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Volumn 28, Issue 1, 2003, Pages 131-139

High-level expression of a novel FMN-dependent heme-containing lyase, phenylacetaldoxime dehydratase of Bacillus sp. strain OxB-1, in heterologous hosts

Author keywords

[No Author keywords available]

Indexed keywords

BACILLUS SP.; BACILLUS SUBTILIS; ESCHERICHIA COLI;

EID: 0037361443     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1046-5928(02)00638-1     Document Type: Article
Times cited : (27)

References (28)
  • 2
    • 0032518677 scopus 로고    scopus 로고
    • Z-Phenylacetaldoxime degradation by a novel aldoxime dehydratase from Bacillus sp. strain OxB-1
    • Y. Asano, Y. Kato, Z-Phenylacetaldoxime degradation by a novel aldoxime dehydratase from Bacillus sp. strain OxB-1, FEMS Microbiol. Lett. 158 (1998) 185-190.
    • (1998) FEMS Microbiol. Lett. , vol.158 , pp. 185-190
    • Asano, Y.1    Kato, Y.2
  • 3
    • 0031866847 scopus 로고    scopus 로고
    • Isolation and characterization of a bacterium possessing a novel aldoxime-dehydration activity and nitrile-degrading enzymes
    • Y. Kato, R. Ooi, Y. Asano, Isolation and characterization of a bacterium possessing a novel aldoxime-dehydration activity and nitrile-degrading enzymes, Arch. Microbiol. 170 (1998) 85-90.
    • (1998) Arch. Microbiol. , vol.170 , pp. 85-90
    • Kato, Y.1    Ooi, R.2    Asano, Y.3
  • 4
    • 0037075689 scopus 로고    scopus 로고
    • Overview of screening for new microbial catalysts and their uses in organic synthesis - Selection and optimization of biocatalysts
    • Y. Asano, Overview of screening for new microbial catalysts and their uses in organic synthesis - selection and optimization of biocatalysts, J. Biotech. 94 (2002) 65-72.
    • (2002) J. Biotech. , vol.94 , pp. 65-72
    • Asano, Y.1
  • 5
    • 0033545557 scopus 로고    scopus 로고
    • A new enzymatic method of nitrile synthesis by Rhodococcus sp. strain YH3-3
    • Y. Kato, R. Ooi, Y. Asano, A new enzymatic method of nitrile synthesis by Rhodococcus sp. strain YH3-3, J. Mol. Catal. B: Enzymatic 6 (1999) 249-256.
    • (1999) J. Mol. Catal. B: Enzymatic , vol.6 , pp. 249-256
    • Kato, Y.1    Ooi, R.2    Asano, Y.3
  • 6
    • 0035757148 scopus 로고    scopus 로고
    • High yield synthesis of nitriles by a new enzyme phenylacetaldoxime dehydratase from Bacillus sp. strain OxB-1
    • S.-X. Xie, Y. Kato, Y. Asano, High yield synthesis of nitriles by a new enzyme phenylacetaldoxime dehydratase from Bacillus sp. strain OxB-1, Biosci. Biotechnol. Biochem. 65 (2001) 2666-2672.
    • (2001) Biosci. Biotechnol. Biochem. , vol.65 , pp. 2666-2672
    • Xie, S.-X.1    Kato, Y.2    Asano, Y.3
  • 7
    • 0034142390 scopus 로고    scopus 로고
    • A novel heme-containing lyase, phenylacetaldoxime dehydratase from Bacillus sp. strain OxB-1: Purification, characterization, and molecular cloning of the gene
    • Y. Kato, K. Nakamura, H. Sakiyama, S.G. Mayhew, Y. Asano, A novel heme-containing lyase, phenylacetaldoxime dehydratase from Bacillus sp. strain OxB-1: purification, characterization, and molecular cloning of the gene, Biochemistry 39 (2000) 800-809.
    • (2000) Biochemistry , vol.39 , pp. 800-809
    • Kato, Y.1    Nakamura, K.2    Sakiyama, H.3    Mayhew, S.G.4    Asano, Y.5
  • 8
    • 0039466853 scopus 로고    scopus 로고
    • Nitrile hydratase involved in aldoxime metabolism from Rhodococcus sp. strain YH3-3 - Purification and characterization
    • Y. Kato, T. Tsuda, Y. Asano, Nitrile hydratase involved in aldoxime metabolism from Rhodococcus sp. strain YH3-3 - purification and characterization, Eur. J. Biochem. 263 (1999) 662-670.
    • (1999) Eur. J. Biochem. , vol.263 , pp. 662-670
    • Kato, Y.1    Tsuda, T.2    Asano, Y.3
  • 9
    • 0342803567 scopus 로고    scopus 로고
    • Distribution of aldoxime dehydratase in microorganisms
