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Volumn 9, Issue 12, 1999, Pages 1175-1183

A prokaryotic gene cluster involved in synthesis of lysine through the amino adipate pathway: A key to the evolution of amino acid biosynthesis

Author keywords

[No Author keywords available]

Indexed keywords

ADIPIC ACID; AMINO ACID; ARGININE; LEUCINE; LYSINE;

EID: 0033404080     PISSN: 10889051     EISSN: None     Source Type: Journal    
DOI: 10.1101/gr.9.12.1175     Document Type: Article
Times cited : (113)

References (33)
  • 2
    • 0031913669 scopus 로고    scopus 로고
    • Genes and enzymes of the acetyl cycle of arginine biosynthesis in the extreme thermophilic bacterium Thermus thermophilus HB27
    • Baetens, M., C. Legrain, A. Boyen, and M. Glansdorff. 1998. Genes and enzymes of the acetyl cycle of arginine biosynthesis in the extreme thermophilic bacterium Thermus thermophilus HB27. Microbiology 144: 479-492.
    • (1998) Microbiology , vol.144 , pp. 479-492
    • Baetens, M.1    Legrain, C.2    Boyen, A.3    Glansdorff, M.4
  • 3
    • 0029846517 scopus 로고    scopus 로고
    • Comparison of β-glucosidase and β-mannosidase from the hyperthermophilic archaeon Pyrococcus furiosus. Purification, characterization, gene cloning, and sequence analysis
    • Bauer, M.W., E.J. Bylina, R.V. Swanson, and R.M. Kelly. 1996. Comparison of β-glucosidase and β-mannosidase from the hyperthermophilic archaeon Pyrococcus furiosus. Purification, characterization, gene cloning, and sequence analysis. J. Biol. Chem. 271: 23749-23755.
    • (1996) J. Biol. Chem. , vol.271 , pp. 23749-23755
    • Bauer, M.W.1    Bylina, E.J.2    Swanson, R.V.3    Kelly, R.M.4
  • 4
    • 77957016095 scopus 로고
    • Lysine biosynthesis (yeast)
    • Broquist, H.P. 1971. Lysine biosynthesis (yeast). Methods Enzymol. 17: 112-129.
    • (1971) Methods Enzymol. , vol.17 , pp. 112-129
    • Broquist, H.P.1
  • 7
    • 0030708748 scopus 로고    scopus 로고
    • The carbamate kinase-like carbamoyl phosphate synthetase of the hyperthermophilic archaeon Pyrococcus furiosus: A missing link in the evolution of carbamoyl phosphate biosynthesis
    • Durbecq, V., C. Legrain, M. Roovers, A. Piérard, and N. Glansdorff. 1997. The carbamate kinase-like carbamoyl phosphate synthetase of the hyperthermophilic archaeon Pyrococcus furiosus: A missing link in the evolution of carbamoyl phosphate biosynthesis. Proc. Natl. Acad. Sci. 94: 12803-12808.
    • (1997) Proc. Natl. Acad. Sci. , vol.94 , pp. 12803-12808
    • Durbecq, V.1    Legrain, C.2    Roovers, M.3    Piérard, A.4    Glansdorff, N.5
  • 8
    • 0000461280 scopus 로고
    • Confidence limits on phytogenies: An approach using the bootstrap
    • Felsenstein, J. 1985. Confidence limits on phytogenies: An approach using the bootstrap. Evolution 39: 783-791.
    • (1985) Evolution , vol.39 , pp. 783-791
    • Felsenstein, J.1
  • 9
    • 0030061364 scopus 로고    scopus 로고
    • Catalytical potency of β-glucosidase from the extremophile Pyrococcus furiosus in glucoconjugate synthesis
    • Fischer, L., R. Bromann, S.W. Kengen, W.M. de Vos, and F. Wagner. 1996. Catalytical potency of β-glucosidase from the extremophile Pyrococcus furiosus in glucoconjugate synthesis. Biotechnology 14: 88-91.
    • (1996) Biotechnology , vol.14 , pp. 88-91
    • Fischer, L.1    Bromann, R.2    Kengen, S.W.3    De Vos, W.M.4    Wagner, F.5
  • 10
    • 0031467818 scopus 로고    scopus 로고
    • Diverse superfamily of enzymes with ATP-dependent carboxylate-amine/thiol ligase activity
    • Galperin, M.Y. and E.V.A. Koonin. 1997. Diverse superfamily of enzymes with ATP-dependent carboxylate-amine/thiol ligase activity. Protein Sci. 12: 2639-2643.
