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Volumn 21, Issue 4, 2010, Pages 593-602

Cloning, expression and functional analysis of nicotinate dehydrogenase gene cluster from Comamonas testosteroni JA1 that can hydroxylate 3-cyanopyridine

Author keywords

3 Cyano 6 hydrxoypyridine; 3 Cyanopyridine; 6 Hydroxynicotinic acid; Comamonas testosteroni; Nicotinate dehydrogenase (NaDH); Nicotinic acid

Indexed keywords

3-CYANOPYRIDINE; 6-HYDROXYNICOTINIC ACID; AMINO ACID SEQUENCE; COMAMONAS TESTOSTERONI; CYTOCHROME C; GENE CLUSTERS; NICOTINIC ACID; SEQUENCE ALIGNMENTS; SMALL SUBUNITS; SUBSTRATE SPECIFICITY; TYPE II;

EID: 77952958648     PISSN: 09239820     EISSN: None     Source Type: Journal    
DOI: 10.1007/s10532-010-9327-2     Document Type: Article
Times cited : (17)

References (35)
  • 2
    • 0036359682 scopus 로고    scopus 로고
    • The molybdenum-containing hydroxylases of nicotinate, isonicotinate, and nicotine
    • Andreesen JR, Fetzner S (2002) The molybdenum-containing hydroxylases of nicotinate, isonicotinate, and nicotine. Met Ions Biol Syst 39: 405-430.
    • (2002) Met Ions Biol Syst , vol.39 , pp. 405-430
    • Andreesen, J.R.1    Fetzner, S.2
  • 3
    • 23144441840 scopus 로고
    • The bacterial oxidation of nicotinic acid
    • Behrman EJ, Stanier RY (1957) The bacterial oxidation of nicotinic acid. J Biol Chem 228: 923-945.
    • (1957) J Biol Chem , vol.228 , pp. 923-945
    • Behrman, E.J.1    Stanier, R.Y.2
  • 4
    • 0023100333 scopus 로고
    • Microbial metabolism of homocyclic and heterocyclic aromatic compounds under anaerobic conditions
    • Berry DF, Francis AJ, Bollag JM (1987) Microbial metabolism of homocyclic and heterocyclic aromatic compounds under anaerobic conditions. Microbiol Rev 51: 43-59.
    • (1987) Microbiol Rev , vol.51 , pp. 43-59
    • Berry, D.F.1    Francis, A.J.2    Bollag, J.M.3
  • 5
    • 0030942268 scopus 로고    scopus 로고
    • Construction and use of a versatile set of broad-host-range cloning and expression vectors based on the RK2 replicon
    • Blatny JM, Brautaset T, Winther-Larsen HC, Haugan K, Valla S (1997a) Construction and use of a versatile set of broad-host-range cloning and expression vectors based on the RK2 replicon. Appl Environ Microbiol 63: 370-379.
    • (1997) Appl Environ Microbiol , vol.63 , pp. 370-379
    • Blatny, J.M.1    Brautaset, T.2    Winther-Larsen, H.C.3    Haugan, K.4    Valla, S.5
  • 6
    • 0030819591 scopus 로고    scopus 로고
    • Improved broad-host-range RK2 vectors useful for high and low regulated gene expression levels in gram-negative bacteria
    • Blatny JM, Brautaset T, Winther-Larsen HC, Karunakaran P, Valla S (1997b) Improved broad-host-range RK2 vectors useful for high and low regulated gene expression levels in gram-negative bacteria. Plasmid 38: 35-51.
    • (1997) Plasmid , vol.38 , pp. 35-51
    • Blatny, J.M.1    Brautaset, T.2    Winther-Larsen, H.C.3    Karunakaran, P.4    Valla, S.5
  • 7
    • 4143136285 scopus 로고    scopus 로고
    • Active site geometry and substrate recognition of the molybdenum hydroxylase quinoline 2-oxidoreductase
    • Bonin I, Martins BM, Purvanov V, Fetzner S, Huber R, Dobbek H (2004) Active site geometry and substrate recognition of the molybdenum hydroxylase quinoline 2-oxidoreductase. Structure 12: 1425-1435.
    • (2004) Structure , vol.12 , pp. 1425-1435
    • Bonin, I.1    Martins, B.M.2    Purvanov, V.3    Fetzner, S.4    Huber, R.5    Dobbek, H.6
  • 9
    • 0029006062 scopus 로고
    • The multiplicity of domains in proteins
    • Doolittle RF (1995) The multiplicity of domains in proteins. Annu Rev Biochem 64: 287-314.
    • (1995) Annu Rev Biochem , vol.64 , pp. 287-314
    • Doolittle, R.F.1
  • 10
    • 0023948010 scopus 로고
    • High efficiency transformation of E. coli by high voltage electroporation
