메뉴 건너뛰기




Volumn 266, Issue 5, 1997, Pages 1016-1031

Crystal structures of Escherichia coli and Salmonella typhimurium 3-isopropylmalate dehydrogenase and comparison with their thermophilic counterpart from Thermus thermophilus

Author keywords

3 isopropylmalate dehydrogenase; Crystal structure; Escherichia coli; Salmonella typhimurium; Thermal stability

Indexed keywords

3 ISOPROPYLMALATE DEHYDROGENASE;

EID: 0031567156     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1996.0797     Document Type: Article
Times cited : (130)

References (54)
  • 1
    • 0025327584 scopus 로고
    • Protein stability and electrostatic interactions between solvent exposed charged side chains
    • Akke, M. & Forsen, S. (1990). Protein stability and electrostatic interactions between solvent exposed charged side chains. Proteins: Struct. Funct. Genet. 8, 23-29.
    • (1990) Proteins: Struct. Funct. Genet. , vol.8 , pp. 23-29
    • Akke, M.1    Forsen, S.2
  • 2
  • 4
    • 85030285333 scopus 로고
    • The free R.-value: A novel statistical approach for assessing the accuracy of crystal structures
    • Brüenger, A. T. (1992). The free R.-value: a novel statistical approach for assessing the accuracy of crystal structures. Nature, 249, 267-270.
    • (1992) Nature , vol.249 , pp. 267-270
    • Brüenger, A.T.1
  • 5
    • 0023140814 scopus 로고
    • Crystallographic R.-factor refinement by molecular dynamics
    • Brüenger, A. T., Kuriyan, J. & Karplus, M. (1987). Crystallographic R.-factor refinement by molecular dynamics. Sciences, 235, 458-460.
    • (1987) Sciences , vol.235 , pp. 458-460
    • Brüenger, A.T.1    Kuriyan, J.2    Karplus, M.3
  • 6
    • 0022419375 scopus 로고
    • Aromatic-aromatic interaction: A mechanism of protein stabilization
    • Burley, S. K. & Petsko, G. A. (1985). Aromatic-aromatic interaction: a mechanism of protein stabilization. Science, 229, 23-28.
    • (1985) Science , vol.229 , pp. 23-28
    • Burley, S.K.1    Petsko, G.A.2
  • 7
    • 0027219504 scopus 로고
    • Protein unfolding pathways explored through molecular dynamics simulations
    • Daggett, V. & Levitt, M. (1993). Protein unfolding pathways explored through molecular dynamics simulations. J. Mol. Biol. 232, 600-619.
    • (1993) J. Mol. Biol. , vol.232 , pp. 600-619
    • Daggett, V.1    Levitt, M.2
  • 8
    • 0027383273 scopus 로고
    • Kinetic mechanism of Escherichia coli isocitrate dehydrogenase
    • Dean, A. M. & Koshland, D. E. Jr. (1993). Kinetic mechanism of Escherichia coli isocitrate dehydrogenase. Biochemistry, 32, 9302-9309.
    • (1993) Biochemistry , vol.32 , pp. 9302-9309
    • Dean, A.M.1    Koshland D.E., Jr.2
  • 9
    • 0029020484 scopus 로고
    • N- and C-capping preferences for all 20 amino acids in α-helical peptides
    • Doig, A. J. & Baldwin, R. L. (1995). N-and C-capping preferences for all 20 amino acids in α-helical peptides. Protein Sci. 4, 1325-1336.
    • (1995) Protein Sci. , vol.4 , pp. 1325-1336
    • Doig, A.J.1    Baldwin, R.L.2
  • 10
    • 0026567907 scopus 로고
    • Response of a protein structure to cavity-creating mutations and its relatin to the hydrophobic effect
    • Erikson, A. E., Baase, W. A., Zhang, X.-J., Heinz, D. W., Blaber, M., Baldwin, E. P. & Matthews, B. W. (1992). Response of a protein structure to cavity-creating mutations and its relatin to the hydrophobic effect. Science, 255, 178-183.
