메뉴 건너뛰기




Volumn 16, Issue 6, 2006, Pages 933-938

Production of coenzyme Q10 by recombinant E. coli harboring the decaprenyl diphosphate synthase gene from Sinorhizobium meliloti

Author keywords

Coenzyme Q10; Decaprenyl diphosphate synthase; Sinorhizobium meliloti

Indexed keywords

BACTERIAL PROTEIN; DECAPRENYL DIPHOSPHATE SYNTHASE; UBIDECARENONE; UNCLASSIFIED DRUG;

EID: 33745601375     PISSN: 10177825     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (8)

References (23)
  • 1
    • 0035839019 scopus 로고    scopus 로고
    • Coenzyme Q blocks biochemical but not receptor-mediated apoptosis by increasing mitochondrial antioxidant protection
    • Alleva, R., M. Tomasetti, L. Andera, N. Gellert, B. Borghi, C. Weber, M. P. Murphy, and J. Neuzil. 2001. Coenzyme Q blocks biochemical but not receptor-mediated apoptosis by increasing mitochondrial antioxidant protection. FEBS Lett. 503: 46-50.
    • (2001) FEBS Lett. , vol.503 , pp. 46-50
    • Alleva, R.1    Tomasetti, M.2    Andera, L.3    Gellert, N.4    Borghi, B.5    Weber, C.6    Murphy, M.P.7    Neuzil, J.8
  • 3
    • 0028269724 scopus 로고
    • Isoprenyl diphosphate synthases: Protein sequence comparisons, a phylogenetic tree, and predictions of secondary structure
    • Chen, A., P. A. Kroon, and C. D. Poulter. 1994. Isoprenyl diphosphate synthases: Protein sequence comparisons, a phylogenetic tree, and predictions of secondary structure. Protein Sci. 3: 600-607.
    • (1994) Protein Sci. , vol.3 , pp. 600-607
    • Chen, A.1    Kroon, P.A.2    Poulter, C.D.3
  • 4
    • 0029042393 scopus 로고
    • Biochemical, physiological and medical aspects of ubiquinone function
    • Ernster, L. and G. Dallner. 1995. Biochemical, physiological and medical aspects of ubiquinone function. Biochim. Biophys. Acta 1271: 195-204.
    • (1995) Biochim. Biophys. Acta , vol.1271 , pp. 195-204
    • Ernster, L.1    Dallner, G.2
  • 5
    • 0027768770 scopus 로고
    • Effect of site-directed mutagenesis of conserved aspartate and arginine residues upon farnesyl diphosphate synthase activity
    • Joly, A. and P. A. Edwards. 1993. Effect of site-directed mutagenesis of conserved aspartate and arginine residues upon farnesyl diphosphate synthase activity. J. Biol. Chem. 268: 26983-26989.
    • (1993) J. Biol. Chem. , vol.268 , pp. 26983-26989
    • Joly, A.1    Edwards, P.A.2
  • 6
    • 0036965887 scopus 로고    scopus 로고
    • Biosynthesis, bioproduction and novel roles of ubiquinone
    • Kawamukai, M. 2002. Biosynthesis, bioproduction and novel roles of ubiquinone. J. Biosci. Bioeng. 94: 511-517.
    • (2002) J. Biosci. Bioeng. , vol.94 , pp. 511-517
    • Kawamukai, M.1
  • 7
    • 0027503220 scopus 로고
    • Thermostable farnesyl diphosphate synthase of Bacillus stearothermophilus: Molecular cloning, sequence determination, overproduction, and purification
    • Koyama, T., S. Obata, M. Osabe, A. Takeshita, K. Yokoyama, M. Uchida, T. Nishino, and K. Ogura. 1993. Thermostable farnesyl diphosphate synthase of Bacillus stearothermophilus: Molecular cloning, sequence determination, overproduction, and purification. J. Biochem. (Tokyo) 113: 355-363.
    • (1993) J. Biochem. (Tokyo) , vol.113 , pp. 355-363
    • Koyama, T.1    Obata, S.2    Osabe, M.3    Takeshita, A.4    Yokoyama, K.5    Uchida, M.6    Nishino, T.7    Ogura, K.8
  • 8
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. 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
  • 9
    • 1142305999 scopus 로고    scopus 로고
    • Cloning and functional expression of the dps gene encoding decaprenyl diphosphate synthase from Agrobacterium tumefaciens
    • Lee, J. K., G. Her, S. Y. Kim, and J. H. Seo. 2004. Cloning and functional expression of the dps gene encoding decaprenyl diphosphate synthase from Agrobacterium tumefaciens. Biotechnol. Prog. 20: 51-56.
    • (2004) Biotechnol. Prog. , vol.20 , pp. 51-56
    • Lee, J.K.1    Her, G.2    Kim, S.Y.3    Seo, J.H.4
  • 10
    • 0035949539 scopus 로고    scopus 로고
    • Ubiquinone biosynthesis in microorganisms
    • Meganathan, R. 2001. Ubiquinone biosynthesis in microorganisms. FEMS Microbiol. Lett. 203: 131-139.
    • (2001) FEMS Microbiol. Lett. , vol.203 , pp. 131-139
    • Meganathan, R.1
  • 11
    • 0028180730 scopus 로고
    • Characterization of polyprenyldiphosphate: 4-Hydroxybenzoate polyprenyltransferase from Escherichia coli
    • Melzer, M. and L. Heide. 1994. Characterization of polyprenyldiphosphate: 4-Hydroxybenzoate polyprenyltransferase from Escherichia coli. Biochim. Biophys. Acta 1212: 93-102.
