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Volumn 288, Issue 4, 1999, Pages 753-763

The hyperthermostable indoleglycerol phosphate synthase from Thermotoga maritima is destabilized by mutational disruption of two solvent-exposed salt bridges

Author keywords

( )8 barrel protein; Indoleglycerol phosphate synthase; Site directed mutagenesis; Thermostability; Tryptophan biosynthesis

Indexed keywords

RECOMBINANT PROTEIN; SYNTHETASE; TRYPTOPHAN;

EID: 0344848664     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1999.2709     Document Type: Article
Times cited : (63)

References (53)
  • 1
    • 0027487614 scopus 로고
    • Enzymes and proteins from organisms that grow near and above 100 °c
    • Adams M. W. W. Enzymes and proteins from organisms that grow near and above 100 °C. Annu. Rev. Microbiol. 47:1993;627-658.
    • (1993) Annu. Rev. Microbiol. , vol.47 , pp. 627-658
    • Adams, M.W.W.1
  • 2
    • 0031554925 scopus 로고    scopus 로고
    • Crystal structure of the β-glycosidase from the hyperthermophilic archeon Sulfolobus solfataricus: Resilience as a key factor in thermostability
    • Aguilar C. F., Sanderson I., Moracci M., Ciaramella M., Nucci R., Rossi M., Pearl L. H. Crystal structure of the β-glycosidase from the hyperthermophilic archeon Sulfolobus solfataricus: resilience as a key factor in thermostability. J. Mol. Biol. 271:1997;789-802.
    • (1997) J. Mol. Biol. , vol.271 , pp. 789-802
    • Aguilar, C.F.1    Sanderson, I.2    Moracci, M.3    Ciaramella, M.4    Nucci, R.5    Rossi, M.6    Pearl, L.H.7
  • 3
    • 0030906459 scopus 로고    scopus 로고
    • Stability of a thermophilic TIM-barrel enzyme: Indole-3-glycerol phosphate synthase from the thermophilic archaeonSulfolobus solfataricus
    • Andreotti G., Cubellis M. V., Di Palo M., Fessas D., Sannia G., Marino G. Stability of a thermophilic TIM-barrel enzyme: indole-3-glycerol phosphate synthase from the thermophilic archaeonSulfolobus solfataricus. Biochem. J. 323:1997;259-264.
    • (1997) Biochem. J. , vol.323 , pp. 259-264
    • Andreotti, G.1    Cubellis, M.V.2    Di Palo, M.3    Fessas, D.4    Sannia, G.5    Marino, G.6
  • 4
    • 0031573453 scopus 로고    scopus 로고
    • Closed structure of phosphoglycerate kinase from Thermotoga maritima reveals the catalytic mechanism and determinants of thermal stability
    • Auerbach G., Huber R., Grättinger M., Zaiss K., Schurig H., Jaenicke R., Jacob U. Closed structure of phosphoglycerate kinase from Thermotoga maritima reveals the catalytic mechanism and determinants of thermal stability. Structure. 5:1997;1475-1483.
    • (1997) Structure , vol.5 , pp. 1475-1483
    • Auerbach, G.1    Huber, R.2    Grättinger, M.3    Zaiss, K.4    Schurig, H.5    Jaenicke, R.6    Jacob, U.7
  • 5
    • 0032526414 scopus 로고    scopus 로고
    • Lactate dehydrogenase from the hyperthermophilic bacterium Thermotoga maritima: The crystal structure at 2.1 Å resolution reveals strategies for intrinsic protein stabilization
    • Auerbach G., Ostendorp R., Prade L., Korndorfer I., Dams T., Huber R., Jaenicke R. Lactate dehydrogenase from the hyperthermophilic bacterium Thermotoga maritima: the crystal structure at 2.1 Å resolution reveals strategies for intrinsic protein stabilization. Structure. 6:1998;769-781.
    • (1998) Structure , vol.6 , pp. 769-781
    • Auerbach, G.1    Ostendorp, R.2    Prade, L.3    Korndorfer, I.4    Dams, T.5    Huber, R.6    Jaenicke, R.7
  • 7
    • 0014028006 scopus 로고
    • Indole-3-glycerol phosphate synthetase of Escherichia coli, an enzyme of the tryptophan operon
    • Creighton T. E., Yanofsky C. Indole-3-glycerol phosphate synthetase of Escherichia coli, an enzyme of the tryptophan operon. J. Biol. Chem. 241:1966;4616-4624.
