메뉴 건너뛰기




Volumn 7, Issue 6, 2012, Pages

Glutamine versus ammonia utilization in the NAD synthetase family

Author keywords

[No Author keywords available]

Indexed keywords

AMMONIA; GLUTAMINE; NICOTINAMIDE ADENINE DINUCLEOTIDE SYNTHASE; SYNTHETASE; UNCLASSIFIED DRUG;

EID: 84862492833     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0039115     Document Type: Article
Times cited : (37)

References (60)
  • 2
  • 3
    • 0037376665 scopus 로고    scopus 로고
    • Nicotinamide adenine dinucleotide, a metabolic regulator of transcription, longevity and disease
    • Lin SJ, Guarente L, (2003) Nicotinamide adenine dinucleotide, a metabolic regulator of transcription, longevity and disease. Curr Opin Cell Biol 15: 241-246.
    • (2003) Curr Opin Cell Biol , vol.15 , pp. 241-246
    • Lin, S.J.1    Guarente, L.2
  • 5
    • 33846922557 scopus 로고    scopus 로고
    • A subsystems-based approach to the identification of drug targets in bacterial pathogens
    • Osterman AL, Begley TP, (2007) A subsystems-based approach to the identification of drug targets in bacterial pathogens. Prog Drug Res 64: 131, 133-170.
    • (2007) Prog Drug Res , vol.64
    • Osterman, A.L.1    Begley, T.P.2
  • 6
    • 50349099789 scopus 로고    scopus 로고
    • Biosynthesis and recycling of nicotinamide cofactors in mycobacterium tuberculosis. An essential role for NAD in nonreplicating bacilli
    • Boshoff HI, Xu X, Tahlan K, Dowd CS, Pethe K, et al. (2008) Biosynthesis and recycling of nicotinamide cofactors in mycobacterium tuberculosis. An essential role for NAD in nonreplicating bacilli. J Biol Chem 283: 19329-19341.
    • (2008) J Biol Chem , vol.283 , pp. 19329-19341
    • Boshoff, H.I.1    Xu, X.2    Tahlan, K.3    Dowd, C.S.4    Pethe, K.5
  • 8
    • 34250161577 scopus 로고    scopus 로고
    • Antibacterial nicotinamide adenine dinucleotide synthetase inhibitors: amide- and ether-linked tethered dimers with alpha-amino acid end groups
    • Velu SE, Mou L, Luan CH, Yang ZW, DeLucas LJ, et al. (2007) Antibacterial nicotinamide adenine dinucleotide synthetase inhibitors: amide- and ether-linked tethered dimers with alpha-amino acid end groups. J Med Chem 50: 2612-2621.
    • (2007) J Med Chem , vol.50 , pp. 2612-2621
    • Velu, S.E.1    Mou, L.2    Luan, C.H.3    Yang, Z.W.4    DeLucas, L.J.5
  • 9
    • 0036947230 scopus 로고    scopus 로고
    • Ribosylnicotinamide kinase domain of NadR protein: identification and implications in NAD biosynthesis
    • Kurnasov OV, Polanuyer BM, Ananta S, Sloutsky R, Tam A, et al. (2002) Ribosylnicotinamide kinase domain of NadR protein: identification and implications in NAD biosynthesis. J Bacteriol 184: 6906-6917.
    • (2002) J Bacteriol , vol.184 , pp. 6906-6917
    • Kurnasov, O.V.1    Polanuyer, B.M.2    Ananta, S.3    Sloutsky, R.4    Tam, A.5
  • 10
    • 78649827278 scopus 로고    scopus 로고
    • Genomics-driven reconstruction of acinetobacter NAD metabolism: insights for antibacterial target selection
    • Sorci L, Blaby I, De Ingeniis J, Gerdes S, Raffaelli N, et al. (2010) Genomics-driven reconstruction of acinetobacter NAD metabolism: insights for antibacterial target selection. J Biol Chem 285: 39490-39499.