    • (1992) Science , vol.255 , pp. 178-183
    • Erikson, A.E.1    Baase, W.A.2    Zhang, X.-J.3    Heinz, D.W.4    Blaber, M.5    Baldwin, E.P.6    Matthews, B.W.7
  • 11
    • 0027462173 scopus 로고
    • Principles in protein stability derived from protein engineering experiments
    • Fersht, A. R. & Serrano, L. (1993). Principles in protein stability derived from protein engineering experiments. Curr. Opin. Struct. Biol. 3, 75-83.
    • (1993) Curr. Opin. Struct. Biol. , vol.3 , pp. 75-83
    • Fersht, A.R.1    Serrano, L.2
  • 12
    • 0027491528 scopus 로고
    • Refined crystal structure of the seryl-tRNA synthetase from Thermus thermophilus at 2.5 Å resolution
    • Fujinaga, M., Berthet-Colominas, C., Yaremchuck, A. D., Tukalo, M. A. & Cusack, S. (1993). Refined crystal structure of the seryl-tRNA synthetase from Thermus thermophilus at 2.5 Å resolution. J. Mol. Biol. 234, 222-233.
    • (1993) J. Mol. Biol. , vol.234 , pp. 222-233
    • Fujinaga, M.1    Berthet-Colominas, C.2    Yaremchuck, A.D.3    Tukalo, M.A.4    Cusack, S.5
  • 13
    • 0028107325 scopus 로고
    • The effect of engineering surface loops on the thermal stability of Bacillus subtilis neutral protease
    • Hardy, F., Vriend, G., van der Vinne, B., Frigerio, F., Grandi, G., Venema, G. & Eijsink, V. G. H. (1994). The effect of engineering surface loops on the thermal stability of Bacillus subtilis neutral protease. Protein Eng. 7, 425-430.
    • (1994) Protein Eng. , vol.7 , pp. 425-430
    • Hardy, F.1    Vriend, G.2    Van Der Vinne, B.3    Frigerio, F.4    Grandi, G.5    Venema, G.6    Eijsink, V.G.H.7
  • 14
    • 0029881741 scopus 로고    scopus 로고
    • A stable intermediate in the thermal unfolding process of a chimeric 3-isopropylmalate dehydrogenase between a thermophilic and a mesophilic enzyme
    • Hayashi-Iwasaki, Y., Numata, K., Yamagishi, A., Yutani, K., Sakkurai, M., Tanaka, N. & Oshima, T. A. (1996). A stable intermediate in the thermal unfolding process of a chimeric 3-isopropylmalate dehydrogenase between a thermophilic and a mesophilic enzyme. Protein Sci. 5, 511-516.
    • (1996) Protein Sci. , vol.5 , pp. 511-516
    • Hayashi-Iwasaki, Y.1    Numata, K.2    Yamagishi, A.3    Yutani, K.4    Sakkurai, M.5    Tanaka, N.6    Oshima, T.A.7
  • 15
    • 0028204490 scopus 로고
    • Do salt bridges stabilize proteins? A continuum electrostatic analysis
    • Hendsch, Z. S. & Tidor, B. (1994). Do salt bridges stabilize proteins? A continuum electrostatic analysis. Protein Sci. 3, 211-226.
    • (1994) Protein Sci. , vol.3 , pp. 211-226
    • Hendsch, Z.S.1    Tidor, B.2
  • 16
    • 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. (1995). 2.0 Å structure of indole-3-glycerol phosphate synthase from the hyperthermophile Sulfolobus solfataricus: possible determinants of protein stability. Structure, 3, 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
  • 17
    • 0026714968 scopus 로고
    • Role of proline residues in human lysozyme stability: A scanning calorimetric study combined with X-ray structure analysis of proline mutants
    • Herning, T., Yutani, K., Inaka, K., Kuroki, R., Matsuhima, M. & Kikuchi, M. (1992). Role of proline residues in human lysozyme stability: a scanning calorimetric study combined with X-ray structure analysis of proline mutants. Biochemistry, 31, 7077-7085.