    • Dower WJ, Miller JF, Ragsdale CW (1988) High efficiency transformation of E. coli by high voltage electroporation. Nucleic Acids Res 16: 6127-6145.
    • (1988) Nucleic Acids Res , vol.16 , pp. 6127-6145
    • Dower, W.J.1    Miller, J.F.2    Ragsdale, C.W.3
  • 11
    • 0000047252 scopus 로고
    • The pathway of nicotinic acid oxidation by a Bacillus species
    • Ensign JC, Rittenberg SC (1964) The pathway of nicotinic acid oxidation by a Bacillus species. J Biol Chem 239: 2285-2291.
    • (1964) J Biol Chem , vol.239 , pp. 2285-2291
    • Ensign, J.C.1    Rittenberg, S.C.2
  • 12
    • 0028021488 scopus 로고
    • Structural analysis and molybdenum-dependent expression of the pAO1-encoded nicotine dehydrogenase genes of Arthrobacter nicotinovorans
    • Grether-Beck S, Igloi GL, Pust S, Schilz E, Decker K, Brandsch R (1994) Structural analysis and molybdenum-dependent expression of the pAO1-encoded nicotine dehydrogenase genes of Arthrobacter nicotinovorans. Mol Microbiol 13: 929-936.
    • (1994) Mol Microbiol , vol.13 , pp. 929-936
    • Grether-Beck, S.1    Igloi, G.L.2    Pust, S.3    Schilz, E.4    Decker, K.5    Brandsch, R.6
  • 13
    • 0013652168 scopus 로고
    • Bacterial fermantation of nicotinic acid. II. Anaerobic reversible hydroxylation of nicotinic acid to 6-hydroxynicotinic acid
    • Harary I (1957) Bacterial fermantation of nicotinic acid. II. Anaerobic reversible hydroxylation of nicotinic acid to 6-hydroxynicotinic acid. J Biol Chem 227: 823-831.
    • (1957) J Biol Chem , vol.227 , pp. 823-831
    • Harary, I.1
  • 14
    • 0001391442 scopus 로고
    • 6-Hydroxynicotinic acid as an intermediate in the oxidation of nicotinic acid by Pseudomonas fluorescens
    • Hughes DE (1955) 6-Hydroxynicotinic acid as an intermediate in the oxidation of nicotinic acid by Pseudomonas fluorescens. Biochem J 60: 303-310.
    • (1955) Biochem J , vol.60 , pp. 303-310
    • Hughes, D.E.1
  • 15
    • 0013649022 scopus 로고
    • Purification of the nicotinic acid hydroxylase system of Pseudomonas fluorescens KB1
    • Hunt AL (1959) Purification of the nicotinic acid hydroxylase system of Pseudomonas fluorescens KB1. Biochem J 72: 1-7.
    • (1959) Biochem J , vol.72 , pp. 1-7
    • Hunt, A.L.1
  • 16
    • 0008808912 scopus 로고
    • The hydroxylation of nicotinic acid by Pseudomonas fluorescens
    • Hunt AL, Hughes DE, Lowenstein JM (1958) The hydroxylation of nicotinic acid by Pseudomonas fluorescens. Biochem J 69: 170-173.
    • (1958) Biochem J , vol.69 , pp. 170-173
    • Hunt, A.L.1    Hughes, D.E.2    Lowenstein, J.M.3
  • 17
    • 0028228752 scopus 로고
    • Microbial production of 6-hydroxynicotinic acid, an important building block for the synthesis of modern insecticides
    • Hurh B, Ohshima M, Yamane T, Nagasawa T (1994a) Microbial production of 6-hydroxynicotinic acid, an important building block for the synthesis of modern insecticides. J Ferment Bioeng 77: 382-385.
    • (1994) J Ferment Bioeng , vol.77 , pp. 382-385
    • Hurh, B.1    Ohshima, M.2    Yamane, T.3    Nagasawa, T.4
  • 18
    • 0028133247 scopus 로고
    • Purification and characterization of nicotinic acid dehydrogenase from Pseudomonas fluoescens TN5
    • Hurh B, Yamane T, Nagasawa T (1994b) Purification and characterization of nicotinic acid dehydrogenase from Pseudomonas fluoescens TN5. Ferment Bioeng 78: 19-26.
    • (1994) Ferment Bioeng , vol.78 , pp. 19-26
    • Hurh, B.1    Yamane, T.2    Nagasawa, T.3
  • 21
    • 0015883076 scopus 로고
    • Cytochrome c linked nicotinic acid hydroxylase in Pseudomonas ovalis Chester
    • Jones MV (1973) Cytochrome c linked nicotinic acid hydroxylase in Pseudomonas ovalis Chester. FEBS Lett 32: 321-324.
    • (1973) FEBS Lett , vol.32 , pp. 321-324
    • Jones, M.V.1
  • 22
    • 0015390202 scopus 로고
    • The oxidation of nicotinic acid by Pseudomonas ovalis Chester. The terminal oxidase
    • Jones MV, Hughes DE (1972) The oxidation of nicotinic acid by Pseudomonas ovalis Chester. The terminal oxidase. Biochem J 129: 755-761.