    • (2010) J Biol Chem , vol.285 , pp. 39490-39499
    • Sorci, L.1    Blaby, I.2    de Ingeniis, J.3    Gerdes, S.4    Raffaelli, N.5
  • 11
    • 62549094038 scopus 로고    scopus 로고
    • Nicotinamide mononucleotide synthetase is the key enzyme for an alternative route of NAD biosynthesis in Francisella tularensis
    • Sorci L, Martynowski D, Rodionov DA, Eyobo Y, Zogaj X, et al. (2009) Nicotinamide mononucleotide synthetase is the key enzyme for an alternative route of NAD biosynthesis in Francisella tularensis. Proc Natl Acad Sci U S A 106: 3083-3088.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 3083-3088
    • Sorci, L.1    Martynowski, D.2    Rodionov, D.A.3    Eyobo, Y.4    Zogaj, X.5
  • 12
    • 38949157741 scopus 로고    scopus 로고
    • Bifunctional NMN adenylyltransferase/ADP-ribose pyrophosphatase: structure and function in bacterial NAD metabolism
    • Huang N, Sorci L, Zhang X, Brautigam CA, Li X, et al. (2008) Bifunctional NMN adenylyltransferase/ADP-ribose pyrophosphatase: structure and function in bacterial NAD metabolism. Structure 16: 196-209.
    • (2008) Structure , vol.16 , pp. 196-209
    • Huang, N.1    Sorci, L.2    Zhang, X.3    Brautigam, C.A.4    Li, X.5
  • 13
    • 2342550554 scopus 로고    scopus 로고
    • Discoveries of nicotinamide riboside as a nutrient and conserved NRK genes establish a Preiss-Handler independent route to NAD+ in fungi and humans
    • Bieganowski P, Brenner C, (2004) Discoveries of nicotinamide riboside as a nutrient and conserved NRK genes establish a Preiss-Handler independent route to NAD+ in fungi and humans. Cell 117: 495-502.
    • (2004) Cell , vol.117 , pp. 495-502
    • Bieganowski, P.1    Brenner, C.2
  • 14
    • 0030024963 scopus 로고    scopus 로고
    • The crystal structure of GMP synthetase reveals a novel catalytic triad and is a structural paradigm for two enzyme families
    • Tesmer JJ, Klem TJ, Deras ML, Davisson VJ, Smith JL, (1996) The crystal structure of GMP synthetase reveals a novel catalytic triad and is a structural paradigm for two enzyme families. Nat Struct Biol 3: 74-86.
    • (1996) Nat Struct Biol , vol.3 , pp. 74-86
    • Tesmer, J.J.1    Klem, T.J.2    Deras, M.L.3    Davisson, V.J.4    Smith, J.L.5
  • 15
    • 84855290528 scopus 로고    scopus 로고
    • Divergence and convergence in enzyme evolution
    • Galperin MY, Koonin EV, (2012) Divergence and convergence in enzyme evolution. J Biol Chem 287: 21-28.
    • (2012) J Biol Chem , vol.287 , pp. 21-28
    • Galperin, M.Y.1    Koonin, E.V.2
  • 16
    • 0031721044 scopus 로고    scopus 로고
    • Salmonella typhimurium nit is nadE: defective nitrogen utilization and ammonia-dependent NAD synthetase
    • Schneider BL, Reitzer LJ, (1998) Salmonella typhimurium nit is nadE: defective nitrogen utilization and ammonia-dependent NAD synthetase. J Bacteriol 180: 4739-4741.
    • (1998) J Bacteriol , vol.180 , pp. 4739-4741
    • Schneider, B.L.1    Reitzer, L.J.2
  • 17
    • 0036909261 scopus 로고    scopus 로고
    • Catalysis in the nitrilase superfamily
    • Brenner C, (2002) Catalysis in the nitrilase superfamily. Curr Opin Struct Biol 12: 775-782.
    • (2002) Curr Opin Struct Biol , vol.12 , pp. 775-782
    • Brenner, C.1
  • 18
    • 0042377362 scopus 로고    scopus 로고
    • Eukaryotic NAD+ synthetase Qns1 contains an essential, obligate intramolecular thiol glutamine amidotransferase domain related to nitrilase
    • Bieganowski P, Pace HC, Brenner C, (2003) Eukaryotic NAD+ synthetase Qns1 contains an essential, obligate intramolecular thiol glutamine amidotransferase domain related to nitrilase. J Biol Chem 278: 33049-33055.
    • (2003) J Biol Chem , vol.278 , pp. 33049-33055
    • Bieganowski, P.1    Pace, H.C.2    Brenner, C.3
  • 19
    • 0043198091 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae QNS1 codes for NAD(+) synthetase that is functionally conserved in mammals
    • Suda Y, Tachikawa H, Yokota A, Nakanishi H, Yamashita N, et al. (2003) Saccharomyces cerevisiae QNS1 codes for NAD(+) synthetase that is functionally conserved in mammals. Yeast 20: 995-1005.
