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Volumn 78, Issue 8-9, 1996, Pages 792-799

Two isozymes of P450nor of Cylindrocarpon tonkinense: Molecular cloning of the cDNAs and genes, expressions in the yeast, and the putative NAD(P)H-binding site

Author keywords

Cylindrocarpon tonkinense; Cytochrome P450nor; Nitric oxide reductase; P450nor

Indexed keywords

CHIMERIC PROTEIN; COMPLEMENTARY DNA; CYTOCHROME P450 ISOENZYME; FUNGAL DNA; FUNGAL PROTEIN; RECOMBINANT PROTEIN; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE;

EID: 0030458981     PISSN: 03009084     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0300-9084(97)82538-2     Document Type: Article
Times cited : (48)

References (23)
  • 1
    • 0020838840 scopus 로고
    • Purification and properties of a cytochrome P-450 of a fungus, Fusarium oxysporum
    • 1 Shoun H, Sudo Y, Seto Y, Beppu T (1983) Purification and properties of a cytochrome P-450 of a fungus, Fusarium oxysporum. J Biochem 94, 1219-1229
    • (1983) J Biochem , vol.94 , pp. 1219-1229
    • Shoun, H.1    Sudo, Y.2    Seto, Y.3    Beppu, T.4
  • 2
    • 0024589146 scopus 로고
    • Soluble. Nitrate/nitrite-inducible cytochrome P-450 of the fungus, Fusarium oxysporum
    • 2 Shoun H, Suyama W, Yasui T (1989) Soluble. nitrate/nitrite-inducible cytochrome P-450 of the fungus, Fusarium oxysporum. FEBS Lett 244, 11-14
    • (1989) Febs Lett , vol.244 , pp. 11-14
    • Shoun, H.1    Suyama, W.2    Yasui, T.3
  • 3
    • 0025737114 scopus 로고
    • Denitrificatioon by the fungus Fusarium oxysporum and involvement of cytochrome P-450 in the respiratory nitrite reduction
    • 3 Shoun H, Tanimoto T (1991) Denitrificatioon by the fungus Fusarium oxysporum and involvement of cytochrome P-450 in the respiratory nitrite reduction. J Biol Chem 266, 11078-11082
    • (1991) J Biol Chem , vol.266 , pp. 11078-11082
    • Shoun, H.1    Tanimoto, T.2
  • 4
    • 85030290239 scopus 로고
    • Cytochrome P-450 (NOR) of the denitrifier fungus Fusarium oxysporum involved in the respiratory nitrite reduction
    • (Archakov AI, Bachmanova GI, eds) Joint stock company, Moscow
    • 4 Shoun H, Tanimoto T (1991) Cytochrome P-450 (NOR) of the denitrifier fungus Fusarium oxysporum involved in the respiratory nitrite reduction. In: Cytochrome P-450: Biochemistry and Biophysics (Archakov AI, Bachmanova GI, eds) Joint stock company, Moscow, 626-628
    • (1991) Cytochrome P-450: Biochemistry and Biophysics , pp. 626-628
    • Shoun, H.1    Tanimoto, T.2
  • 5
    • 0027418338 scopus 로고
    • Cytochrome P-450 55A1 (P-450dNIR) acts as nitric oxide reductase employing NADH as the direct electron donor
    • 5 Nakahara K, Tanimoto T, Hatano K, Usuda K, Shoun H (1993) Cytochrome P-450 55A1 (P-450dNIR) acts as nitric oxide reductase employing NADH as the direct electron donor. J Biol Chem 268, 8350-8355
    • (1993) J Biol Chem , vol.268 , pp. 8350-8355
    • Nakahara, K.1    Tanimoto, T.2    Hatano, K.3    Usuda, K.4    Shoun, H.5
  • 6
  • 7
    • 0028017299 scopus 로고
    • Kinetics and thermodynamics of CO binding to cytochrome P450nor