    • Y. Kato, R. Ooi, Y. Asano, Distribution of aldoxime dehydratase in microorganisms, Appl. Environ. Microbiol. 66 (2000) 2290-2296.
    • (2000) Appl. Environ. Microbiol. , vol.66 , pp. 2290-2296
    • Kato, Y.1    Ooi, R.2    Asano, Y.3
  • 10
    • 0027405142 scopus 로고
    • Overproduction, purification and characterization of the bacterioferrin of Escherichia coli and a C-terminally extended variant
    • S.C. Andrews, J.M.A. Smith, C. Hawkins, J.M. Williams, P.M. Harrison, J.R. Guest, Overproduction, purification and characterization of the bacterioferrin of Escherichia coli and a C-terminally extended variant, Eur. J. Biochem 213 (1993) 329-338.
    • (1993) Eur. J. Biochem. , vol.213 , pp. 329-338
    • Andrews, S.C.1    Smith, J.M.A.2    Hawkins, C.3    Williams, J.M.4    Harrison, P.M.5    Guest, J.R.6
  • 11
    • 0028001350 scopus 로고
    • The high-level expression in Escherichia coli of the membrane-bound form of human and rat cytochrome b5 and studies on their mechanism of function
    • R.L. Holmans, M.S. Shet, C.A. Martin-Wixtrom, C.W. Fisher, R.W. Estabrook, The high-level expression in Escherichia coli of the membrane-bound form of human and rat cytochrome b5 and studies on their mechanism of function. Arch. Biochem. Biophys. 312 (1994) 554-565.
    • (1994) Arch. Biochem. Biophys. , vol.312 , pp. 554-565
    • Holmans, R.L.1    Shet, M.S.2    Martin-Wixtrom, C.A.3    Fisher, C.W.4    Estabrook, R.W.5
  • 12
    • 78651153791 scopus 로고
    • Disk electrophoresis-II. Method and application to human serum proteins
    • B.J. Davis, Disk electrophoresis-II. Method and application to human serum proteins, Ann. N. Y. Acad. Sci. 121 (Part 2) (1964) 404-406.
    • (1964) Ann. N. Y. Acad. Sci. , vol.121 , Issue.PART 2 , pp. 404-406
    • Davis, B.J.1
  • 13
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • U.K. Laemmli, Cleavage of structural proteins during the assembly of the head of bacteriophage T4, Nature (London) 227 (1970) 680-685.
    • (1970) Nature (London) , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 14
    • 0021825108 scopus 로고
    • New shuttle vector for Escherichia coli and Bacillus subtilis. II. Plasmid pHY300PLK, a multipurpose cloning vector with a polylinker, derived from pHY460
    • H. Ishiwa, H. Shibahara, New shuttle vector for Escherichia coli and Bacillus subtilis. II. Plasmid pHY300PLK, a multipurpose cloning vector with a polylinker, derived from pHY460, Jpn. J. Genet. 60 (1985) 235-243.
    • (1985) Jpn. J. Genet. , vol.60 , pp. 235-243
    • Ishiwa, H.1    Shibahara, H.2
  • 15
    • 0019467387 scopus 로고
    • Chromosomal loci of genes controlling site-specific restriction endonucleases of Bacillus subtilis
    • S. Ikawa, T. Shibata, K. Matsumoto, T. Iijima, Chromosomal loci of genes controlling site-specific restriction endonucleases of Bacillus subtilis, Mol. Gen. Genet. 183 (1981) 1-6.
    • (1981) Mol. Gen. Genet. , vol.183 , pp. 1-6
    • Ikawa, S.1    Shibata, T.2    Matsumoto, K.3    Iijima, T.4
  • 16
    • 0020687257 scopus 로고
    • Formation of competent Bacillus subtilis cells
    • Y. Sadaie, T. Kada, Formation of competent Bacillus subtilis cells, J. Bacteriol. 153 (1983) 813-821.
    • (1983) J. Bacteriol. , vol.153 , pp. 813-821
    • Sadaie, Y.1    Kada, T.2
  • 18
    • 0026690122 scopus 로고
    • Cloning, sequencing, and high expression of the proline iminopeptidase gene from Bacillus coagulans
    • A. Kitazono, T. Yoshimoto, D. Tsuru, Cloning, sequencing, and high expression of the proline iminopeptidase gene from Bacillus coagulans, J. Bacteriol. 174 (1992) 7919-7925.
    • (1992) J. Bacteriol. , vol.174 , pp. 7919-7925
    • Kitazono, A.1    Yoshimoto, T.2    Tsuru, D.3
  • 19
    • 0025910133 scopus 로고
    • Cloning and sequencing of a cyclodextrin glucanotransferase gene from Bacillus ohbensis and its expression in Escherichia coli