    • (1966) J. Biol. Chem. , vol.241 , pp. 4616-4624
    • Creighton, T.E.1    Yanofsky, C.2
  • 9
    • 0014429434 scopus 로고
    • Ammonium sulfate concentration conversion nomograph for 0 degrees
    • Di Jeso F. Ammonium sulfate concentration conversion nomograph for 0 degrees. J. Biol. Chem. 243:1968;2022-2023.
    • (1968) J. Biol. Chem. , vol.243 , pp. 2022-2023
    • Di Jeso, F.1
  • 10
    • 0025102221 scopus 로고
    • A set of programs for analysis of kinetic and equilibrium data
    • Eberhard M. A set of programs for analysis of kinetic and equilibrium data. Comput. Appl. Biosci. 6:1990;213-221.
    • (1990) Comput. Appl. Biosci. , vol.6 , pp. 213-221
    • Eberhard, M.1
  • 11
    • 0029003832 scopus 로고
    • Indoleglycerol phosphate synthase - phosporibosyl anthranilate isomerase: Comparison of the bifunctional enzyme fromEscherichia coli with engineered monofunctional domains
    • Eberhard M., Tsai-Pflugfelder M., Bolewska K., Hommel U., Kirschner K. Indoleglycerol phosphate synthase - phosporibosyl anthranilate isomerase: comparison of the bifunctional enzyme fromEscherichia coli with engineered monofunctional domains. Biochemistry. 34:1995;5419-5428.
    • (1995) Biochemistry , vol.34 , pp. 5419-5428
    • Eberhard, M.1    Tsai-Pflugfelder, M.2    Bolewska, K.3    Hommel, U.4    Kirschner, K.5
  • 12
    • 0026692715 scopus 로고
    • Protein engineering of a disulfide bond in a β/α-barrel protein
    • Eder J., Wilmans M. Protein engineering of a disulfide bond in a β/α-barrel protein. Biochemistry. 31:1992;4437-4444.
    • (1992) Biochemistry , vol.31 , pp. 4437-4444
    • Eder, J.1    Wilmans, M.2
  • 13
    • 0032573431 scopus 로고    scopus 로고
    • The stability of salt bridges at high temperatures: Implications for hyperthermophilic proteins
    • Elcock A. H. The stability of salt bridges at high temperatures: implications for hyperthermophilic proteins. J. Mol. Biol. 284:1998;489-502.
    • (1998) J. Mol. Biol. , vol.284 , pp. 489-502
    • Elcock, A.H.1
  • 14
    • 2142746284 scopus 로고
    • The activated complex in chemical reactions
    • Eyring H. The activated complex in chemical reactions. J. Chem. Phys. 3:1935;107-115.
    • (1935) J. Chem. Phys. , vol.3 , pp. 107-115
    • Eyring, H.1
  • 16
    • 0016648840 scopus 로고
    • A rapid spectrophotofluorometric assay for indoleglycerol phosphate synthase
    • Hankins C. N., Largen M., Mills S. E. A rapid spectrophotofluorometric assay for indoleglycerol phosphate synthase. Anal. Biochem. 69:1975;510-517.
    • (1975) Anal. Biochem. , vol.69 , pp. 510-517
    • Hankins, C.N.1    Largen, M.2    Mills, S.E.3
  • 17
    • 0028158008 scopus 로고
    • Rapid crystallization of T4 lysozyme by intermolecular disulfide cross-linking
    • Heinz D. W., Matthews B. W. Rapid crystallization of T4 lysozyme by intermolecular disulfide cross-linking. Protein Eng. 7:1994;301-307.
    • (1994) Protein Eng. , vol.7 , pp. 301-307
    • Heinz, D.W.1    Matthews, B.W.2
  • 18
    • 0028994307 scopus 로고
    • 2.0 Å structure of indole-3-glycerol phosphate synthase from the hyperthermophile Sulfolobus solfataricus: Possible determinants of protein stability
    • Hennig M., Darimont B., Sterner R., Kirschner K., Jansonius J. N. 2.0 Å structure of indole-3-glycerol phosphate synthase from the hyperthermophile Sulfolobus solfataricus: possible determinants of protein stability. Structure. 3:1995;1295-1306.
