메뉴 건너뛰기




Volumn 269, Issue 24, 2002, Pages 6302-6307

Cloning, expression and characterization of a gene encoding nitroalkane-oxidizing enzyme from Streptomyces ansochromogenes

Author keywords

Enzymatic properties; Expression; Gene cloning; Nitroalkane oxidizing enzyme; Streptomyces

Indexed keywords

1 NITROPROPANE; 2 NITROPROPANE; AMINO ACID; BACTERIAL ENZYME; CARBONYL DERIVATIVE; NITRO DERIVATIVE; NITROALKANE; NITROBLUE TETRAZOLIUM; NITROETHANE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; UNCLASSIFIED DRUG;

EID: 0036453913     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1033.2002.03350.x     Document Type: Article
Times cited : (15)

References (39)
  • 1
    • 0003506155 scopus 로고
    • Biochemistry and pharmacology of the nitro and nitroso group
    • Feuer, H., ed. Interscience Press, New York
    • Venulet, J. & Van-Etten, R.L. (1970) Biochemistry and pharmacology of the nitro and nitroso group. In The Chemistry of the Nitro and Nitroso Groups, Part II (Feuer, H., ed.), pp. 201-287. Interscience Press, New York.
    • (1970) The Chemistry of the Nitro and Nitroso Groups, Part II , pp. 201-287
    • Venulet, J.1    Van-Etten, R.L.2
  • 2
    • 0343983913 scopus 로고
    • 3-Nitropropionate, the toxic substance of Indigofera, is a suicide inactivator of succinate dehydrogenase
    • Alston, T.A., Mela, L. & Bright, H.J. (1977) 3-Nitropropionate, the toxic substance of Indigofera, is a suicide inactivator of succinate dehydrogenase. Proc. Natl. Acad. Sci. U S A 74, 3767-3771.
    • (1977) Proc. Natl. Acad. Sci. U S A , vol.74 , pp. 3767-3771
    • Alston, T.A.1    Mela, L.2    Bright, H.J.3
  • 3
    • 85007975042 scopus 로고
    • 2-Nitropropane dioxygenase from Hansenula mrakii: Re-characterization of the enzyme and oxidation of anionic nitroalkanes
    • Kido, T., Tanizawa, K., Inagaki, K., Yoshimura, T., Ishida, M., Hashizume, K. & Soda, K. (1984) 2-Nitropropane dioxygenase from Hansenula mrakii: Re-characterization of the enzyme and oxidation of anionic nitroalkanes. Agric. Biol. Chem. 48, 2549-2554.
    • (1984) Agric. Biol. Chem. , vol.48 , pp. 2549-2554
    • Kido, T.1    Tanizawa, K.2    Inagaki, K.3    Yoshimura, T.4    Ishida, M.5    Hashizume, K.6    Soda, K.7
  • 4
    • 0017160945 scopus 로고
    • A new oxygenase, 2-nitropropane dioxygenase of Hansenula mrakii
    • Kido, T., Soda, K., Suzuki, T. & Asada, K. (1976) A new oxygenase, 2-nitropropane dioxygenase of Hansenula mrakii. J. Biol. Chem. 251, 6994-7000.
    • (1976) J. Biol. Chem. , vol.251 , pp. 6994-7000
    • Kido, T.1    Soda, K.2    Suzuki, T.3    Asada, K.4
  • 5
    • 0017179825 scopus 로고
    • Purification and properties of nitroalkane-oxidizing enzyme from Hansenula mrakii
    • Kido, T., Yamamoto, T. & Soda, K. (1976) Purification and properties of nitroalkane-oxidizing enzyme from Hansenula mrakii. J. Bacteriol. 126, 1261-1265.
    • (1976) J. Bacteriol. , vol.126 , pp. 1261-1265
    • Kido, T.1    Yamamoto, T.2    Soda, K.3
  • 6
    • 0031909037 scopus 로고    scopus 로고
    • Purification, characterization and mechanism of a flavin mononucleotide-dependent 2-nitropropane dioxygenase from Neurospora crassa
    • Gorlatova, N., Tchorzewski, M., Kurihara, T., Soda, K. & Esaki, N. (1998) Purification, characterization and mechanism of a flavin mononucleotide-dependent 2-nitropropane dioxygenase from Neurospora crassa. Appl. Environ. Microbiol. 64, 1029-1033.