    • (2003) Yeast , vol.20 , pp. 995-1005
    • Suda, Y.1    Tachikawa, H.2    Yokota, A.3    Nakanishi, H.4    Yamashita, N.5
  • 20
    • 0037500302 scopus 로고    scopus 로고
    • Molecular identification of human glutamine- and ammonia-dependent NAD synthetases. Carbon-nitrogen hydrolase domain confers glutamine dependency
    • Hara N, Yamada K, Terashima M, Osago H, Shimoyama M, et al. (2003) Molecular identification of human glutamine- and ammonia-dependent NAD synthetases. Carbon-nitrogen hydrolase domain confers glutamine dependency. J Biol Chem 278: 10914-10921.
    • (2003) J Biol Chem , vol.278 , pp. 10914-10921
    • Hara, N.1    Yamada, K.2    Terashima, M.3    Osago, H.4    Shimoyama, M.5
  • 22
    • 64049098303 scopus 로고    scopus 로고
    • Regulation of active site coupling in glutamine-dependent NAD(+) synthetase
    • LaRonde-LeBlanc N, Resto M, Gerratana B, (2009) Regulation of active site coupling in glutamine-dependent NAD(+) synthetase. Nat Struct Mol Biol 16: 421-429.
    • (2009) Nat Struct Mol Biol , vol.16 , pp. 421-429
    • LaRonde-LeBlanc, N.1    Resto, M.2    Gerratana, B.3
  • 23
    • 70249112557 scopus 로고    scopus 로고
    • An ancestral glutamine-dependent NAD(+) synthetase revealed by poor kinetic synergism
    • Resto M, Yaffe J, Gerratana B, (2009) An ancestral glutamine-dependent NAD(+) synthetase revealed by poor kinetic synergism. Biochim Biophys Acta 1794: 1648-1653.
    • (2009) Biochim Biophys Acta , vol.1794 , pp. 1648-1653
    • Resto, M.1    Yaffe, J.2    Gerratana, B.3
  • 24
    • 84859456944 scopus 로고    scopus 로고
    • Regulation of the intersubunit ammonia tunnel in Mycobacterium tuberculosis glutamine-dependent NAD+ synthetase
    • Chuenchor W, Doukov TI, Resto M, Chang A, Gerratana B, (2012) Regulation of the intersubunit ammonia tunnel in Mycobacterium tuberculosis glutamine-dependent NAD+ synthetase. Biochem J 443: 417-426.
    • (2012) Biochem J , vol.443 , pp. 417-426
    • Chuenchor, W.1    Doukov, T.I.2    Resto, M.3    Chang, A.4    Gerratana, B.5
  • 25
    • 0041876231 scopus 로고    scopus 로고
    • The reported human NADsyn2 is ammonia-dependent NAD synthetase from a pseudomonad
    • Bieganowski P, Brenner C, (2003) The reported human NADsyn2 is ammonia-dependent NAD synthetase from a pseudomonad. J Biol Chem 278: 33056-33059.
    • (2003) J Biol Chem , vol.278 , pp. 33056-33059
    • Bieganowski, P.1    Brenner, C.2
  • 26
    • 0028934050 scopus 로고
    • The outB gene of Bacillus subtilis codes for NAD synthetase
    • Nessi C, Albertini AM, Speranza ML, Galizzi A, (1995) The outB gene of Bacillus subtilis codes for NAD synthetase. J Biol Chem 270: 6181-6185.
    • (1995) J Biol Chem , vol.270 , pp. 6181-6185
    • Nessi, C.1    Albertini, A.M.2    Speranza, M.L.3    Galizzi, A.4
  • 27
    • 0346655241 scopus 로고    scopus 로고
    • Identification of NAD+ synthetase from Streptococcus sobrinus as a B-cell-stimulatory protein
    • Veiga-Malta I, Duarte M, Dinis M, Madureira P, Ferreira P, et al. (2004) Identification of NAD+ synthetase from Streptococcus sobrinus as a B-cell-stimulatory protein. J Bacteriol 186: 419-426.