    • (1997) Protein Sci. , vol.12 , pp. 2639-2643
    • Galperin, M.Y.1    Koonin, E.V.A.2
  • 11
    • 0031039802 scopus 로고    scopus 로고
    • Purification and properties of acetyl-CoA synthase (ADP-forming), an archaeal enzyme of acetate formation and ATP synthesis, from the hyperthermophile Pyrococcus furiosus
    • Glasemacher, J., A.K. Bock, R. Schmid, and P. Schönheit. 1997. Purification and properties of acetyl-CoA synthase (ADP-forming), an archaeal enzyme of acetate formation and ATP synthesis, from the hyperthermophile Pyrococcus furiosus. Eur. J. Biochem. 244: 561-567.
    • (1997) Eur. J. Biochem. , vol.244 , pp. 561-567
    • Glasemacher, J.1    Bock, A.K.2    Schmid, R.3    Schönheit, P.4
  • 13
    • 0031960184 scopus 로고    scopus 로고
    • A unique fungal lysine biosynthesis enzyme shares a common ancestor with tricarboxylic acid cycle and leucine biosynthetic enzymes found in diverse organisms
    • Irvin, S.D. and J.K. Bhattacharjee. 1998. A unique fungal lysine biosynthesis enzyme shares a common ancestor with tricarboxylic acid cycle and leucine biosynthetic enzymes found in diverse organisms. J. Mol. Evol. 46: 401-408.
    • (1998) J. Mol. Evol. , vol.46 , pp. 401-408
    • Irvin, S.D.1    Bhattacharjee, J.K.2
  • 14
    • 0017272554 scopus 로고
    • Enzyme recruitment in evolution of new function
    • Jensen, R.A. 1976. Enzyme recruitment in evolution of new function. Annu. Rev. Microbiol. 30: 409-425.
    • (1976) Annu. Rev. Microbiol. , vol.30 , pp. 409-425
    • Jensen, R.A.1
  • 15
    • 0024674214 scopus 로고
    • Characterization of the gene rimK responsible for the addition of glutamic acid residues to the C-terminus of ribosomal protein s6 in Escherichia coli K12
    • Rang, W.K., T. Icho, S. Isono, M. Kitakawa, and K. Isono. 1989. Characterization of the gene rimK responsible for the addition of glutamic acid residues to the C-terminus of ribosomal protein S6 in Escherichia coli K12. Mol. & Gen. Genet. 217: 281-288.
    • (1989) Mol. & Gen. Genet. , vol.217 , pp. 281-288
    • Rang, W.K.1    Icho, T.2    Isono, S.3    Kitakawa, M.4    Isono, K.5
  • 17
    • 0027465230 scopus 로고
    • Purification and characterization of extremely thermostable β-glucosidase from the hyperthermophilic archaeon Pyrococcus furiosus
    • Kengen, S.W., E.J. Luesink, A.J. Stams, and A.J. Zehnder. 1993. Purification and characterization of extremely thermostable β-glucosidase from the hyperthermophilic archaeon Pyrococcus furiosus. Eur. J. Biochem. 213: 305-312.
    • (1993) Eur. J. Biochem. , vol.213 , pp. 305-312
    • Kengen, S.W.1    Luesink, E.J.2    Stams, A.J.3    Zehnder, A.J.4
  • 19
    • 0032989249 scopus 로고    scopus 로고
    • Aspartate kinase-independent lysine synthesis in an extremely thermophilic bacterium, Thermus thermophilus: Lysine is synthesized via α-aminoadipic acid not via diaminopimelic acid
    • Kobashi, N., M. Nishiyama, and M. Tanokura. 1999. Aspartate kinase-independent lysine synthesis in an extremely thermophilic bacterium, Thermus thermophilus: Lysine is synthesized via α-aminoadipic acid not via diaminopimelic acid. J. Bacteriol. 181: 1713-1718.
    • (1999) J. Bacteriol. , vol.181 , pp. 1713-1718
    • Kobashi, N.1    Nishiyama, M.2    Tanokura, M.3
  • 20
    • 0031407215 scopus 로고    scopus 로고
    • Molecular cloning and sequence analysis of the lysR gene from the extremely thermophilic eubacterium, Thermus thermophilus HB27
    • Kosuge, T. and T. Hoshino. 1997. Molecular cloning and sequence analysis of the lysR gene from the extremely thermophilic eubacterium, Thermus thermophilus HB27. FEMS Microbiol. Lett. 157: 73-79.