    • (1998) Appl. Environ. Microbiol. , vol.64 , pp. 1029-1033
    • Gorlatova, N.1    Tchorzewski, M.2    Kurihara, T.3    Soda, K.4    Esaki, N.5
  • 7
    • 0000235360 scopus 로고
    • Oxidation of mitroethane by extracts from Neurospora crassa
    • Little, H.N. (1951) Oxidation of mitroethane by extracts from Neurospora crassa. J. Biol. Chem. 193, 347-358.
    • (1951) J. Biol. Chem. , vol.193 , pp. 347-358
    • Little, H.N.1
  • 8
    • 0017879037 scopus 로고
    • Purification and properties of nitroalkane oxidase from Fusarium oxysporum
    • Kido, T., Hashizume, K. & Soda, K. (1978) Purification and properties of nitroalkane oxidase from Fusarium oxysporum. J. Bacteriol. 133, 53-58.
    • (1978) J. Bacteriol. , vol.133 , pp. 53-58
    • Kido, T.1    Hashizume, K.2    Soda, K.3
  • 9
    • 0001370823 scopus 로고
    • Nitrification by Aspergillus flavus
    • Marshall, K.C. & Alexander, M. (1962) Nitrification by Aspergillus flavus. J. Bacteriol. 83, 572-578.
    • (1962) J. Bacteriol. , vol.83 , pp. 572-578
    • Marshall, K.C.1    Alexander, M.2
  • 10
    • 0034620511 scopus 로고    scopus 로고
    • Identification of an essential tyrosine residue in nitroalkane oxidase by modification with tetranitromethane
    • Gadda, G., Banerjee, A. & Fitzpatrick, P.F. (2000) Identification of an essential tyrosine residue in nitroalkane oxidase by modification with tetranitromethane. Biochemistry 39, 1162-1168.
    • (2000) Biochemistry , vol.39 , pp. 1162-1168
    • Gadda, G.1    Banerjee, A.2    Fitzpatrick, P.F.3
  • 11
    • 0033558778 scopus 로고    scopus 로고
    • Substrate specificity of a nitroalkane-oxidizing enzyme
    • Gadda, G. & Fitzpatrick, P.F. (1999) Substrate specificity of a nitroalkane-oxidizing enzyme. Arch. Biochem. Biophys. 363, 309-313.
    • (1999) Arch. Biochem. Biophys. , vol.363 , pp. 309-313
    • Gadda, G.1    Fitzpatrick, P.F.2
  • 12
    • 0031054970 scopus 로고    scopus 로고
    • Identification of the naturally occurring flavin of nitroalkane oxidase from Fusarium oxysporum as a 5-nitrobutyl-FAD and conversion of the enzyme to the active FAD-containing form
    • Gadda, G., Edmondson, R.D., Russell, D.H. & Fitzpatrick, P.F. (1997) Identification of the naturally occurring flavin of nitroalkane oxidase from Fusarium oxysporum as a 5-nitrobutyl-FAD and conversion of the enzyme to the active FAD-containing form. J. Biol. Chem. 272, 5563-5570.
    • (1997) J. Biol. Chem. , vol.272 , pp. 5563-5570
    • Gadda, G.1    Edmondson, R.D.2    Russell, D.H.3    Fitzpatrick, P.F.4
  • 13
    • 0032574753 scopus 로고    scopus 로고
    • Biochemical and physical characterization of the active FAD-containing form of nitroalkane oxidase from Fusarium oxysporum
    • Gadda, G. & Fitzpatrick, P.F. (1998) Biochemical and physical characterization of the active FAD-containing form of nitroalkane oxidase from Fusarium oxysporum. Biochemistry 37, 6154-6164.
    • (1998) Biochemistry , vol.37 , pp. 6154-6164
    • Gadda, G.1    Fitzpatrick, P.F.2
  • 14
    • 0028584335 scopus 로고
    • Unique primary structure of 2-nitropropane dioxygenase from Hansenula mrakii
    • Tchorzewski, M., Kurihara, T., Esaki, N. & Soda, K. (1994) Unique primary structure of 2-nitropropane dioxygenase from Hansenula mrakii. Eur. J. Biochem. 226, 841-846.
    • (1994) Eur. J. Biochem. , vol.226 , pp. 841-846
    • Tchorzewski, M.1    Kurihara, T.2    Esaki, N.3    Soda, K.4
  • 15