    • (1995) Structure , vol.3 , pp. 1295-1306
    • Hennig, M.1    Darimont, B.2    Sterner, R.3    Kirschner, K.4    Jansonius, J.N.5
  • 19
    • 0030977659 scopus 로고    scopus 로고
    • Crystal structure at 2.0 Å resolution of phosphoribosyl anthranilate isomerase from the hyperthermophileThermotoga maritima : Possible determinants of protein stability
    • Hennig M., Sterner R., Kirschner K., Jansonius J. N. Crystal structure at 2.0 Å resolution of phosphoribosyl anthranilate isomerase from the hyperthermophileThermotoga maritima : possible determinants of protein stability. Biochemistry. 36:1997;6009-6016.
    • (1997) Biochemistry , vol.36 , pp. 6009-6016
    • Hennig, M.1    Sterner, R.2    Kirschner, K.3    Jansonius, J.N.4
  • 20
    • 0029048523 scopus 로고
    • Phosphoribosyl anthranilate isomerase catalyzes a reversible Amadori reaction
    • Hommel U., Eberhard M., Kirschner K. Phosphoribosyl anthranilate isomerase catalyzes a reversible Amadori reaction. Biochemistry. 34:1995;5429-5439.
    • (1995) Biochemistry , vol.34 , pp. 5429-5439
    • Hommel, U.1    Eberhard, M.2    Kirschner, K.3
  • 21
    • 0025663105 scopus 로고
    • Strength and co-operativity of contributions of surface salt bridges to protein stability
    • Horovitz A., Serrano L., Avron B., Bycroft M., Fersht A. R. Strength and co-operativity of contributions of surface salt bridges to protein stability. J. Mol. Biol. 216:1990;1031-1044.
    • (1990) J. Mol. Biol. , vol.216 , pp. 1031-1044
    • Horovitz, A.1    Serrano, L.2    Avron, B.3    Bycroft, M.4    Fersht, A.R.5
  • 22
    • 0031042074 scopus 로고    scopus 로고
    • Ion-pair and charged hydrogen-bond interactions between histidine and aspartate in a peptide helix
    • Huyghues-Despointes B. M. P., Baldwin R. L. Ion-pair and charged hydrogen-bond interactions between histidine and aspartate in a peptide helix. Biochemistry. 36:1997;1965-1970.
    • (1997) Biochemistry , vol.36 , pp. 1965-1970
    • Huyghues-Despointes, B.M.P.1    Baldwin, R.L.2
  • 23
    • 0030067190 scopus 로고    scopus 로고
    • Stability and folding of ultrastable proteins: Eye lens crystallins and enzymes from thermophiles
    • Jaenicke R. Stability and folding of ultrastable proteins: eye lens crystallins and enzymes from thermophiles. FASEB J. 10:1996;84-92.
    • (1996) FASEB J. , vol.10 , pp. 84-92
    • Jaenicke, R.1
  • 24
    • 0032438190 scopus 로고    scopus 로고
    • Stability of proteins in extreme environments
    • Jaenicke R., Böhm G. Stability of proteins in extreme environments. Curr. Opin. Struct. Biol. 8:1998;738-748.
    • (1998) Curr. Opin. Struct. Biol. , vol.8 , pp. 738-748
    • Jaenicke, R.1    Böhm, G.2
  • 25
    • 0029786277 scopus 로고    scopus 로고
    • Structure and stability of hyperstable proteins: Glycolytic enzymes from hyperthermophilic bacterium Thermotoga maritima
    • Jaenicke R., Schurig H., Beaucamp N., Ostendorp R. Structure and stability of hyperstable proteins: glycolytic enzymes from hyperthermophilic bacterium Thermotoga maritima. Advan. Protein Chem. 48:1996;181-269.
    • (1996) Advan. Protein Chem. , vol.48 , pp. 181-269
    • Jaenicke, R.1    Schurig, H.2    Beaucamp, N.3    Ostendorp, R.4
  • 26
    • 0031003188 scopus 로고    scopus 로고
    • Contribution of a salt bridge to the thermostability of DNA binding protein HU from Bacillus stearothermophilus determined by site-directed mutagenes
    • Kawamura S., Tanaka I., Yamasaki N., Kimura M. Contribution of a salt bridge to the thermostability of DNA binding protein HU from Bacillus stearothermophilus determined by site-directed mutagenes. J. Biochem. 121:1997;448-455.
    • (1997) J. Biochem. , vol.121 , pp. 448-455
    • Kawamura, S.1    Tanaka, I.2    Yamasaki, N.3    Kimura, M.4
  • 27
    • 0027237407 scopus 로고
    • Studies of the hyperthermophile Thermotoga maritima by random sequencing of cDNA and genomic libraries
    • Kim C. W., Markiewicz P., Lee J. J., Schierle C. F., Miller J. H. Studies of the hyperthermophile Thermotoga maritima by random sequencing of cDNA and genomic libraries. J. Mol. Biol. 231:1993;960-981.
