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Volumn 36, Issue 2, 1999, Pages 238-248

A new subfamily of short bacterial adenylate kinases with the Mycobacterium tuberculosis enzyme as a model: A predictive and experimental study

Author keywords

Adenylate kinase; Infrared spectroscopy; Mycobacterium tuberculosis; NMR spectroscopy; Short variant

Indexed keywords

ADENYLATE KINASE; ENZYME VARIANT;

EID: 0033180953     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0134(19990801)36:2<238::AID-PROT9>3.0.CO;2-K     Document Type: Article
Times cited : (29)

References (34)
  • 1
    • 70349640265 scopus 로고
    • Adenylate kinase
    • Boyer PD, editor. New York: Academic Press
    • rd edition), vol. 8. Boyer PD, editor. New York: Academic Press; 1973. p 279-305.
    • (1973) rd Edition) , vol.8 , pp. 279-305
    • Noda, L.H.1
  • 3
    • 0022869412 scopus 로고
    • Structural relationships in the adenylate kinase family
    • Schulz GE, Schiltz E, Tomasselli AG, et al. Structural relationships in the adenylate kinase family. Eur J Biochem 1986;161:127-132.
    • (1986) Eur J Biochem , vol.161 , pp. 127-132
    • Schulz, G.E.1    Schiltz, E.2    Tomasselli, A.G.3
  • 4
    • 0029897810 scopus 로고    scopus 로고
    • The structure of bovine mitochondrial adenylate kinase: Comparison with isoenzymes in other compartments
    • Schlauderer GJ, Schulz GE. The structure of bovine mitochondrial adenylate kinase: comparison with isoenzymes in other compartments. Protein Sci 1996;5:434-441.
    • (1996) Protein Sci , vol.5 , pp. 434-441
    • Schlauderer, G.J.1    Schulz, G.E.2
  • 5
    • 0026079373 scopus 로고
    • The refined structure of the complex between adenylate kinase from beef heart mitochondrial matrix and its substrate AMP at 1.85 Å resolution
    • Diederichs K, Schulz GE. The refined structure of the complex between adenylate kinase from beef heart mitochondrial matrix and its substrate AMP at 1.85 Å resolution. J Mol Biol 1991;217: 541-549.
    • (1991) J Mol Biol , vol.217 , pp. 541-549
    • Diederichs, K.1    Schulz, G.E.2
  • 6
    • 0023887425 scopus 로고
    • Refined structure of porcine cytosolic adenylate kinase at 2·1 Å resolution
    • Dreusicke D, Karplus PA, Schulz GE. Refined structure of porcine cytosolic adenylate kinase at 2·1 Å resolution. J Mol Biol 1988;199: 359-371.
    • (1988) J Mol Biol , vol.199 , pp. 359-371
    • Dreusicke, D.1    Karplus, P.A.2    Schulz, G.E.3
  • 7
    • 0027448592 scopus 로고
    • Relation structure-fonction chez les enzymes ATP-dépendants, vue à travers la plus petite phosphotransférase, l'adényl kinase
    • Paris: Elsevier
    • Bârzu O, Gilles A.-M. Relation structure-fonction chez les enzymes ATP-dépendants, vue à travers la plus petite phosphotransférase, l'adényl kinase. In: Annals de l' Institut Pasteur lactualites, vol. 4. Paris: Elsevier; 1993. p 121-132.
    • (1993) Annals de L' Institut Pasteur Lactualites , vol.4 , pp. 121-132
    • Bârzu, O.1    Gilles, A.-M.2
  • 8
    • 0025887633 scopus 로고
    • Mechanism of adenylate kinase: Site-directed mutagenesis versus X-ray and NMR
    • Tsai M-D, Yan H. Mechanism of adenylate kinase: site-directed mutagenesis versus X-ray and NMR. Biochemistry 1991;30:6806-6818.
    • (1991) Biochemistry , vol.30 , pp. 6806-6818
    • Tsai, M.-D.1    Yan, H.2
  • 9
    • 0031051923 scopus 로고    scopus 로고
    • The adenylate kinase genes of M. Voltae, M. Thermolithotrophicus, M. Jannaschii, and M. Igneus define a new family of adenylate kinases
    • Ferber DM, Haney PJ, Berk H, Lynn D, Konisky J. The adenylate kinase genes of M. voltae, M. thermolithotrophicus, M. jannaschii, and M. igneus define a new family of adenylate kinases. Gene 1997;185:239-244.
    • (1997) Gene , vol.185 , pp. 239-244
    • Ferber, D.M.1    Haney, P.J.2    Berk, H.3    Lynn, D.4    Konisky, J.5
  • 10
    • 0344815899 scopus 로고    scopus 로고