    • 0037022634 scopus 로고    scopus 로고
    • Cloning of nitroalkane oxidase from Fusarium oxysporum identifies a new member of the acyl-CoA dehydrogenase superfamily
    • Daubner, S.C., Gadda, G., Valley, M.P. & Fitzpatrick, P.F. (2002) Cloning of nitroalkane oxidase from Fusarium oxysporum identifies a new member of the acyl-CoA dehydrogenase superfamily. Proc. Natl. Acad. Sci. USA 99, 2702-2707.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 2702-2707
    • Daubner, S.C.1    Gadda, G.2    Valley, M.P.3    Fitzpatrick, P.F.4
  • 16
    • 0018340378 scopus 로고
    • Nitroalkanes oxidase in Streptomyces
    • Dhawale, M.R. & Hornemann, U. (1979) Nitroalkanes oxidase in Streptomyces. J. Bacteriol. 137, 916-924.
    • (1979) J. Bacteriol. , vol.137 , pp. 916-924
    • Dhawale, M.R.1    Hornemann, U.2
  • 17
    • 0027399382 scopus 로고
    • Two developmentally controlled promoters of Streptomyces coelicolor A3 (2) that resemble the major class of motility-related promoters in other bacteria
    • Tan, H. & Chater, K.F. (1993) Two developmentally controlled promoters of Streptomyces coelicolor A3 (2) that resemble the major class of motility-related promoters in other bacteria. J. Bacteriol. 175, 933.
    • (1993) J. Bacteriol. , vol.175 , pp. 933
    • Tan, H.1    Chater, K.F.2
  • 19
    • 0036189237 scopus 로고    scopus 로고
    • A novel Streptomyces gene, samR, with different effects on differentiation of Streptomyces ansochromogenes and Streptomyces coelicolor
    • Tan, H., Tian, Y., Yang, H., Liu, G. & Nie, L. (2002) A novel Streptomyces gene, samR, with different effects on differentiation of Streptomyces ansochromogenes and Streptomyces coelicolor. Arch. Microbiol. 177, 274-278.
    • (2002) Arch. Microbiol. , vol.177 , pp. 274-278
    • Tan, H.1    Tian, Y.2    Yang, H.3    Liu, G.4    Nie, L.5
  • 20
    • 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
  • 21
    • 0023634094 scopus 로고
    • Production of single-stranded plasmid
    • Vieira, J. & Messing, J. (1987) Production of single-stranded plasmid. Methods Enzymol. 153, 3-11.
    • (1987) Methods Enzymol. , vol.153 , pp. 3-11
    • Vieira, J.1    Messing, J.2
  • 24
    • 0021253525 scopus 로고
    • Undirectional digestion with exonuclease III creates targeted breakpoints for DNA sequencing
    • Henikoff, S. (1984) Undirectional digestion with exonuclease III creates targeted breakpoints for DNA sequencing. Gene 28, 351-359.
    • (1984) Gene , vol.28 , pp. 351-359
    • Henikoff, S.1
  • 25
    • 0021710537 scopus 로고
    • The relationship between base composition and codon usage in bacterial genes and its use in the simple and reliable identification of protein coding sequences
    • Bibb, M.J., Findlay, P.R. & Johnson, M.W. (1984) The relationship between base composition and codon usage in bacterial genes and its use in 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
  • 27
    • 0003320378 scopus 로고
    • The biuret reaction for the determination of protein: An improved reagent and its application
    • Levin, R. & Brauer, R.W. (1951) The biuret reaction for the determination of protein: An improved reagent and its application. J. Lab. Clin. Med. 38, 474.
    • (1951) J. Lab. Clin. Med. , vol.38 , pp. 474
    • Levin, R.1    Brauer, R.W.2
  • 28
    • 85182615928 scopus 로고
    • Nitroethane oxidase
    • Little. H.N. (1955) Nitroethane oxidase. Methods Enzymol. 2, 401-402.