    • (1992) Biochemistry , vol.31 , pp. 7077-7085
    • Herning, T.1    Yutani, K.2    Inaka, K.3    Kuroki, R.4    Matsuhima, M.5    Kikuchi, M.6
  • 18
    • 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. (1990). Strength and co-operativity of contributions of surface salt bridges to protein stability. J. Mol. Biol. 216, 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
  • 19
    • 0028607523 scopus 로고
    • Cavities and packing at protein interfaces
    • Hubbard, S. J. & Argos, P. (1994). Cavities and packing at protein interfaces. Protein Sci. 3, 2194-2206.
    • (1994) Protein Sci. , vol.3 , pp. 2194-2206
    • Hubbard, S.J.1    Argos, P.2
  • 20
    • 0028274954 scopus 로고
    • Intramolecular cavities in globular proteins
    • Hubbard, S. J., Gross, K.-H. & Argos, P. (1994). Intramolecular cavities in globular proteins. Protein Eng. 7, 613-626.
    • (1994) Protein Eng. , vol.7 , pp. 613-626
    • Hubbard, S.J.1    Gross, K.-H.2    Argos, P.3
  • 23
    • 0026334204 scopus 로고
    • Three-dimensional structure of a highly thermostable enzyme, 3-isopropylmalate dehydrogenase from Thermus thermophilus at 22 Å resolution
    • Imada, K., Sato, M., Tanaka, N., Katsube, Y., Matsuura, Y. & Oshima, T. (1991). Three-dimensional structure of a highly thermostable enzyme, 3-isopropylmalate dehydrogenase from Thermus thermophilus at 22 Å resolution. J. Mol. Biol. 222, 725-738.
    • (1991) J. Mol. Biol. , vol.222 , pp. 725-738
    • Imada, K.1    Sato, M.2    Tanaka, N.3    Katsube, Y.4    Oshima, T.5
  • 24
    • 0027384577 scopus 로고
    • Effect of cavity creating mutations in the hydrophobic core of chymotrypsin inhibitor 2
    • Jackson, S. E., Moracci, M., erMasry, H., Johnson, C. M. & Fersht, A. R. (1993). Effect of cavity creating mutations in the hydrophobic core of chymotrypsin inhibitor 2. Biochemistry, 32, 11259-11269.
    • (1993) Biochemistry , vol.32 , pp. 11259-11269
    • Jackson, S.E.1    Moracci, M.2    Ermasry, H.3    Johnson, C.M.4    Fersht, A.R.5
  • 25
    • 0028853604 scopus 로고
    • Ligand-induced changes in the conformation of 3-isopropylmalate dehydrogenase from Thermus thermophilus
    • Kadono, S., Sakurai, M., Moriyama, H., Sato, M., Hayashi, Y., Oshima, T. & Tanaka, N. (1995). Ligand-induced changes in the conformation of 3-isopropylmalate dehydrogenase from Thermus thermophilus. J. Biochem. 118, 745-752.
    • (1995) J. Biochem. , vol.118 , pp. 745-752
    • Kadono, S.1    Sakurai, M.2    Moriyama, H.3    Sato, M.4    Hayashi, Y.5    Oshima, T.6    Tanaka, N.7
  • 26
    • 0028091179 scopus 로고
    • Hydrophobic interaction at the subunit interface contributes to the thermostability of 3-isopropylmalate dehydrogenase from an extreme thermophile, Thermus thermophilus
    • Kirino, H., Aoki, M., Aoshima, M., Hayashi, Y., Ohba, M., Yamagishi, A., Wakagi, T. & Oshima, T. (1994). Hydrophobic interaction at the subunit interface contributes to the thermostability of 3-isopropylmalate dehydrogenase from an extreme thermophile, Thermus thermophilus. Eur. J. Biochem. 200, 275-281.
