메뉴 건너뛰기




Volumn 180, Issue 10, 1998, Pages 2782-2787

Menaquinone (vitamin K2) biosynthesis: Localization and characterization of the menA gene from Escherichia coli

Author keywords

[No Author keywords available]

Indexed keywords

FARNOQUINONE; MENAQUINONE; 1,4 DIHYDROXY 2 NAPHTHOIC ACID; 1,4-DIHYDROXY-2-NAPHTHOIC ACID; 4 HYDROXYBENZOATE POLYPRENYLTRANSFERASE; 4-HYDROXYBENZOATE POLYPRENYLTRANSFERASE; BACTERIAL PROTEIN; ESCHERICHIA COLI PROTEIN; MENA PROTEIN, E COLI; NAPHTHOL DERIVATIVE; TRANSFERASE; VITAMIN K GROUP;

EID: 0031596770     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.180.10.2782-2787.1998     Document Type: Article
Times cited : (119)

References (25)
  • 1
    • 0026731820 scopus 로고
    • COQ2 is a candidate for the structural gene encoding para-hydroxybenzoate:Octaprenyltransferase
    • Asby, M. N., S. Y. Kutsunai, S. Ackerman, A. Tzagoloff, and P. A. Edwards. 1992. COQ2 is a candidate for the structural gene encoding para-hydroxybenzoate:octaprenyltransferase. J. Biol. Chem. 267:4128-4136.
    • (1992) J. Biol. Chem. , vol.267 , pp. 4128-4136
    • Asby, M.N.1    Kutsunai, S.Y.2    Ackerman, S.3    Tzagoloff, A.4    Edwards, P.A.5
  • 3
    • 15444345457 scopus 로고
    • Biosynthesis of vitamin K and other natural naphthoquinones
    • Bentley, R. 1975. Biosynthesis of vitamin K and other natural naphthoquinones. Pure Appl. Chem. 41:47-68.
    • (1975) Pure Appl. Chem. , vol.41 , pp. 47-68
    • Bentley, R.1
  • 4
    • 0020413535 scopus 로고
    • Biosynthesis of vitamin K (menaquinone) in bacteria
    • Bentley, R., and R. Meganathan. 1982. Biosynthesis of vitamin K (menaquinone) in bacteria. Microbiol. Rev. 46:241-280.
    • (1982) Microbiol. Rev. , vol.46 , pp. 241-280
    • Bentley, R.1    Meganathan, R.2
  • 5
    • 0018800089 scopus 로고
    • A rapid alkaline extraction procedure for screening recombinant plasmid DNA
    • Birnboim, B. G., and J. Doly. 1979. A rapid alkaline extraction procedure for screening recombinant plasmid DNA. Nucleic Acids Res. 7:1513-1523.
    • (1979) Nucleic Acids Res. , vol.7 , pp. 1513-1523
    • Birnboim, B.G.1    Doly, J.2
  • 6
    • 33845261493 scopus 로고
    • A rapid method of total lipid extraction and purification
    • Bligh, E. G., and W. J. Dyer. 1959. A rapid method of total lipid extraction and purification. Can. J. Biochem. Physiol. 37:911-917.
    • (1959) Can. J. Biochem. Physiol. , vol.37 , pp. 911-917
    • Bligh, E.G.1    Dyer, W.J.2
  • 7
    • 0025944865 scopus 로고
    • Dimethyl sulfoxide reductase is not required for trimethylamine N-oxide reduction in Escherichia coli
    • Daruwala, R., and R. Meganathan. 1991. Dimethyl sulfoxide reductase is not required for trimethylamine N-oxide reduction in Escherichia coli. FEMS Microbiol. Lett. 83:255-260.
    • (1991) FEMS Microbiol. Lett. , vol.83 , pp. 255-260
    • Daruwala, R.1    Meganathan, R.2
  • 8
    • 0026602761 scopus 로고
    • A 5′-terminal stem-loop structure can stabilize mRNA in Escherichia coli
    • Emory, S. A., P. Bouvet, and J. G. Belasco. 1992. A 5′-terminal stem-loop structure can stabilize mRNA in Escherichia coli. Genes Dev. 6:135-148.
    • (1992) Genes Dev. , vol.6 , pp. 135-148
    • Emory, S.A.1    Bouvet, P.2    Belasco, J.G.3
  • 9