    • (2004) J Bacteriol , vol.186 , pp. 419-426
    • Veiga-Malta, I.1    Duarte, M.2    Dinis, M.3    Madureira, P.4    Ferreira, P.5
  • 28
    • 0028238982 scopus 로고
    • The Escherichia coli efg gene and the Rhodobacter capsulatus adgA gene code for NH3-dependent NAD synthetase
    • Willison JC, Tissot G, (1994) The Escherichia coli efg gene and the Rhodobacter capsulatus adgA gene code for NH3-dependent NAD synthetase. J Bacteriol 176: 3400-3402.
    • (1994) J Bacteriol , vol.176 , pp. 3400-3402
    • Willison, J.C.1    Tissot, G.2
  • 29
    • 1842848056 scopus 로고    scopus 로고
    • Stable ammonia-specific NAD synthetase from Bacillus stearothermophilus: purification, characterization, gene cloning, and applications
    • Yamaguchi F, Koga S, Yoshioka I, Takahashi M, Sakuraba H, et al. (2002) Stable ammonia-specific NAD synthetase from Bacillus stearothermophilus: purification, characterization, gene cloning, and applications. Biosci Biotechnol Biochem 66: 2052-2059.
    • (2002) Biosci Biotechnol Biochem , vol.66 , pp. 2052-2059
    • Yamaguchi, F.1    Koga, S.2    Yoshioka, I.3    Takahashi, M.4    Sakuraba, H.5
  • 31
    • 17644400173 scopus 로고    scopus 로고
    • Structures of Escherichia coli NAD synthetase with substrates and products reveal mechanistic rearrangements
    • Jauch R, Humm A, Huber R, Wahl MC, (2005) Structures of Escherichia coli NAD synthetase with substrates and products reveal mechanistic rearrangements. J Biol Chem 280: 15131-15140.
    • (2005) J Biol Chem , vol.280 , pp. 15131-15140
    • Jauch, R.1    Humm, A.2    Huber, R.3    Wahl, M.C.4
  • 32
    • 13944249564 scopus 로고    scopus 로고
    • Crystal structure of NH3-dependent NAD+ synthetase from Helicobacter pylori
    • Kang GB, Kim YS, Im YJ, Rho SH, Lee JH, et al. (2005) Crystal structure of NH3-dependent NAD+ synthetase from Helicobacter pylori. Proteins 58: 985-988.
    • (2005) Proteins , vol.58 , pp. 985-988
    • Kang, G.B.1    Kim, Y.S.2    Im, Y.J.3    Rho, S.H.4    Lee, J.H.5
  • 33
    • 34447641825 scopus 로고    scopus 로고
    • Structural adaptation of an interacting non-native C-terminal helical extension revealed in the crystal structure of NAD+ synthetase from Bacillus anthracis
    • McDonald HM, Pruett PS, Deivanayagam C, Protasevich, II, Carson WM, et al. (2007) Structural adaptation of an interacting non-native C-terminal helical extension revealed in the crystal structure of NAD+ synthetase from Bacillus anthracis. Acta Crystallogr D Biol Crystallogr 63: 891-905.
    • (2007) Acta Crystallogr D Biol Crystallogr , vol.63 , pp. 891-905
    • McDonald, H.M.1    Pruett, P.S.2    Deivanayagam, C.3    Protasevich II4    Carson, W.M.5
  • 34
    • 0032531011 scopus 로고    scopus 로고
    • A novel deamido-NAD+-binding site revealed by the trapped NAD-adenylate intermediate in the NAD+ synthetase structure
    • Rizzi M, Bolognesi M, Coda A, (1998) A novel deamido-NAD+-binding site revealed by the trapped NAD-adenylate intermediate in the NAD+ synthetase structure. Structure 6: 1129-1140.
    • (1998) Structure , vol.6 , pp. 1129-1140
    • Rizzi, M.1    Bolognesi, M.2    Coda, A.3
  • 36
    • 0017194604 scopus 로고
    • Mutant strains (nit) of Salmonella typhimurium with a pleiotropic defect in nitrogen metabolism
    • Broach J, Neumann C, Kustu S, (1976) Mutant strains (nit) of Salmonella typhimurium with a pleiotropic defect in nitrogen metabolism. J Bacteriol 128: 86-98.
    • (1976) J Bacteriol , vol.128 , pp. 86-98
    • Broach, J.1    Neumann, C.2    Kustu, S.3
  • 37
    • 0028853811 scopus 로고
    • Domain organization and a protease-sensitive loop in eukaryotic ornithine decarboxylase
    • Osterman AL, Lueder DV, Quick M, Myers D, Canagarajah BJ, et al. (1995) Domain organization and a protease-sensitive loop in eukaryotic ornithine decarboxylase. Biochemistry 34: 13431-13436.
