Bacteriol. , vol.177 , pp. 5994-5996
    • Golderer, G.1    Dlaska, M.2    Grobner, P.3    Piendl, W.4
  • 21
    • 0028338626 scopus 로고
    • Molecular characterization of an enterotoxin from Salmonella typhimurium
    • Chopra, A.K., Peterson, J.W., Chary, P., and Prasad, R. (1994) Molecular characterization of an enterotoxin from Salmonella typhimurium. Microb. Pathog. 16, 85-98
    • (1994) Microb. Pathog. , vol.16 , pp. 85-98
    • Chopra, A.K.1    Peterson, J.W.2    Chary, P.3    Prasad, R.4
  • 22
    • 0028206870 scopus 로고
    • Structure and expression of a gene coding for thermostable α-glucosidase with a broad substrate specificity from Bacillus sp. SAM1606
    • Nakao, M., Nakayama, T., Kakudo, A., Inohara, M., Harada, M., Omura, P., and Shibano, Y. (1994) Structure and expression of a gene coding for thermostable α-glucosidase with a broad substrate specificity from Bacillus sp. SAM1606. Eur. J. Biochem. 220, 293-300
    • (1994) Eur. J. Biochem. , vol.220 , pp. 293-300
    • Nakao, M.1    Nakayama, T.2    Kakudo, A.3    Inohara, M.4    Harada, M.5    Omura, P.6    Shibano, Y.7
  • 23
    • 0026459799 scopus 로고
    • Cloning, sequencing, and expression of the fadD gene of Escherichia coli encoding acyl coenzyme A synthetase
    • Black, P.N., DiRusso, C.C., Metzger, A.K., and Heimert, T.L. (1992) Cloning, sequencing, and expression of the fadD gene of Escherichia coli encoding acyl coenzyme A synthetase. J. Biol. Chem. 267, 25513-25520
    • (1992) J. Biol. Chem. , vol.267 , pp. 25513-25520
    • Black, P.N.1    DiRusso, C.C.2    Metzger, A.K.3    Heimert, T.L.4
  • 24
    • 0026690122 scopus 로고
    • Cloning, sequencing, and high expression of the proline iminopeptidase gene from Bacillus coagulans
    • Kitazono, A., Yoshimoto, T., and Tsuru, D. (1992) Cloning, sequencing, and high expression of the proline iminopeptidase gene from Bacillus coagulans. J. Bacteriol. 174, 7919-7925
    • (1992) J. Bacteriol. , vol.174 , pp. 7919-7925
    • Kitazono, A.1    Yoshimoto, T.2    Tsuru, D.3
  • 25
    • 0025778359 scopus 로고
    • Characterization of an operon encoding succinyl-CoA synthetase and malate dehydrogenase from Thermus flavus AT-62 and its expression in Escherichia coli
    • Nishiyama, M., Horinouchi, S., and Beppu, T. (1991) Characterization of an operon encoding succinyl-CoA synthetase and malate dehydrogenase from Thermus flavus AT-62 and its expression in Escherichia coli. Mol. Gen. Genet. 226, 1-9
    • (1991) Mol. Gen. Genet. , vol.226 , pp. 1-9
    • Nishiyama, M.1    Horinouchi, S.2    Beppu, T.3
  • 26
    • 0025910133 scopus 로고
    • Cloning and sequencing of a cyclodextrin glucanotransferase gene from Bacillus ohbensis and its expression in Escherichia coli
    • Sin, K., Nakamura, A., Kobayashi, K., Masaki, H., and Uozumi, T. (1991) Cloning and sequencing of a cyclodextrin glucanotransferase gene from Bacillus ohbensis and its expression in Escherichia coli. Appl. Microbiol. Biotechnol. 35, 600-605
    • (1991) Appl. Microbiol. Biotechnol. , vol.35 , pp. 600-605
    • Sin, K.1    Nakamura, A.2    Kobayashi, K.3    Masaki, H.4    Uozumi, T.5
  • 27
    • 0025831866 scopus 로고
    • The rice mitochondrial nad3 gene has an extended reading frame at its 5′ end: Nucleotide sequence analysis of rice trns, nad3, and rps12 genes
    • Suzuki, T., Kazama, S., Hirai, A., Akihama, T., and Kadowaki, K. (1991) The rice mitochondrial nad3 gene has an extended reading frame at its 5′ end: nucleotide sequence analysis of rice trnS, nad3, and rps12 genes. Curr. Genet. 20, 331-337
    • (1991) Curr. Genet. , vol.20 , pp. 331-337
    • Suzuki, T.1    Kazama, S.2    Hirai, A.3    Akihama, T.4    Kadowaki, K.5
  • 28
    • 0025369720 scopus 로고
    • Functional analysis of the 5′ regulatory region and the UUG translation initiation codon of the Arthrobacter oxidans 6-hydroxy-D-nicotine oxidase gene
    • Mauch, L., Bichler, V., and Brandsch, R. (1990) Functional analysis of the 5′ regulatory region and the UUG translation initiation codon of the Arthrobacter oxidans 6-hydroxy-D-nicotine oxidase gene. Mol. Gen. Genet. 221, 427-434
    • (1990) Mol. Gen. Genet. , vol.221 , pp. 427-434
    • Mauch, L.1    Bichler, V.2    Brandsch, R.3
  • 29
    • 0030716522 scopus 로고    scopus 로고
    • Identification of a novel conserved sequence motif in flavoprotein hydroxylases with a putative dual function in FAD/ NAD(P)H binding
    • Eppink, M.H.M., Schreuder, H.A., and Van Berkel, W.J.H. (1997) Identification of a novel conserved sequence motif in flavoprotein hydroxylases with a putative dual function in FAD/ NAD(P)H binding. Protein Sci. 6, 2454-2458
    • (1997) Protein Sci. , vol.6 , pp. 2454-2458
    • Eppink, M.H.M.1    Schreuder, H.A.2    Van Berkel, W.J.H.3


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