    • World Health Conference. World Health Organisation, G J Commun Dis Vol. 28, p 215-219.
    • G J Commun Dis , vol.28 , pp. 215-219
  • 11
    • 0027497926 scopus 로고
    • Selection of bacterial virulence genes that are specifically induced in host tissues
    • Mahan MJ, Slauch JM, Mekalanos JJ. Selection of bacterial virulence genes that are specifically induced in host tissues. Science 1993;259:686-688.
    • (1993) Science , vol.259 , pp. 686-688
    • Mahan, M.J.1    Slauch, J.M.2    Mekalanos, J.J.3
  • 12
    • 0030866940 scopus 로고    scopus 로고
    • Fluorescence-based isolation of bacterial genes expressed within host cells
    • Valdivia RH, Falkow S. Fluorescence-based isolation of bacterial genes expressed within host cells. Science 1997;277:2007-2011.
    • (1997) Science , vol.277 , pp. 2007-2011
    • Valdivia, R.H.1    Falkow, S.2
  • 13
    • 0028913920 scopus 로고
    • Identification of bacterial genes that contribute to survival and growth in an intracellular environment
    • Moors MA, Portnoy DA. Identification of bacterial genes that contribute to survival and growth in an intracellular environment. Trends Microbiol 1995;3:83-85.
    • (1995) Trends Microbiol , vol.3 , pp. 83-85
    • Moors, M.A.1    Portnoy, D.A.2
  • 14
    • 0027980891 scopus 로고
    • Five Listeria monocytogenes genes preferentially expressed in infected mammalian cells: plcA, purH, purD, pyrE and an arginine ABC transporter gene, arpJ
    • Klarsfeld AD, Goossens PL, Cossart P Five Listeria monocytogenes genes preferentially expressed in infected mammalian cells: plcA, purH, purD, pyrE and an arginine ABC transporter gene, arpJ. Mol Microbiol 1994; 13:585-597.
    • (1994) Mol Microbiol , vol.13 , pp. 585-597
    • Klarsfeld, A.D.1    Goossens, P.L.2    Cossart, P.3
  • 15
    • 0013902812 scopus 로고
    • Mutants thermosensibles d'Escherichia coli K 12. Isolement et caractérisation rapide
    • Kohiyama M, Cousin D, Ryter A, Jacob F. Mutants thermosensibles d'Escherichia coli K 12. Isolement et caractérisation rapide. Ann Inst Pasteur 1966;110:465-486.
    • (1966) Ann Inst Pasteur , vol.110 , pp. 465-486
    • Kohiyama, M.1    Cousin, D.2    Ryter, A.3    Jacob, F.4
  • 18
    • 0024296268 scopus 로고
    • McrA and McrB restriction phenotypes of some E. coli strains and implications for gene cloning
    • Raleigh EA, Murray NE, Revel H et al. McrA and McrB restriction phenotypes of some E. coli strains and implications for gene cloning. Nucleic Acids Res 1988;16:1563-1575.
    • (1988) Nucleic Acids Res , vol.16 , pp. 1563-1575
    • Raleigh, E.A.1    Murray, N.E.2    Revel, H.3
  • 19
    • 0028953772 scopus 로고
    • Escherichia coli UMP-kinase, a member of the aspartokinase family, is a hexamer regulated by guanine nucleotides and UTP
    • Serina L, Blondin C, Krin E, et al. Escherichia coli UMP-kinase, a member of the aspartokinase family, is a hexamer regulated by guanine nucleotides and UTP. Biochemistry 1995;34:5066-5074.
    • (1995) Biochemistry , vol.34 , pp. 5066-5074
    • Serina, L.1    Blondin, C.2    Krin, E.3
  • 20
    • 0020583803 scopus 로고
    • Simple and fast purification of Escherichia coli adenylate kinase
    • Barzu O, Michelson S. Simple and fast purification of Escherichia coli adenylate kinase. FEBS Lett 1983;153:280-284.
    • (1983) FEBS Lett , vol.153 , pp. 280-284
    • Barzu, O.1    Michelson, S.2
  • 21
    • 0023100239 scopus 로고
    • Structural and catalytic characteristics of Escherichia coli adenylate kinase
    • Saint Girons I, Gilles A-M, Margarita D, et al. Structural and catalytic characteristics of Escherichia coli adenylate kinase. J Biol Chem 1987;262:622-629.
    • (1987) J Biol Chem , vol.262 , pp. 622-629
    • Girons S. I1    Gilles, A.-M.2    Margarita, D.3
  • 22
    • 0026643554 scopus 로고
    • Zinc, a novel structural element found in the family of bacterial adenylate kinases
