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Volumn 3, Issue , 2003, Pages

Molecular evolution of adenylating domain of aminoadipate reductase

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIA (MICROORGANISMS); FUNGI; INSERTION SEQUENCES;

EID: 2942618786     PISSN: 14712148     EISSN: None     Source Type: Journal    
DOI: 10.1186/1471-2148-3-9     Document Type: Article
Times cited : (13)

References (23)
  • 1
    • 0037119358 scopus 로고    scopus 로고
    • The Sulfolobus solfataricus Lrp-like protein LysM regulates lysine biosynthesis in response to lysine availability
    • Brinkman AB, Bell SD, Lebbink RJ, de Vos WM and van der Oost J The Sulfolobus solfataricus Lrp-like protein LysM regulates lysine biosynthesis in response to lysine availability J Biol Chem 2002, 277:29537-29549
    • (2002) J Biol Chem , vol.277 , pp. 29537-29549
    • Brinkman, A.B.1    Bell, S.D.2    Lebbink, R.J.3    De Vos, W.M.4    Van Der Oost, J.5
  • 2
    • 0033404080 scopus 로고    scopus 로고
    • A prokaryotic gene cluster involved in synthesis of lysine through the amino adipate pathway: A key to the evolution of amino acid biosynthesis
    • Nishida H, Nishiyama M, Kobashi N, Kosuge T, Hoshino T and Yamane H A prokaryotic gene cluster involved in synthesis of lysine through the amino adipate pathway: a key to the evolution of amino acid biosynthesis Genome Res 1999, 9:1175-1183
    • (1999) Genome Res , vol.9 , pp. 1175-1183
    • Nishida, H.1    Nishiyama, M.2    Kobashi, N.3    Kosuge, T.4    Hoshino, T.5    Yamane, H.6
  • 3
    • 0036789272 scopus 로고    scopus 로고
    • Molecular evolution of the lysine biosynthetic pathways
    • Velasco AM, Leguina JI and Lazcano A Molecular evolution of the lysine biosynthetic pathways J Mol Evol 2002, 55:445-459
    • (2002) J Mol Evol , vol.55 , pp. 445-459
    • Velasco, A.M.1    Leguina, J.I.2    Lazcano, A.3
  • 4
    • 0033809804 scopus 로고    scopus 로고
    • What is characteristic of fungal lysine synthesis through the α-aminoadipate pathway?
    • Nishida H and Nishiyama M What is characteristic of fungal lysine synthesis through the α-aminoadipate pathway? J Mol Evol 2000, 51:299-302
    • (2000) J Mol Evol , vol.51 , pp. 299-302
    • Nishida, H.1    Nishiyama, M.2
  • 5
    • 0015168691 scopus 로고
    • Lysine biosynthesis in Saccharomyces cerevisiae: Conversion of α-aminoadipate into α-aminoadipate δ-semialdehyde
    • Sinha AK and Bhattacharjee JK Lysine biosynthesis in Saccharomyces cerevisiae : conversion of α-aminoadipate into α-aminoadipate δ-semialdehyde Biochem J 1971, 125:743-749
    • (1971) Biochem J , vol.125 , pp. 743-749
    • Sinha, A.K.1    Bhattacharjee, J.K.2
  • 6
    • 0033545834 scopus 로고    scopus 로고
    • Lysine biosynthesis in Saccharomyces cerevisiae: Mechanism of α-aminoadipate reductase (Lys2) involves post-translational phosphopantetheinylation by Lys5
    • Ehmann DE, Gehring AM and Walsh CT Lysine biosynthesis in Saccharomyces cerevisiae : mechanism of α-aminoadipate reductase (Lys2) involves post-translational phosphopantetheinylation by Lys5 Biochemistry 1999, 38:6171-6177
    • (1999) Biochemistry , vol.38 , pp. 6171-6177
    • Ehmann, D.E.1    Gehring, A.M.2    Walsh, C.T.3
  • 7
    • 0035208474 scopus 로고    scopus 로고
    • Novel posttranslational activation of the LYS2-encoded α-aminoadipate reductase for biosynthesis of lysine and site-directed mutational analysis of conserved amino acid residues in the activation domain of Candida albicans
    • Guo S, Evans SA, Wilkes MB and Bhattacharjee JK Novel posttranslational activation of the LYS2-encoded α-aminoadipate reductase for biosynthesis of lysine and site-directed mutational analysis of conserved amino acid residues in the activation domain of Candida albicans J Bacteriol 2001, 183:7120-7125
    • (2001) J Bacteriol , vol.183 , pp. 7120-7125
    • Guo, S.1    Evans, S.A.2    Wilkes, M.B.3    Bhattacharjee, J.K.4
  • 8
    • 0029921158 scopus 로고    scopus 로고
    • A nonribosomal system of peptide biosynthesis
    • Kleinkauf H and Von Döhren H A nonribosomal system of peptide biosynthesis Eur J Biochem 1996, 236:335-351
    • (1996) Eur J Biochem , vol.236 , pp. 335-351
    • Kleinkauf, H.1    Von Döhren, H.2
  • 9
    • 0025969665 scopus 로고
    • Nucleotide sequence of the LYS2 gene of Saccharomyces cerevisiae: Homology to Bacillus brevis tyrocidine synthetase 1
    • Morris ME and Jinks-Robertson S Nucleotide sequence of the LYS2 gene of Saccharomyces cerevisiae : homology to Bacillus brevis tyrocidine synthetase 1 Gene 1991, 98:141-145
    • (1991) Gene , vol.98 , pp. 141-145
    • Morris, M.E.1    Jinks-Robertson, S.2