    • (1993) J. Mol. Biol. , vol.231 , pp. 960-981
    • Kim, C.W.1    Markiewicz, P.2    Lee, J.J.3    Schierle, C.F.4    Miller, J.H.5
  • 28
    • 0023084230 scopus 로고
    • Phophoribosylanthranilate isomerase-indoleglycerol-phosphate synthase from Escherichia coli
    • Kirschner K., Szadkowski H., Jardetzky T. S., Hager V. Phophoribosylanthranilate isomerase-indoleglycerol-phosphate synthase from Escherichia coli. Methods Enzymol. 142:1987;386-397.
    • (1987) Methods Enzymol. , vol.142 , pp. 386-397
    • Kirschner, K.1    Szadkowski, H.2    Jardetzky, T.S.3    Hager, V.4
  • 29
    • 0031564613 scopus 로고    scopus 로고
    • Crystal structure of glutamate dehydrogenase from the hyperthermophilic eubacterium Thermotoga maritima at 3.0 Å resolution
    • Knapp S., de Vos W. M., Rice D., Ladenstein R. Crystal structure of glutamate dehydrogenase from the hyperthermophilic eubacterium Thermotoga maritima at 3.0 Å resolution. J. Mol. Biol. 267:1997;916-932.
    • (1997) J. Mol. Biol. , vol.267 , pp. 916-932
    • Knapp, S.1    De Vos, W.M.2    Rice, D.3    Ladenstein, R.4
  • 31
    • 0030568997 scopus 로고    scopus 로고
    • The crystal structure of indole-3-glycerol phosphate synthase from the hyperthermophilic archaeon Sulfolobus solfataricus in three different crystal forms: Effect of ionic strength
    • Knöchel T., Hennig M., Merz A., Darimont B., Kirschner K., Jansonius J. N. The crystal structure of indole-3-glycerol phosphate synthase from the hyperthermophilic archaeon Sulfolobus solfataricus in three different crystal forms: effect of ionic strength. J. Mol. Biol. 262:1996;502-515.
    • (1996) J. Mol. Biol. , vol.262 , pp. 502-515
    • Knöchel, T.1    Hennig, M.2    Merz, A.3    Darimont, B.4    Kirschner, K.5    Jansonius, J.N.6
  • 32
    • 0028903461 scopus 로고
    • The crystal structure of holo-glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic bacteriumThermotoga maritima at 2.5 Å resolution
    • Korndörfer I., Steipe B., Huber R., Tomschy A., Jaenicke R. The crystal structure of holo-glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic bacteriumThermotoga maritima at 2.5 Å resolution. J. Mol. Biol. 246:1995;511-521.
    • (1995) J. Mol. Biol. , vol.246 , pp. 511-521
    • Korndörfer, I.1    Steipe, B.2    Huber, R.3    Tomschy, A.4    Jaenicke, R.5
  • 33
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis P. J. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallog. 24:1991;946-950.
    • (1991) J. Appl. Crystallog. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 34
    • 0020490602 scopus 로고
    • Quantitation of aromatic residues in proteins: Model compounds for second-derivative spectroscopy
    • Levine R. L., Federici M. M. Quantitation of aromatic residues in proteins: model compounds for second-derivative spectroscopy. Biochemistry. 21:1982;2600-2606.
    • (1982) Biochemistry , vol.21 , pp. 2600-2606
    • Levine, R.L.1    Federici, M.M.2
  • 35
    • 0030748521 scopus 로고    scopus 로고
    • The crystal structure of an Fe-superoxide dismutase from the hyperthermophile Aquifex pyrophilus at 1.9 Å resolution: Structural basis for thermostability
    • Lim J., Yu Y. G., Han Y. S., Cho S., Ahn B., Kim S., Cho Y. The crystal structure of an Fe-superoxide dismutase from the hyperthermophile Aquifex pyrophilus at 1.9 Å resolution: structural basis for thermostability. J. Mol. Biol. 270:1997;259-274.