    • (1995) Biochemistry , vol.34 , pp. 13431-13436
    • Osterman, A.L.1    Lueder, D.V.2    Quick, M.3    Myers, D.4    Canagarajah, B.J.5
  • 38
    • 0035180870 scopus 로고    scopus 로고
    • Archaeal shikimate kinase, a new member of the GHMP-kinase family
    • Daugherty M, Vonstein V, Overbeek R, Osterman A, (2001) Archaeal shikimate kinase, a new member of the GHMP-kinase family. J Bacteriol 183: 292-300.
    • (2001) J Bacteriol , vol.183 , pp. 292-300
    • Daugherty, M.1    Vonstein, V.2    Overbeek, R.3    Osterman, A.4
  • 39
    • 25644458211 scopus 로고    scopus 로고
    • The subsystems approach to genome annotation and its use in the project to annotate 1000 genomes
    • Overbeek R, Begley T, Butler RM, Choudhuri JV, Chuang H-Y, et al. (2005) The subsystems approach to genome annotation and its use in the project to annotate 1000 genomes. Nucleic acids research 33: 5691-5702.
    • (2005) Nucleic Acids Research , vol.33 , pp. 5691-5702
    • Overbeek, R.1    Begley, T.2    Butler, R.M.3    Choudhuri, J.V.4    Chuang, H.-Y.5
  • 41
    • 84872487803 scopus 로고    scopus 로고
    • Oracle Express (XE) website, Available
    • Oracle Express (XE) website. Accessed Available:http://www.oracle.com/technetwork/products/express-edition/downloads/index.html. 23 May (2012)
    • (2012)
  • 42
    • 3042666256 scopus 로고    scopus 로고
    • MUSCLE: multiple sequence alignment with high accuracy and high throughput
    • Edgar RC, (2004) MUSCLE: multiple sequence alignment with high accuracy and high throughput. Nucleic acids research 32: 1792-1797.
    • (2004) Nucleic Acids Research , vol.32 , pp. 1792-1797
    • Edgar, R.C.1
  • 43
    • 77949718257 scopus 로고    scopus 로고
    • FastTree 2-approximately maximum-likelihood trees for large alignments
    • Price MN, Dehal PS, Arkin AP, (2010) FastTree 2-approximately maximum-likelihood trees for large alignments. PLoS One 5: e9490.
    • (2010) PLoS One , vol.5
    • Price, M.N.1    Dehal, P.S.2    Arkin, A.P.3
  • 44
    • 50249100595 scopus 로고    scopus 로고
    • A rapid bootstrap algorithm for the RAxML Web servers
    • Stamatakis A, Hoover P, Rougemont J, (2008) A rapid bootstrap algorithm for the RAxML Web servers. Syst Biol 57: 758-771.
    • (2008) Syst Biol , vol.57 , pp. 758-771
    • Stamatakis, A.1    Hoover, P.2    Rougemont, J.3
  • 49
    • 84906292166 scopus 로고    scopus 로고
    • Genomics and Enzymology of NAD Biosynthesis
    • In: Lew M, Hung-Wen L, editors, editors
    • Sorci L, Kurnasov O, Rodionov DA, Osterman AL, (2010) Genomics and Enzymology of NAD Biosynthesis. In: Lew M, Hung-Wen L, editors. pp. 213-257 editors. Comprehensive Natural Products II. Oxford: Elsevier.
    • (2010) , pp. 213-257
    • Sorci, L.1    Kurnasov, O.2    Rodionov, D.A.3    Osterman, A.L.4
  • 50
    • 33749347331 scopus 로고    scopus 로고
    • NAD+ utilization in Pasteurellaceae: simplification of a complex pathway
    • Gerlach G, Reidl J, (2006) NAD+ utilization in Pasteurellaceae: simplification of a complex pathway. J Bacteriol 188: 6719-6727.
    • (2006) J Bacteriol , vol.188 , pp. 6719-6727
    • Gerlach, G.1    Reidl, J.2
  • 51
    • 0037398732 scopus 로고    scopus 로고
    • Missing genes in metabolic pathways: a comparative genomics approach
    • Osterman A, Overbeek R, (2003) Missing genes in metabolic pathways: a comparative genomics approach. Curr Opin Chem Biol 7: 238-251.