    • (1997) FEMS Microbiol. Lett. , vol.157 , pp. 73-79
    • Kosuge, T.1    Hoshino, T.2
  • 21
    • 0032466343 scopus 로고    scopus 로고
    • Lysine is synthesized through the α-aminoadipate pathway in Thermus thermophilus
    • _. 1998. Lysine is synthesized through the α-aminoadipate pathway in Thermus thermophilus. FEMS Microbiol. Lett. 169: 361-367.
    • (1998) FEMS Microbiol. Lett. , vol.169 , pp. 361-367
  • 22
    • 0022448655 scopus 로고
    • Genetic transformation of the extreme thermophile Thermus thermophilus and of other Thermus spp
    • Koyama, Y., T. Hoshino, N. Tomizuka, and K. Furukawa. 1986. Genetic transformation of the extreme thermophile Thermus thermophilus and of other Thermus spp. J. Bacteriol. 166: 338-340.
    • (1986) J. Bacteriol. , vol.166 , pp. 338-340
    • Koyama, Y.1    Hoshino, T.2    Tomizuka, N.3    Furukawa, K.4
  • 24
    • 0029794709 scopus 로고    scopus 로고
    • Purification and characterization of two reversible and ATP-dependent acetyl coenzyme A synthases from the hyperthermophilic archaeon Pyrococcus furiosus
    • Mai, X. and M.W. Adams 1996. Purification and characterization of two reversible and ATP-dependent acetyl coenzyme A synthases from the hyperthermophilic archaeon Pyrococcus furiosus. J. Bacteriol. 178: 5897-5903.
    • (1996) J. Bacteriol. , vol.178 , pp. 5897-5903
    • Mai, X.1    Adams, M.W.2
  • 25
    • 0029933657 scopus 로고    scopus 로고
    • The LYS5 gene of Saccharomyces cerevisiae
    • Miller, K.G. and J.K. Bhattacharjee. 1996. The LYS5 gene of Saccharomyces cerevisiae. Gene 172: 167-168.
    • (1996) Gene , vol.172 , pp. 167-168
    • Miller, K.G.1    Bhattacharjee, J.K.2
  • 26
    • 0025969665 scopus 로고
    • Nucleotide sequence of the LYS2 gene of Saccharomyces cerevisiae: Homology to Bacillus brevis tyrocidine synthetase 1
    • Morris, M.E. and S. Jinks-Robertson. 1991. Nucleotide sequence of the LYS2 gene of Saccharomyces cerevisiae: Homology to Bacillus brevis tyrocidine synthetase 1. Gene 98: 141-145.
    • (1991) Gene , vol.98 , pp. 141-145
    • Morris, M.E.1    Jinks-Robertson, S.2
  • 28
    • 0023375195 scopus 로고
    • The neighbor-joining method: A new method for reconstructing phylogenetic trees
    • Saitou, N. and M. Nei. 1987. The neighbor-joining method: A new method for reconstructing phylogenetic trees. Mol. Biol. Evol. 4: 406-425.
    • (1987) Mol. Biol. Evol. , vol.4 , pp. 406-425
    • Saitou, N.1    Nei, M.2
  • 31
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, positions-specific gap penalties and weight matrix choice
    • Thompson, J.D., D.G. Higgins, and T.J. Gilson. 1994. CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, positions-specific gap penalties and weight matrix choice. Nucleic Acid Res. 22: 4553-4559.
    • (1994) Nucleic Acid Res. , vol.22 , pp. 4553-4559
    • Thompson, J.D.1    Higgins, D.G.2    Gilson, T.J.3
  • 32
    • 0000966280 scopus 로고
    • Distribution of lysine pathways among fungi: Evolutionary implications
    • Vogel, H.J. 1964. Distribution of lysine pathways among fungi: Evolutionary implications. Am. Nat. 98: 446-455.
    • (1964) Am. Nat. , vol.98 , pp. 446-455
    • Vogel, H.J.1
  • 33
    • 0002974895 scopus 로고
    • Lysine biosynthesis and evolution
    • ed. V. Bryson and H.J. Vogel, Academic Press, New York, NY
    • _. 1965. Lysine biosynthesis and evolution. In Evolving genes and proteins (ed. V. Bryson and H.J. Vogel), pp. 25-40. Academic Press, New York, NY.
    • (1965) Evolving Genes and Proteins , pp. 25-40


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.