    • (1997) J. Mol. Biol. , vol.270 , pp. 259-274
    • Lim, J.1    Yu, Y.G.2    Han, Y.S.3    Cho, S.4    Ahn, B.5    Kim, S.6    Cho, Y.7
  • 36
    • 0027255479 scopus 로고
    • Structural and genetic analysis of protein stability
    • Matthews B. W. Structural and genetic analysis of protein stability. Annu. Rev. Biochem. 62:1993;139-160.
    • (1993) Annu. Rev. Biochem. , vol.62 , pp. 139-160
    • Matthews, B.W.1
  • 37
    • 0031565980 scopus 로고    scopus 로고
    • Disruption of an ionic network leads to accelerated thermal denaturation of D -glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic bacterium Thermotoga maritima
    • Pappenberger G., Schurig H., Jaenicke R. Disruption of an ionic network leads to accelerated thermal denaturation of D -glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic bacterium Thermotoga maritima. J. Mol. Biol. 274:1997;676-683.
    • (1997) J. Mol. Biol. , vol.274 , pp. 676-683
    • Pappenberger, G.1    Schurig, H.2    Jaenicke, R.3
  • 38
    • 0019324517 scopus 로고
    • Calibration of stopped-flow spectrophotometers using a two-step disulfide exchange reaction
    • Paul C., Kirschner K., Haenisch G. Calibration of stopped-flow spectrophotometers using a two-step disulfide exchange reaction. Anal. Biochem. 101:1980;442-448.
    • (1980) Anal. Biochem. , vol.101 , pp. 442-448
    • Paul, C.1    Kirschner, K.2    Haenisch, G.3
  • 39
    • 0016771835 scopus 로고
    • Stereochemical basis of heat stability in bacterial ferredoxins and in haemoglobin A2
    • Perutz M. F., Raidt H. Stereochemical basis of heat stability in bacterial ferredoxins and in haemoglobin A2. Nature. 255:1975;256-259.
    • (1975) Nature , vol.255 , pp. 256-259
    • Perutz, M.F.1    Raidt, H.2
  • 40
    • 0031816805 scopus 로고    scopus 로고
    • A protein disulfide oxidoreductase from the archaeon Pyrococcus furiosus contains two thioredoxin fold units
    • Ren B., Tibbelin G., de Pascale D., Rossi M., Bartolucci S., Ladenstein R. A protein disulfide oxidoreductase from the archaeon Pyrococcus furiosus contains two thioredoxin fold units. Nature Struct. Biol. 5:1998;602-611.
    • (1998) Nature Struct. Biol. , vol.5 , pp. 602-611
    • Ren, B.1    Tibbelin, G.2    De Pascale, D.3    Rossi, M.4    Bartolucci, S.5    Ladenstein, R.6
  • 41
    • 0030741375 scopus 로고    scopus 로고
    • The crystal structure of citrate synthase from the hyperthermophilic archaeon Pyrococcus furiosus at 1.9 Å resolution
    • Russell R. J. M., Ferguson J. M. C., Hough D. W., Danson M. J., Taylor G. L. The crystal structure of citrate synthase from the hyperthermophilic archaeon Pyrococcus furiosus at 1.9 Å resolution. Biochemistry. 36:1997;9983-9994.
    • (1997) Biochemistry , vol.36 , pp. 9983-9994
    • Russell, R.J.M.1    Ferguson, J.M.C.2    Hough, D.W.3    Danson, M.J.4    Taylor, G.L.5
  • 43
    • 0025325983 scopus 로고
    • The "megaprimer" method of site-directed mutagenesis
    • Sarkar G., Sommer S. S. The "megaprimer" method of site-directed mutagenesis. BioTechniques. 8:1990;404-407.
    • (1990) BioTechniques , vol.8 , pp. 404-407
    • Sarkar, G.1    Sommer, S.S.2
  • 44
    • 0005014890 scopus 로고
    • Procedure for production of hybrid genes and proteins and its use in assessing significance of amino acid differences in homologous tryptophan synthetase α polypeptides
    • Schneider W. P., Nichols B. P., Yanofsky C. Procedure for production of hybrid genes and proteins and its use in assessing significance of amino acid differences in homologous tryptophan synthetase α polypeptides. Proc. Natl Acad. Sci. USA. 78:1981;2169-2173.
    • (1981) Proc. Natl Acad. Sci. USA , vol.78 , pp. 2169-2173
    • Schneider, W.P.1    Nichols, B.P.2    Yanofsky, C.3
  • 45
    • 0032488654 scopus 로고    scopus 로고
    • Energetics of polar side-chain interactions in helical peptides: Salt effects of ion pairs and hydrogen bonds
    • Smith J. S., Scholtz J. M. Energetics of polar side-chain interactions in helical peptides: salt effects of ion pairs and hydrogen bonds. Biochemistry. 37:1998;33-40.