  • 10
    • 0026926521 scopus 로고
    • Four homologous domains in the primary structure of GrsB are related to domains in a superfamily of adenylate-forming enzymes
    • Turgay K, Krause M and Marahiel MA Four homologous domains in the primary structure of GrsB are related to domains in a superfamily of adenylate-forming enzymes Mol Microbiol 1992, 6:529-546
    • (1992) Mol Microbiol , vol.6 , pp. 529-546
    • Turgay, K.1    Krause, M.2    Marahiel, M.A.3
  • 11
    • 0242668745 scopus 로고    scopus 로고
    • A new redox-cofactor vitamin for mammals
    • Kasahara T and Kato T A new redox-cofactor vitamin for mammals Nature 2003, 422:832
    • (2003) Nature , vol.422 , pp. 832
    • Kasahara, T.1    Kato, T.2
  • 12
    • 0035095042 scopus 로고    scopus 로고
    • Characterization of the lys2 gene of Acremonium chrysogenum encoding a functional α-aminoadipate activating and reducing enzyme
    • Hijarrubia MJ, Aparico JF, Casqueiro JF and Martín JF Characterization of the lys2 gene of Acremonium chrysogenum encoding a functional α-aminoadipate activating and reducing enzyme Mol Gen Genet 2001, 264:755-762
    • (2001) Mol Gen Genet , vol.264 , pp. 755-762
    • Hijarrubia, M.J.1    Aparico, J.F.2    Casqueiro, J.F.3    Martín, J.F.4
  • 13
    • 2942564339 scopus 로고    scopus 로고
    • Aminoadipate reductase gene: A new fungal-specific gene for comparative evolutionary analyses
    • An KD, Nishida H, Miura Y and Yokota A Aminoadipate reductase gene: a new fungal-specific gene for comparative evolutionary analyses BMC Evol Biol 2002, 2:6
    • (2002) BMC Evol Biol , vol.2 , pp. 6
    • An, K.D.1    Nishida, H.2    Miura, Y.3    Yokota, A.4
  • 15
    • 0029945141 scopus 로고    scopus 로고
    • Comparative sequence analysis on the 18S rRNA gene of Aspergillus oryzae, A. sojae, A. flavus, A. parasticus, A.awamori and A. tamari
    • Nikkuni S, Kosaka N, Suzuki C and Mori K Comparative sequence analysis on the 18S rRNA gene of Aspergillus oryzae, A. sojae, A. flavus, A. parasticus, A.awamori and A. tamari J Gen Appl Microbiol 1996, 42:181-187
    • (1996) J Gen Appl Microbiol , vol.42 , pp. 181-187
    • Nikkuni, S.1    Kosaka, N.2    Suzuki, C.3    Mori, K.4
  • 16
    • 0028185370 scopus 로고
    • Evolutionary conservation of the transcribed spacer sequences of the rDNA repeat unit in three species of the genus Aspergillus
    • Borsuk P, Gniadkowski M, Kucharski R, Bisko M, Kanabus M, Stepien PP and Bartnik E Evolutionary conservation of the transcribed spacer sequences of the rDNA repeat unit in three species of the genus Aspergillus Acta Biochim Pol 1994, 41:73-77
    • (1994) Acta Biochim Pol , vol.41 , pp. 73-77
    • Borsuk, P.1    Gniadkowski, M.2    Kucharski, R.3    Bisko, M.4    Kanabus, M.5    Stepien, P.P.6    Bartnik, E.7
  • 17
    • 0035377219 scopus 로고    scopus 로고
    • Methods for intergrated air sampling and DNA analysis for detection of airborne fungal spores
    • Williams RH, Ward E and McCartney HA Methods for intergrated air sampling and DNA analysis for detection of airborne fungal spores Appl Environ Microbiol 2001, 67:2453-2459
    • (2001) Appl Environ Microbiol , vol.67 , pp. 2453-2459
    • Williams, R.H.1    Ward, E.2    McCartney, H.A.3
  • 18
    • 0031715753 scopus 로고    scopus 로고
    • Characterization of the lys2 gene of Penicillium chrysogenum encoding α-aminoadipic acid reductase
    • Casqueiro J, Gutierrez S, Banuelos O, Fierro F, Velasco J and Martín JF Characterization of the lys2 gene of Penicillium chrysogenum encoding α-aminoadipic acid reductase Mol Gen Genet 1998, 259:549-556
    • (1998) Mol Gen Genet , vol.259 , pp. 549-556
    • Casqueiro, J.1    Gutierrez, S.2    Banuelos, O.3    Fierro, F.4    Velasco, J.5    Martín, J.F.6
  • 19
    • 0031761883 scopus 로고    scopus 로고
    • Evolutionary relationships among Aspergillus oryzae and related species based on the sequences of 18S rRNA genes and internal transcribed spacers
    • Nikkuni S, Nakajima H, Hoshina S, Ohno M, Suzuki C, Kashiwagi Y and Mori K Evolutionary relationships among Aspergillus oryzae and related species based on the sequences of 18S rRNA genes and internal transcribed spacers J Gen Appl Microbiol 1998, 44:225-230
    • (1998) J Gen Appl Microbiol , vol.44 , pp. 225-230
    • Nikkuni, S.1    Nakajima, H.2    Hoshina, S.3    Ohno, M.4    Suzuki, C.5    Kashiwagi, Y.6    Mori, K.7
  • 22
    • 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 JD, Higgins DG and Gibson TJ CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice Nucleic Acids Res 1994, 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.