    • 0031038898 scopus 로고    scopus 로고
    • A C-methyltransferase involved in both ubiquinone and menaquinone biosynthesis: Isolation and identification of the Escherichia coli ubiE gene
    • Lee, P. T., A. Y. Hsu, H. T. Ha, and C. F. Clarke. 1997. A C-methyltransferase involved in both ubiquinone and menaquinone biosynthesis: isolation and identification of the Escherichia coli ubiE gene. J. Bacteriol. 179:1748-1754.
    • (1997) J. Bacteriol. , vol.179 , pp. 1748-1754
    • Lee, P.T.1    Hsu, A.Y.2    Ha, H.T.3    Clarke, C.F.4
  • 10
    • 0002496082 scopus 로고
    • Pathways for anaerobic electron transport
    • F. C. Neidhardt, J. L. Ingraham, K. B. Low, B. Magasanik, M. Schaechter, and H. E. Umbarger (ed.), American Society for Microbiology, Washington, D.C.
    • Lin, E. C. C., and D. Kuritzkes. 1987. Pathways for anaerobic electron transport, p. 202-221. In F. C. Neidhardt, J. L. Ingraham, K. B. Low, B. Magasanik, M. Schaechter, and H. E. Umbarger (ed.), Escherichia coli and Salmonella typhimurium: cellular and molecular biology. American Society for Microbiology, Washington, D.C.
    • (1987) Escherichia Coli and Salmonella Typhimurium: Cellular and Molecular Biology , pp. 202-221
    • Lin, E.C.C.1    Kuritzkes, D.2
  • 12
    • 0000036588 scopus 로고    scopus 로고
    • 2) and ubiquinone (coenzyme Q)
    • F. C. Neidhardt, R. Curtiss III, J. L. Ingraham, E. C. C. Lin, K. B. Low, B. Magasanik, W. S. Reznikoff, M. Riley, M. Schaechter, and H. E. Umbarger (ed.), American Society for Microbiology, Washington, D.C.
    • 2) and ubiquinone (coenzyme Q), p. 642-656. In F. C. Neidhardt, R. Curtiss III, J. L. Ingraham, E. C. C. Lin, K. B. Low, B. Magasanik, W. S. Reznikoff, M. Riley, M. Schaechter, and H. E. Umbarger (ed.), Escherichia coli and Salmonella: cellular and molecular biology, 2nd ed. American Society for Microbiology, Washington, D.C.
    • (1996) Escherichia Coli and Salmonella: Cellular and Molecular Biology, 2nd Ed. , pp. 642-656
    • Meganathan, R.1
  • 13
    • 0022393659 scopus 로고
    • Identity of the quinone in Bacillus alcalophilus
    • Meganathan, R., and R. Coffell. 1985. Identity of the quinone in Bacillus alcalophilus. J. Bacteriol. 164:911-913.
    • (1985) J. Bacteriol. , vol.164 , pp. 911-913
    • Meganathan, R.1    Coffell, R.2
  • 14
    • 0025763253 scopus 로고
    • Electron donors and the quinone involved in dimethyl sulfoxide reduction in Escherichia coli
    • Miguel, L., and R. Meganathan. 1991. Electron donors and the quinone involved in dimethyl sulfoxide reduction in Escherichia coli. Curr. Microbiol. 22:109-115.
    • (1991) Curr. Microbiol. , vol.22 , pp. 109-115
    • Miguel, L.1    Meganathan, R.2
  • 15
    • 0015233824 scopus 로고
    • The function of menaquinone (vitamin K2) in Escherichia coli K12
    • Newton, N. A., G. B. Cox, and F. Gibson. 1971. The function of menaquinone (vitamin K2) in Escherichia coli K12. Biochim. Biophys. Acta. 244:155-166.
    • (1971) Biochim. Biophys. Acta , vol.244 , pp. 155-166
    • Newton, N.A.1    Cox, G.B.2    Gibson, F.3
  • 16
    • 0026521577 scopus 로고
    • Correlation of a subset of the pLC plasmids to the physical map of Escherichia coli K-12