    • (1998) Biochemistry , vol.37 , pp. 33-40
    • Smith, J.S.1    Scholtz, J.M.2
  • 47
    • 0029912086 scopus 로고    scopus 로고
    • Phosphoribosyl anthranilate isomerase from Thermotoga maritima is an extremely stable and active homodimer
    • Sterner R., Kleemann G. R., Szadkowski H., Lustig A., Hennig M., Kirschner K. Phosphoribosyl anthranilate isomerase from Thermotoga maritima is an extremely stable and active homodimer. Protein Sci. 5:1996;2000-2008.
    • (1996) Protein Sci. , vol.5 , pp. 2000-2008
    • Sterner, R.1    Kleemann, G.R.2    Szadkowski, H.3    Lustig, A.4    Hennig, M.5    Kirschner, K.6
  • 48
    • 0000926770 scopus 로고
    • System for high-level production in Escherichia coli and rapid purification of recombinant proteins: Application to epitope mapping, preparation of antibodies, and structure-function analysis
    • I. Lefkovits, & B. Pernis. New York: Academic Press Inc.
    • Stüber D., Matile H., Garotta G. System for high-level production in Escherichia coli and rapid purification of recombinant proteins: application to epitope mapping, preparation of antibodies, and structure-function analysis. Lefkovits I., Pernis B. Immunological Methods. 1990;121-152 Academic Press Inc. New York.
    • (1990) Immunological Methods , pp. 121-152
    • Stüber, D.1    Matile, H.2    Garotta, G.3
  • 49
    • 0029893110 scopus 로고    scopus 로고
    • Thermozymes: Identifying molecular determinants of protein structural and functional stability
    • Vielle C., Zeikus J. G. Thermozymes: identifying molecular determinants of protein structural and functional stability. Trends Biotechnol. 14:1996;183-197.
    • (1996) Trends Biotechnol. , vol.14 , pp. 183-197
    • Vielle, C.1    Zeikus, J.G.2
  • 50
    • 0032539795 scopus 로고    scopus 로고
    • The crystal structure of Pyrococcus furiosus ornithine carbamoyltransferase reveals a key role for oligomerization in enzyme stability at extremely high temperatures
    • Villeret V., Clantin B., Tricot C., Legrain C., Roovers M., Stalon V., Glansdorff N., Van Beeumen J. The crystal structure of Pyrococcus furiosus ornithine carbamoyltransferase reveals a key role for oligomerization in enzyme stability at extremely high temperatures. Proc. Natl Acad. Sci. USA. 95:1998;2801-2806.
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 2801-2806
    • Villeret, V.1    Clantin, B.2    Tricot, C.3    Legrain, C.4    Roovers, M.5    Stalon, V.6    Glansdorff, N.7    Van Beeumen, J.8
  • 51
    • 0031567156 scopus 로고    scopus 로고
    • Crystal structures of Escherichia coli and Salmonella typhimurium 3-isopropylmalate dehydrogenase and comparison with their thermophilic counterpart from Thermus thermophilus
    • Wallon G., Kryger G., Lovett S. T., Oshima T., Ringe D., Petsko G. A. Crystal structures of Escherichia coli and Salmonella typhimurium 3-isopropylmalate dehydrogenase and comparison with their thermophilic counterpart from Thermus thermophilus. J. Mol. Biol. 266:1997;1016-1031.
    • (1997) J. Mol. Biol. , vol.266 , pp. 1016-1031
    • Wallon, G.1    Kryger, G.2    Lovett, S.T.3    Oshima, T.4    Ringe, D.5    Petsko, G.A.6
  • 52
    • 0000783701 scopus 로고    scopus 로고
    • The trp operon and tryptophan biosynthesis in Escherichia coli and Salmonella typhimurium
    • T. E. Creighton. New York: Wiley & Sons, Inc.
    • Yanofsky C., Miles E. C., Bauerle R., Kirschner K. The trp operon and tryptophan biosynthesis in Escherichia coli and Salmonella typhimurium. Creighton T. E. The Encyclopedia of Molecular Biology. 1998;Wiley & Sons, Inc. New York.
    • (1998) The Encyclopedia of Molecular Biology
    • Yanofsky, C.1    Miles, E.C.2    Bauerle, R.3    Kirschner, K.4


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