    • (1955) Methods Enzymol. , vol.2 , pp. 401-402
    • Little, H.N.1
  • 30
    • 0001552687 scopus 로고
    • A spectrophotometric microdetermination of keto acids with 3-methyl-2-benzothiazolone hydrazone
    • Soda, K. (1967) A spectrophotometric microdetermination of keto acids with 3-methyl-2-benzothiazolone hydrazone. Agric. Biol. Chem. 31, 1054-1060.
    • (1967) Agric. Biol. Chem. , vol.31 , pp. 1054-1060
    • Soda, K.1
  • 31
    • 0000242975 scopus 로고
    • Purification and general properties of spinach leaf nitrite reductase
    • Ida, S. & Morita, Y. (1973) Purification and general properties of spinach leaf nitrite reductase. Plant Cell Physiol. 14, 661-671.
    • (1973) Plant Cell Physiol. , vol.14 , pp. 661-671
    • Ida, S.1    Morita, Y.2
  • 33
    • 0030035418 scopus 로고    scopus 로고
    • A set of ordered cosmids and a detailed genetic and physical map for the 8 Mb Streptomyces coelicolor A3 (2) chromosome
    • Redenbach, M., Kieser, H.M., Denapaite, D., Eichner, A., Cullum, J., Kinashi, H. & Hopwood, D.A. (1996) A set of ordered cosmids and a detailed genetic and physical map for the 8 Mb Streptomyces coelicolor A3 (2) chromosome. Mol. Microbiol. 21, 77-96.
    • (1996) Mol. Microbiol. , vol.21 , pp. 77-96
    • Redenbach, M.1    Kieser, H.M.2    Denapaite, D.3    Eichner, A.4    Cullum, J.5    Kinashi, H.6    Hopwood, D.A.7
  • 35
    • 0023041821 scopus 로고
    • Prediction of the ADP-binding beta-alpha-beta-fold in proteins, using an amino-acid sequence fingerprint
    • Wierenga, R.K., Terpstra, P. & Hol, W.G. (1986) Prediction of the ADP-binding beta-alpha-beta-fold in proteins, using an aminoacid 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.3
  • 36
    • 0018264498 scopus 로고
    • Properties of 2-nitropropane dioxygenase of Hansenula mrakii
    • Kido, T., Soda, K. & Asada, K. (1978) Properties of 2-nitropropane dioxygenase of Hansenula mrakii. J. Biol. Chem. 253, 226-232.
    • (1978) J. Biol. Chem. , vol.253 , pp. 226-232
    • Kido, T.1    Soda, K.2    Asada, K.3
  • 37
    • 0022504847 scopus 로고
    • Free-radical chain oxidation of 2-nitropropane initiated and propagated by superoxide
    • Kuo, C.F. & Fridovich, I. (1986) Free-radical chain oxidation of 2-nitropropane initiated and propagated by superoxide. Biochem. J. 237, 505-510.
    • (1986) Biochem. J. , vol.237 , pp. 505-510
    • Kuo, C.F.1    Fridovich, I.2
  • 38
    • 0034644665 scopus 로고    scopus 로고
    • Identification of a cysteine residue in the active site of nitroalkane oxidase by modification with N-ethylmaleimide
    • Gadda, G., Banerjee, A., Dangott, L.J. & Fitzpatrick, P.F. (2000) Identification of a cysteine residue in the active site of nitroalkane oxidase by modification with N-ethylmaleimide. J. Biol. Chem. 275, 31891-31895.
    • (2000) J. Biol. Chem. , vol.275 , pp. 31891-31895
    • Gadda, G.1    Banerjee, A.2    Dangott, L.J.3    Fitzpatrick, P.F.4
  • 39
    • 0024455022 scopus 로고
    • Oxidative DNA and RNA damage in the livers of Sprague-Dawley rats treated with the hepatocarcinogen 2-nitropropane
    • Fiala, E.S., Conaway, C.C. & Mathis, J.E. (1989) Oxidative DNA and RNA damage in the livers of Sprague-Dawley rats treated with the hepatocarcinogen 2-nitropropane. Cancer Res. 49, 5518-5522.
    • (1989) Cancer Res. , vol.49 , pp. 5518-5522
    • Fiala, E.S.1    Conaway, C.C.2    Mathis, J.E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.