    • Glaser P, Presecan E, Delepierre M, et al. Zinc, a novel structural element found in the family of bacterial adenylate kinases. Biochemistry 1992;31:3038-3043.
    • (1992) Biochemistry , vol.31 , pp. 3038-3043
    • Glaser, P.1    Presecan, E.2    Delepierre, M.3
  • 24
    • 0031127385 scopus 로고    scopus 로고
    • Structural and catalytic properties of CMP kinase from Bacillus subtilis: A comparative analysis with the homologous enzyme from Escherichia coli
    • Schultz CP, Ylisastigui-Pons L, Serina, L, et al. Structural and catalytic properties of CMP kinase from Bacillus subtilis: A comparative analysis with the homologous enzyme from Escherichia coli. Arch Biochem Biophys 1997;340:144-153.
    • (1997) Arch Biochem Biophys , vol.340 , pp. 144-153
    • Schultz, C.P.1    Ylisastigui-Pons, L.2    Serina, L.3
  • 25
    • 0027323183 scopus 로고
    • 1 in aqueous solution. A fourier transform induced spectroscopic study
    • 1 in aqueous solution. A Fourier transform induced spectroscopic study. J Mol Biol 1993;232:967-981.
    • (1993) J Mol Biol , vol.232 , pp. 967-981
    • Fabian, H.1    Schultz, C.2    Naumann, D.3
  • 26
    • 0027291015 scopus 로고
    • Prediction of protein secondary structure at better than 70% accuracy
    • Rost B, Sander C. Prediction of protein secondary structure at better than 70% accuracy. J Mol Biol 1993;232:584-599.
    • (1993) J Mol Biol , vol.232 , pp. 584-599
    • Rost, B.1    Sander, C.2
  • 27
    • 0028300741 scopus 로고
    • Combining evolutionary information and neural networks to predict protein secondary structure
    • Rost B, Sander C. Combining evolutionary information and neural networks to predict protein secondary structure. Proteins 1994;19:55-72.
    • (1994) Proteins , vol.19 , pp. 55-72
    • Rost, B.1    Sander, C.2
  • 28
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye-binding
    • Bradford MM. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye-binding. Anal Biochem 1976;72:248-254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 29
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970;227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 30
    • 0021100877 scopus 로고
    • The spc ribosomal protein operon of Escherichia coli: Sequence and cotranscription of the ribosomal protein genes and a protein export gene
    • Cerreti DP, Dean D, Davis GR, Bedwell DM, Nomura M. The spc ribosomal protein operon of Escherichia coli: sequence and cotranscription of the ribosomal protein genes and a protein export gene. Nucleic Acids Res 1983;11:2599-2616.
    • (1983) Nucleic Acids Res , vol.11 , pp. 2599-2616
    • Cerreti, D.P.1    Dean, D.2    Davis, G.R.3    Bedwell, D.M.4    Nomura, M.5
  • 31
    • 0026544877 scopus 로고
    • 5A refined at 1.9 Å resolution. A model for a catalytic transition state
    • 5A refined at 1.9 Å resolution. A model for a catalytic transition state. J Mol Biol 1992;224:159-177.
    • (1992) J Mol Biol , vol.224 , pp. 159-177
    • Müller, C.W.1    Schulz, G.E.2
  • 33
    • 0029937408 scopus 로고    scopus 로고
    • Ancient divergence of long and short isoforms of adenylate kinase: Molecular evolution of the nucleoside monophosphate kinase family
    • Fukami-Kobayashi K, Nosaka M, Nakazawa A, Gõ M. Ancient divergence of long and short isoforms of adenylate kinase: molecular evolution of the nucleoside monophosphate kinase family. FEBS Lett 1996;385:214-220.
    • (1996) FEBS Lett , vol.385 , pp. 214-220
    • Fukami-Kobayashi, K.1    Nosaka, M.2    Nakazawa, A.3    Gõ, M.4
  • 34
    • 0016159839 scopus 로고
    • Studies on the effect of starvation on mycobacteria
    • Nyka W. Studies on the effect of starvation on mycobacteria. Infect Immun 1974;9:843-850.
    • (1974) Infect Immun , vol.9 , pp. 843-850
    • Nyka, W.1


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