    • (1972) Biochem J , vol.129 , pp. 755-761
    • Jones, M.V.1    Hughes, D.E.2
  • 23
    • 0030906745 scopus 로고    scopus 로고
    • Molybdenum-cofactor-containing enzymes: Structure and mechanism
    • Kisker C, Schindelin H, Rees DC (1997) Molybdenum-cofactor-containing enzymes: structure and mechanism. Annu Rev Biochem 66: 233-267.
    • (1997) Annu Rev Biochem , vol.66 , pp. 233-267
    • Kisker, C.1    Schindelin, H.2    Rees, D.C.3
  • 24
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 25
    • 66049154270 scopus 로고    scopus 로고
    • Induction of nicotinic acid hydroxylase activity of Pseudomonas putida NA-1 and optimization of transformation conditions
    • Lu WH, Wang X, Xu L, Dai YJ, Yuan S (2005) Induction of nicotinic acid hydroxylase activity of Pseudomonas putida NA-1 and optimization of transformation conditions. Acta Microbiologica Sinica 45: 6-9.
    • (2005) Acta Microbiologica Sinica , vol.45 , pp. 6-9
    • Lu, W.H.1    Wang, X.2    Xu, L.3    Dai, Y.J.4    Yuan, S.5
  • 26
    • 0037050267 scopus 로고    scopus 로고
    • Cloning and characterization of a glycosyltransferase gene involved in the biosynthesis of anthracycline antibiotic beta-rhodomycin from Streptomyces violaceus
    • Miyamoto Y, Johdo O, Nagamatsu Y, Yoshimoto A (2002) Cloning and characterization of a glycosyltransferase gene involved in the biosynthesis of anthracycline antibiotic beta-rhodomycin from Streptomyces violaceus. FEMS Microbiol Lett 206: 163-168.
    • (2002) FEMS Microbiol Lett , vol.206 , pp. 163-168
    • Miyamoto, Y.1    Johdo, O.2    Nagamatsu, Y.3    Yoshimoto, A.4
  • 27
    • 0000430120 scopus 로고
    • Molybdenum-dependent degradation of nicotinic acid by Bacillus sp. DSM 2923
    • Nagel M, Andreesen JR (1989) Molybdenum-dependent degradation of nicotinic acid by Bacillus sp. DSM 2923. FEMS Microbiol Lett 59: 147-152.
    • (1989) FEMS Microbiol Lett , vol.59 , pp. 147-152
    • Nagel, M.1    Andreesen, J.R.2
  • 30
    • 0020787415 scopus 로고
    • An optimized freeze-squeeze method for the recovery of DNA fragments from agarose gels
    • Tautz D, Renz M (1983) An optimized freeze-squeeze method for the recovery of DNA fragments from agarose gels. Anal Biochem 132: 14-19.
    • (1983) Anal Biochem , vol.132 , pp. 14-19
    • Tautz, D.1    Renz, M.2
  • 32
    • 67349222936 scopus 로고    scopus 로고
    • Cloning, heterologous expression, and functional characterization of the nicotinate dehydrogenase gene from Pseudomonas putida KT2440
    • Yang Y, Yuan S, Chen T, Ma PJ, Shang GD, Dai YJ (2009) Cloning, heterologous expression, and functional characterization of the nicotinate dehydrogenase gene from Pseudomonas putida KT2440. Biodegradation 20: 541-549.
    • (2009) Biodegradation , vol.20 , pp. 541-549
    • Yang, Y.1    Yuan, S.2    Chen, T.3    Ma, P.J.4    Shang, G.D.5    Dai, Y.J.6
  • 33
    • 0021943518 scopus 로고
    • Improved M13 phage cloning vectors and host strains: Nucleotide sequences of the M13mp18 and pUC19 vectors
    • Yanisch-Perron C, Vieira J, Messing J (1985) Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mp18 and pUC19 vectors. Gene 33: 103-119.
    • (1985) Gene , vol.33 , pp. 103-119
    • Yanisch-Perron, C.1    Vieira, J.2    Messing, J.3
  • 35
    • 25444485763 scopus 로고    scopus 로고
    • A combined technology of growing culture hydroxylation of nicotinic acid and resting cells hydroxylation of 3-cyanopyridine by Comamonas testosterone JA1
    • Yuan S, Yang Y, Sun J, Dai YJ (2005) A combined technology of growing culture hydroxylation of nicotinic acid and resting cells hydroxylation of 3-cyanopyridine by Comamonas testosterone JA1. Eng Life Sci 5: 369-374.
    • (2005) Eng Life Sci , vol.5 , pp. 369-374
    • Yuan, S.1    Yang, Y.2    Sun, J.3    Dai, Y.J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.