    • (1994) Eur. J. Biochem. , vol.200 , pp. 275-281
    • Kirino, H.1    Aoki, M.2    Aoshima, M.3    Hayashi, Y.4    Ohba, M.5    Yamagishi, A.6    Wakagi, T.7    Oshima, T.8
  • 27
    • 0002700643 scopus 로고
    • Halloween... Masks and bones
    • Bailey, S., Hubbard, R. & Waller, D., eds, pp. SERC Daresbury Laboratory, Warrington, UK
    • Kleywegt, G. A. & Jones, T. A. (1994a). Halloween... masks and bones. In From First Map to Final Model (Bailey, S., Hubbard, R. & Waller, D., eds), pp. 59-66, SERC Daresbury Laboratory, Warrington, UK.
    • (1994) From First Map to Final Model , pp. 59-66
    • Kleywegt, G.A.1    Jones, T.A.2
  • 28
    • 0027995683 scopus 로고
    • Detection, delineation, measurement and display of cavities in macromolecular structures
    • Kleywegt, G. J. & Jones, A. T. (1994b). Detection, delineation, measurement and display of cavities in macromolecular structures. Acta Crystallog sect. D, 50, 178-185.
    • (1994) Acta Crystallog Sect. D , vol.50 , pp. 178-185
    • Kleywegt, G.J.1    Jones, A.T.2
  • 29
    • 0028903461 scopus 로고
    • The crystal structure of hologlyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic bacterium Thermotoga maritima at 2.5 Å resolution
    • Korndörfer, I., Steipe, B., Huber, R., Tomschy, A. & Jaenicke, R. (1995). The crystal structure of hologlyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic bacterium Thermotoga maritima at 2.5 Å resolution. J. Mol. Biol. 246, 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
  • 30
    • 0030028478 scopus 로고    scopus 로고
    • Further stabilization of 3-isopropylmalate dehydrogease of an extreme thermophile, Thermus thermophilus, by a supressor mutation method
    • 1996
    • Kotsuka, T., Akanuma, S., Tomuro, M., Yamagishi, A. & Oshima, T. (1996). Further stabilization of 3-isopropylmalate dehydrogease of an extreme thermophile, Thermus thermophilus, by a supressor mutation method. J. Bacteriol. (1996) 178, 723-727.
    • (1996) J. Bacteriol. , vol.178 , pp. 723-727
    • Kotsuka, T.1    Akanuma, S.2    Tomuro, M.3    Yamagishi, A.4    Oshima, T.5
  • 31
    • 0028863090 scopus 로고
    • Revision of the amino acid sequence of 3-isopropylmalate dehydrogenase from Salmonella typhimurium by means of X-ray crystallography
    • Kryger, G., Wallon, G., Lovett, S. T., Ringe, D. & Petsko, G. A. (1995). Revision of the amino acid sequence of 3-isopropylmalate dehydrogenase from Salmonella typhimurium by means of X-ray crystallography. Gene, 164, 85-87.
    • (1995) Gene , vol.164 , pp. 85-87
    • Kryger, G.1    Wallon, G.2    Lovett, S.T.3    Ringe, D.4    Petsko, G.A.5
  • 32
    • 2642699794 scopus 로고
    • Rapid and efficient site-specific mutagenesis without phenotypic selection
    • Kunkel, T. A. (1985). Rapid and efficient site-specific mutagenesis without phenotypic selection. Proc. Natl Acad. Sci. USA, 82, 488-492.