    • 7 Shiro Y, Kato M, Iizuka T, Nakahara K, Shoun H (1994) Kinetics and thermodynamics of CO binding to cytochrome P450nor. Biochemistry 33, 8673-8677
    • (1994) Biochemistry , vol.33 , pp. 8673-8677
    • Shiro, Y.1    Kato, M.2    Iizuka, T.3    Nakahara, K.4    Shoun, H.5
  • 8
    • 0029082717 scopus 로고
    • Iron-ligand structure and iron redox property of nitric oxide reductase cytochrome P450nor from Fusarium oxysporum relevance to its NO reduction activity
    • 8 Shiro Y, Fujii M, Isogai Y, Adachi S, Iizuka T, Obayashi E, Makino R, Nakahara K, Shoun H (1995) Iron-ligand structure and iron redox property of nitric oxide reductase cytochrome P450nor from Fusarium oxysporum relevance to its NO reduction activity. Biochemistry 34, 9052-9058
    • (1995) Biochemistry , vol.34 , pp. 9052-9058
    • Shiro, Y.1    Fujii, M.2    Isogai, Y.3    Adachi, S.4    Iizuka, T.5    Obayashi, E.6    Makino, R.7    Nakahara, K.8    Shoun, H.9
  • 9
    • 0025871374 scopus 로고
    • Nucleotidc sequence of the unique nitrate/nitrite-inducible cytochrome P-450 cDNA from Fusarium oxysporum
    • 9 Kizawa H, Tomura D, Oda M, Fukamizu A, Hoshino T, Gotoh O, Yasui T, Shoun H (1991) Nucleotidc sequence of the unique nitrate/nitrite-inducible cytochrome P-450 cDNA from Fusarium oxysporum. J Biol Chem 266, 10632-10637
    • (1991) J Biol Chem , vol.266 , pp. 10632-10637
    • Kizawa, H.1    Tomura, D.2    Oda, M.3    Fukamizu, A.4    Hoshino, T.5    Gotoh, O.6    Yasui, T.7    Shoun, H.8
  • 10
    • 0028959345 scopus 로고
    • Denitrification by the fungus Cylindrocarpon tonkinense: Anaerobic cell growth and two isozyme forms of cytochrome P-450nor
    • 10 Usuda K, Toritsuka N, Matsuo Y, Kim D-H, Shoun H (1995) Denitrification by the fungus Cylindrocarpon tonkinense: anaerobic cell growth and two isozyme forms of cytochrome P-450nor. Appl Environ Microbiol 61, 883-889
    • (1995) Appl Environ Microbiol , vol.61 , pp. 883-889
    • Usuda, K.1    Toritsuka, N.2    Matsuo, Y.3    Kim, D.-H.4    Shoun, H.5
  • 12
    • 0028015584 scopus 로고
    • Nitric oxide reductase cytochrome P-450 gene,CYP55, of the fungus Fusarium oxysporum containing a potential binding-site for FNR, the transcription factor involved in the regulation of anaerobic growth of Escherichia coli
    • 12 Tomura D, Obika K, Fukamizu A, Shoun H (1994) Nitric oxide reductase cytochrome P-450 gene,CYP55, of the fungus Fusarium oxysporum containing a potential binding-site for FNR, the transcription factor involved in the regulation of anaerobic growth of Escherichia coli. J Biochem 116, 88-94
    • (1994) J Biochem , vol.116 , pp. 88-94
    • Tomura, D.1    Obika, K.2    Fukamizu, A.3    Shoun, H.4
  • 13
    • 0027430254 scopus 로고
    • Expression of the fungal cytochrome P-450nor cDNA in Escherichia coli
    • 13 Obika K, Tomura D, Fukamizu A, Shoun H (1993) Expression of the fungal cytochrome P-450nor cDNA in Escherichia coli. Biochem Biophys Res Commun 196, 1255-1260
    • (1993) Biochem Biophys Res Commun , vol.196 , pp. 1255-1260
    • Obika, K.1    Tomura, D.2    Fukamizu, A.3    Shoun, H.4
  • 14
    • 0020529962 scopus 로고
    • Transformation of intact yeast cells treated with alkali cations