    • Nishimura, A., K. Akiyama, Y. Kohara, and K. Horiuchi. 1992. Correlation of a subset of the pLC plasmids to the physical map of Escherichia coli K-12. Microbiol. Rev. 56:137-151.
    • (1992) Microbiol. Rev. , vol.56 , pp. 137-151
    • Nishimura, A.1    Akiyama, K.2    Kohara, Y.3    Horiuchi, K.4
  • 17
    • 0026615820 scopus 로고
    • 2) biosynthesis: Evidence that the Escherichia coli menD gene encodes both 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylic acid synthase and α-ketoglutarate decarboxylase activities
    • 2) biosynthesis: evidence that the Escherichia coli menD gene encodes both 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylic acid synthase and α-ketoglutarate decarboxylase activities. J. Bacteriol. 174:8111-8118.
    • (1992) J. Bacteriol. , vol.174 , pp. 8111-8118
    • Palaniappan, C.1    Sharma, V.2    Hudspeth, M.E.S.3    Meganathan, R.4
  • 18
    • 0027219606 scopus 로고
    • Analysis of the Escherichia coli genome. III. DNA sequence of the region from 87.2 to 89.2 minutes
    • Plunkett, G., III, V. Burland, D. L. Daniels, and F. R. Blattner. 1993. Analysis of the Escherichia coli genome. III. DNA sequence of the region from 87.2 to 89.2 minutes. Nucleic Acids Res. 21:3391-3398.
    • (1993) Nucleic Acids Res. , vol.21 , pp. 3391-3398
    • Plunkett III, G.1    Burland, V.2    Daniels, D.L.3    Blattner, F.R.4
  • 20
    • 0026611037 scopus 로고
    • 2) biosynthesis: Nucleotide sequence and expression of the menB gene from Escherichia coli
    • 2) biosynthesis: nucleotide sequence and expression of the menB gene from Escherichia coli. J. Bacteriol. 174:5057-5062.
    • (1992) J. Bacteriol. , vol.174 , pp. 5057-5062
    • Sharma, V.1    Suvarna, K.2    Meganathan, R.3    Hudspeth, M.E.S.4
  • 21
    • 0017177848 scopus 로고
    • Biosynthesis of bacterial menaquinones: The membrane associated 1,4-dihydroxy-2-naphthoate octaprenyl-transferase of Escherichia coli
    • Shineberg, B., and I. G. Young. 1976. Biosynthesis of bacterial menaquinones: the membrane associated 1,4-dihydroxy-2-naphthoate octaprenyl-transferase of Escherichia coli. Biochemistry 15:2754-2758.
    • (1976) Biochemistry , vol.15 , pp. 2754-2758
    • Shineberg, B.1    Young, I.G.2
  • 23
    • 0024231821 scopus 로고
    • Differential roles of menaquinone and demethylmenaquinone in anaerobic electron transport of E. coli and their fnr-independent expression
    • Unden, G. 1988. Differential roles of menaquinone and demethylmenaquinone in anaerobic electron transport of E. coli and their fnr-independent expression. Arch. Microbiol. 150:499-503.
    • (1988) Arch. Microbiol. , vol.150 , pp. 499-503
    • Unden, G.1
  • 25
    • 0027165748 scopus 로고
    • Mutants of Escherichia coli affected in respiration: The cloning and nucleotide sequence of ubiA, encoding the membrane-bound p-hydroxybenzoate:octaprenyltransferase
    • Wu, G., H. D. Williams, F. Gibson, and R. K. Poole. 1993. Mutants of Escherichia coli affected in respiration: the cloning and nucleotide sequence of ubiA, encoding the membrane-bound p-hydroxybenzoate:octaprenyltransferase. J. Gen. Microbiol. 139:1795-1805.
    • (1993) J. Gen. Microbiol. , vol.139 , pp. 1795-1805
    • Wu, G.1    Williams, H.D.2    Gibson, F.3    Poole, R.K.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.