    • K.-A. Sin, A. Nakamura, K. Kobayashi, H. Masaki, T. Uozumi, Cloning and sequencing of a cyclodextrin glucanotransferase gene from Bacillus ohbensis and its expression in Escherichia coli, Appl. Microbiol. Biotechnol. 35 (1991) 600-605.
    • (1991) Appl. Microbiol. Biotechnol. , vol.35 , pp. 600-605
    • Sin, K.-A.1    Nakamura, A.2    Kobayashi, K.3    Masaki, H.4    Uozumi, T.5
  • 20
    • 0028245069 scopus 로고
    • Expression of recombinant human hemoglobin in Escherichia coli
    • D. Looker, A.J. Mathews, J.O. Neway, G.L. Stetler, Expression of recombinant human hemoglobin in Escherichia coli, Methods Enzymol. 231 (1994) 364-374.
    • (1994) Methods Enzymol. , vol.231 , pp. 364-374
    • Looker, D.1    Mathews, A.J.2    Neway, J.O.3    Stetler, G.L.4
  • 21
    • 0001794011 scopus 로고
    • The biosynthesis of 5-aminolaevulinic acid and its transformation into uroprophyrinogen III
    • P.M. Jordan (Ed.), Elsevier, Amsterdam
    • P.M. Jordan, The biosynthesis of 5-aminolaevulinic acid and its transformation into uroprophyrinogen III, in: P.M. Jordan (Ed.), Biosynthesis of Tetrapyrroles, Elsevier, Amsterdam, 1991, pp. 1-43.
    • (1991) Biosynthesis of Tetrapyrroles , pp. 1-43
    • Jordan, P.M.1
  • 22
    • 0035091505 scopus 로고    scopus 로고
    • High-level production of heme-containing holoproteins in Escherichia coli
    • Y. Jung, J. Kwak, Y. Lee, High-level production of heme-containing holoproteins in Escherichia coli, Appl. Microbiol. Biotechnol. 55 (2001) 187-191.
    • (2001) Appl. Microbiol. Biotechnol. , vol.55 , pp. 187-191
    • Jung, Y.1    Kwak, J.2    Lee, Y.3
  • 23
    • 0018079850 scopus 로고
    • Stimulation of tetrapyrrole formation in Rhizobium japonicum by restricted aeration
    • Y.J. Avissar, K.D. Nadler, Stimulation of tetrapyrrole formation in Rhizobium japonicum by restricted aeration, J. Bacteriol. 135 (1978) 782-789.
    • (1978) J. Bacteriol. , vol.135 , pp. 782-789
    • Avissar, Y.J.1    Nadler, K.D.2
  • 24
    • 0031738218 scopus 로고    scopus 로고
    • Cloning, nucleotide sequencing, and expression of 3-methylaspartate ammonia lyase gene from Citrobacter amalonaticus strain YG-1002
    • Y. Kato, Y. Asano, Cloning, nucleotide sequencing, and expression of 3-methylaspartate ammonia lyase gene from Citrobacter amalonaticus strain YG-1002, Appl. Microbiol. Biotechnol. 50 (1998) 474-486.
    • (1998) Appl. Microbiol. Biotechnol. , vol.50 , pp. 474-486
    • Kato, Y.1    Asano, Y.2
  • 25
    • 0029123307 scopus 로고
    • Cloning, nucleotide sequencing and expression of opine dehydrogenase gene from Arthrobacter sp. strain 1C
    • T. Dairi, Y. Asano, Cloning, nucleotide sequencing and expression of opine dehydrogenase gene from Arthrobacter sp. strain 1C, Appl. Environ. Microbiol. 61 (1995) 3171-3196.
    • (1995) Appl. Environ. Microbiol. , vol.61 , pp. 3171-3196
    • Dairi, T.1    Asano, Y.2
  • 26
    • 0034067403 scopus 로고    scopus 로고
    • Gene cloning, nucleotide sequencing, and purification and characterization of the D-stereospecific amino acid amidase from Ochrobactrum anthropi SV3
    • H. Komeda, Y. Asano, Gene cloning, nucleotide sequencing, and purification and characterization of the D-stereospecific amino acid amidase from Ochrobactrum anthropi SV3, Eur. J. Biochem. 267 (2000) 2028-2036.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 2028-2036
    • Komeda, H.1    Asano, Y.2
  • 27
    • 0034799234 scopus 로고    scopus 로고
    • Novel hemoglobins to enhance microaerobic growth and substrate utilization in Escherichia coli
    • C.J.T. Bollinger, J.E. Bailey, P.T. Kallio, Novel hemoglobins to enhance microaerobic growth and substrate utilization in Escherichia coli, Biotechnol. Prog. 17 (2001) 798-808.
    • (2001) Biotechnol. Prog. , vol.17 , pp. 798-808
    • Bollinger, C.J.T.1    Bailey, J.E.2    Kallio, P.T.3


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