    • (2003) Curr Opin Chem Biol , vol.7 , pp. 238-251
    • Osterman, A.1    Overbeek, R.2
  • 52
    • 0022272456 scopus 로고
    • NAD synthetase
    • Zalkin H, (1985) NAD synthetase. Methods Enzymol 113: 297-302.
    • (1985) Methods Enzymol , vol.113 , pp. 297-302
    • Zalkin, H.1
  • 53
    • 0029789527 scopus 로고    scopus 로고
    • Crystal structure of NH3-dependent NAD+ synthetase from Bacillus subtilis
    • Rizzi M, Nessi C, Mattevi A, Coda A, Bolognesi M, et al. (1996) Crystal structure of NH3-dependent NAD+ synthetase from Bacillus subtilis. Embo J 15: 5125-5134.
    • (1996) Embo J , vol.15 , pp. 5125-5134
    • Rizzi, M.1    Nessi, C.2    Mattevi, A.3    Coda, A.4    Bolognesi, M.5
  • 54
    • 3242891674 scopus 로고    scopus 로고
    • SDPpred: a tool for prediction of amino acid residues that determine differences in functional specificity of homologous proteins
    • Kalinina OV, Novichkov PS, Mironov AA, Gelfand MS, Rakhmaninova AB, (2004) SDPpred: a tool for prediction of amino acid residues that determine differences in functional specificity of homologous proteins. Nucleic Acids Res 32: W424-428.
    • (2004) Nucleic Acids Res , vol.32
    • Kalinina, O.V.1    Novichkov, P.S.2    Mironov, A.A.3    Gelfand, M.S.4    Rakhmaninova, A.B.5
  • 55
    • 84855259681 scopus 로고    scopus 로고
    • The FGGY carbohydrate kinase family: insights into the evolution of functional specificities
    • Zhang Y, Zagnitko O, Rodionova I, Osterman A, Godzik A, (2011) The FGGY carbohydrate kinase family: insights into the evolution of functional specificities. PLoS Comput Biol 7: e1002318.
    • (2011) PLoS Comput Biol , vol.7
    • Zhang, Y.1    Zagnitko, O.2    Rodionova, I.3    Osterman, A.4    Godzik, A.5
  • 56
    • 77955103653 scopus 로고    scopus 로고
    • Systematic analysis of short internal indels and their impact on protein folding
    • Kim R, Guo J-t, (2010) Systematic analysis of short internal indels and their impact on protein folding. BMC structural biology 10: 24.
    • (2010) BMC Structural Biology , vol.10 , pp. 24
    • Kim, R.1    Guo, J.-t.2
  • 57
    • 34548767667 scopus 로고    scopus 로고
    • Interaction-site prediction for protein complexes: a critical assessment
    • Zhou H-X, Qin S, (2007) Interaction-site prediction for protein complexes: a critical assessment. Bioinformatics (Oxford, England) 23: 2203-2209.
    • (2007) Bioinformatics (Oxford, England) , vol.23 , pp. 2203-2209
    • Zhou, H.-X.1    Qin, S.2
  • 58
    • 0036046771 scopus 로고    scopus 로고
    • Evolution of gene fusions: horizontal transfer versus independent events
    • Yanai I, Wolf YI, Koonin EV, (2002) Evolution of gene fusions: horizontal transfer versus independent events. Genome biology 3: research0024.
    • (2002) Genome Biology , vol.3
    • Yanai, I.1    Wolf, Y.I.2    Koonin, E.V.3
  • 59
    • 77955039174 scopus 로고    scopus 로고
    • The origin and early evolution of eukaryotes in the light of phylogenomics
    • Koonin EV, (2010) The origin and early evolution of eukaryotes in the light of phylogenomics. Genome biology 11: 209.
    • (2010) Genome Biology , vol.11 , pp. 209
    • Koonin, E.V.1
  • 60
    • 33845945135 scopus 로고    scopus 로고
    • Glutamine-dependent NAD+ synthetase. How a two-domain, three-substrate enzyme avoids waste
    • Wojcik M, Seidle HF, Bieganowski P, Brenner C, (2006) Glutamine-dependent NAD+ synthetase. How a two-domain, three-substrate enzyme avoids waste. J Biol Chem 281: 33395-33402.
    • (2006) J Biol Chem , vol.281 , pp. 33395-33402
    • Wojcik, M.1    Seidle, H.F.2    Bieganowski, P.3    Brenner, C.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.