    • 14 Ito H, Fukuda Y, Murata K, Kimura A (1983) Transformation of intact yeast cells treated with alkali cations. J Bacteriol 153, 163-168
    • (1983) J Bacteriol , vol.153 , pp. 163-168
    • Ito, H.1    Fukuda, Y.2    Murata, K.3    Kimura, A.4
  • 15
    • 0003136888 scopus 로고
    • Mutagenesis by PCR
    • (Griffin HG, Griffin AM, eds) CRC Press, Boca Raton, Florida
    • 15 Tao BY, Patrick Lee KC (1994) Mutagenesis by PCR. In: PCR Technology: current innovations (Griffin HG, Griffin AM, eds) CRC Press, Boca Raton, Florida, 69-83
    • (1994) PCR Technology: Current Innovations , pp. 69-83
    • Tao, B.Y.1    Patrick Lee, K.C.2
  • 16
    • 50449100139 scopus 로고
    • The carbon monoxide-binding pigment of liver microsomes. II. Solubilization, purification and properties
    • 16 Omura T, Sato R (1964) The carbon monoxide-binding pigment of liver microsomes. II. Solubilization, purification and properties. J Biol Chem 239, 2379-2385
    • (1964) J Biol Chem , vol.239 , pp. 2379-2385
    • Omura, T.1    Sato, R.2
  • 18
    • 0023041821 scopus 로고
    • Prediction of the occurrence of the ADP-binding βαβ-fold in proteins, using an amino acid sequence fingerprint
    • 18 Wirrenga RK, Terpstra P, Hol WGJ (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
    • Wirrenga, R.K.1    Terpstra, P.2    Hol, W.G.J.3
  • 19
    • 0030055213 scopus 로고    scopus 로고
    • Denitrification, a novel type of respiratory metabolism in fungal mitochondrion
    • 19 Kobayashi M, Matsuo Y, Takimoto A, Suzuki S, Maruo F, Shoun H (1996) Denitrification, a novel type of respiratory metabolism in fungal mitochondrion. J Biol Chem 271, 16263-16267
    • (1996) J Biol Chem , vol.271 , pp. 16263-16267
    • Kobayashi, M.1    Matsuo, Y.2    Takimoto, A.3    Suzuki, S.4    Maruo, F.5    Shoun, H.6
  • 20
    • 0026542989 scopus 로고
    • Substrate recognition site in cytochrome P450 family 2 (CYP2) proteins inferred from comparative analyses of amino acid and coding nucleotide sequences
    • 20 Gotoh O (1992) Substrate recognition site in cytochrome P450 family 2 (CYP2) proteins inferred from comparative analyses of amino acid and coding nucleotide sequences. J Biol Chem 267, 83-90
    • (1992) J Biol Chem , vol.267 , pp. 83-90
    • Gotoh, O.1
  • 21
    • 0029586252 scopus 로고
    • Structure of cytochrome P450eryF involved in erythromycin biosynthesis
    • 21 Cupp-Vickery JR, Poulos TL (1995) Structure of cytochrome P450eryF involved in erythromycin biosynthesis. Nature Struct Biology 2, 144-153
    • (1995) Nature Struct Biology , vol.2 , pp. 144-153
    • Cupp-Vickery, J.R.1    Poulos, T.L.2
  • 23
    • 0028282737 scopus 로고
    • Crystallization and preliminary X-ray diffraction studies of nitric oxide reductase cytochrome P450nor from Fusarium oxysporum
    • 23 Nakahara K, Shoun H, Adachi S, Iizuka T, Shiro Y (1994) Crystallization and preliminary X-ray diffraction studies of nitric oxide reductase cytochrome P450nor from Fusarium oxysporum. J Mol Biol 239, 158-159
    • (1994) J Mol Biol , vol.239 , pp. 158-159
    • Nakahara, K.1    Shoun, H.2    Adachi, S.3    Iizuka, T.4    Shiro, Y.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.