    • (1994) Biochim. Biophys. Acta , vol.1212 , pp. 93-102
    • Melzer, M.1    Heide, L.2
  • 12
    • 0029804201 scopus 로고    scopus 로고
    • A role of the amino acid residue located on the fifth position before the first aspartate-rich motif of farnesyl diphosphate synthase on determination of the final product
    • Ohnuma, S., K. Narita, T. Nakazawa, C. Ishida, Y. Takeuchi, C. Ohto, and T. Nishino. 1996. A role of the amino acid residue located on the fifth position before the first aspartate-rich motif of farnesyl diphosphate synthase on determination of the final product. J. Biol. Chem. 271: 30748-30754.
    • (1996) J. Biol. Chem. , vol.271 , pp. 30748-30754
    • Ohnuma, S.1    Narita, K.2    Nakazawa, T.3    Ishida, C.4    Takeuchi, Y.5    Ohto, C.6    Nishino, T.7
  • 14
    • 0032127476 scopus 로고    scopus 로고
    • Molecular cloning and mutational analysis of the ddsA gene encoding decaprenyl diphosphate synthase from Gluconobacter suboxydans
    • Okada, K., T. Kainou, K. Tanaka, T. Nakagawa, H. Matsuda, and M. Kawamukai. 1998. Molecular cloning and mutational analysis of the ddsA gene encoding decaprenyl diphosphate synthase from Gluconobacter suboxydans. Eur. J. Biochem. 255: 52-59.
    • (1998) Eur. J. Biochem. , vol.255 , pp. 52-59
    • Okada, K.1    Kainou, T.2    Tanaka, K.3    Nakagawa, T.4    Matsuda, H.5    Kawamukai, M.6
  • 15
    • 0142025150 scopus 로고    scopus 로고
    • Fission yeast decaprenyl diphosphate synthase consists of Dps1 and the newly characterized Dlp1 protein in a novel heterotetrameric structure
    • Saiki, R., A. Nagata, N. Uchida, T. Kainow, H. Matsuda, and M. Kawamukai. 2003. Fission yeast decaprenyl diphosphate synthase consists of Dps1 and the newly characterized Dlp1 protein in a novel heterotetrameric structure. Eur. J. Biochem. 270: 4113-4121.
    • (2003) Eur. J. Biochem. , vol.270 , pp. 4113-4121
    • Saiki, R.1    Nagata, A.2    Uchida, N.3    Kainow, T.4    Matsuda, H.5    Kawamukai, M.6
  • 16
    • 85026134689 scopus 로고    scopus 로고
    • 10 and cardiovascular disease: A review
    • 10 and cardiovascular disease: A review. J. Cardiovasc. Nurs. 16: 9-20.
    • (2002) J. Cardiovasc. Nurs. , vol.16 , pp. 9-20
    • Sarter, B.1
  • 17
    • 0028288134 scopus 로고
    • Yeast farnesyl-diphosphate synthase: Site-directed mutagenesis of residues in highly conserved prenyltransferase domains I and II
    • Song, L. and C. D. Poulter. 1994. Yeast farnesyl-diphosphate synthase: Site-directed mutagenesis of residues in highly conserved prenyltransferase domains I and II. Proc. Natl. Acad. Sci. USA 91: 3044-3048.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 3044-3048
    • Song, L.1    Poulter, C.D.2
  • 18
    • 0030964846 scopus 로고    scopus 로고
    • Analysis of the decaprenyl diphosphate synthase (dps) gene in fission yeast suggests a role of ubiquinone as an antioxidant
    • Suzuki, K., K. Okada, Y. Kamiya, X. F. Zhu, T. Nakagawa, M. Kawamukai, and H. Matsuda. 1997. Analysis of the decaprenyl diphosphate synthase (dps) gene in fission yeast suggests a role of ubiquinone as an antioxidant. J. Biochem. 121: 496-505.
    • (1997) J. Biochem. , vol.121 , pp. 496-505
    • Suzuki, K.1    Okada, K.2    Kamiya, Y.3    Zhu, X.F.4    Nakagawa, T.5    Kawamukai, M.6    Matsuda, H.7
  • 20
    • 0142107261 scopus 로고    scopus 로고
    • Isolation and expression of Paracoccus denitrificans decaprenyl diphosphate synthase gene for production of ubiquinone-10 in Escherichia coli
    • Takahashi, S., T. Nishino, and T. Koyam. 2003. Isolation and expression of Paracoccus denitrificans decaprenyl diphosphate synthase gene for production of ubiquinone-10 in Escherichia coli. Biochem. Eng. J. 16: 183-190.
    • (2003) Biochem. Eng. J. , vol.16 , pp. 183-190
    • Takahashi, S.1    Nishino, T.2    Koyam, T.3
  • 21
    • 0028145239 scopus 로고
    • Crystal structure of recombinant farnesyl diphosphate synthase at 2.6-A resolution
    • Tarshis, L. C., M. Yan, C. D. Poulter, and J. C. Sacchettini. 1994. Crystal structure of recombinant farnesyl diphosphate synthase at 2.6-A resolution. Biochemistry 3: 10871-10877.
    • (1994) Biochemistry , vol.3 , pp. 10871-10877
    • Tarshis, L.C.1    Yan, M.2    Poulter, C.D.3    Sacchettini, J.C.4
  • 23
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson, J. D., D. G. Higgins, and T. J. Gibson. 1994. CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22: 4673-4680.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.