    • (1985) Proc. Natl Acad. Sci. USA , vol.82 , pp. 488-492
    • Kunkel, T.A.1
  • 33
    • 0027522362 scopus 로고
    • Estimation of the maximum change in stability of globular proteins upon mutation of a hydrophobic residue to another of smaller size
    • Lee, B. (1993). Estimation of the maximum change in stability of globular proteins upon mutation of a hydrophobic residue to another of smaller size. Protein Sci, 2, 733-738.
    • (1993) Protein Sci , vol.2 , pp. 733-738
    • Lee, B.1
  • 35
    • 0022981913 scopus 로고
    • Loops in globular proteins: A novel category of secondary structure
    • Leszczynski, J. & Rose, G. D. (1986). Loops in globular proteins: a novel category of secondary structure. Science, 234, 849-855.
    • (1986) Science , vol.234 , pp. 849-855
    • Leszczynski, J.1    Rose, G.D.2
  • 36
    • 0026766573 scopus 로고
    • Structural and energetic consequences of disruptive mutations in a protein core
    • Lim, W. A., Farruggio, D. C. & Sauer, R. T. (1992). Structural and energetic consequences of disruptive mutations in a protein core. Biochemistry, 31, 4324-4333.
    • (1992) Biochemistry , vol.31 , pp. 4324-4333
    • Lim, W.A.1    Farruggio, D.C.2    Sauer, R.T.3
  • 37
    • 0023430560 scopus 로고
    • Enhanced protein thermostability from site-directed mutations that decrease the entropy of unfolding
    • Matthews, B. W., Nicholson, H. & Becktel, W. J. (1987). Enhanced protein thermostability from site-directed mutations that decrease the entropy of unfolding. Proc. Natl Acad. Sci. USA, 84, 6663-6667.
    • (1987) Proc. Natl Acad. Sci. USA , vol.84 , pp. 6663-6667
    • Matthews, B.W.1    Nicholson, H.2    Becktel, W.J.3
  • 38
    • 0002351177 scopus 로고
    • AMoRE: A new package for molecular replacement
    • Dodson, E. J., Gover, S. & Wolfe, W., eds, SERC Daresbury Laboratory, Warrington, UK
    • Navaza, J. (1992). AMoRE: a new package for molecular replacement. In Molecular Replacement (Dodson, E. J., Gover, S. & Wolfe, W., eds), pp. 87-90. SERC Daresbury Laboratory, Warrington, UK.
    • (1992) Molecular Replacement , pp. 87-90
    • Navaza, J.1
  • 39
    • 0017706821 scopus 로고
    • Reversible thermal unfolding of thermostable phosphoglycerate kinase. Thermostability associated with mean zero enthalpy change
    • Nojima, H., Ikai, A., Oshima, T. & Noda, H. (1977). Reversible thermal unfolding of thermostable phosphoglycerate kinase. Thermostability associated with mean zero enthalpy change. J. Mol. Biol. 116, 429-442.
    • (1977) J. Mol. Biol. , vol.116 , pp. 429-442
    • Nojima, H.1    Ikai, A.2    Oshima, T.3    Noda, H.4
  • 40
    • 0021191208 scopus 로고
    • Fluctuations in protein structure from X-ray diffraction
    • Petsko, G. A. & Ringe, D. (1984). Fluctuations in protein structure from X-ray diffraction. Annu. Rev. Biophys. Bioeng. 13, 331-371.
    • (1984) Annu. Rev. Biophys. Bioeng. , vol.13 , pp. 331-371
    • Petsko, G.A.1    Ringe, D.2
  • 41
    • 0024290472 scopus 로고
    • Amino acid preferences for specific locations at the ends of α-helices
    • Richardson, J. S. & Richardson, D. C. (1988). Amino acid preferences for specific locations at the ends of α-helices. Science, 240, 1648-1642.
    • (1988) Science , vol.240 , pp. 1648-11642
    • Richardson, J.S.1    Richardson, D.C.2
  • 42
    • 0027256739 scopus 로고
    • Hydrogen bonding, hydrophobicity, packing, and protein folding
    • Rose, G. D. & Wolfenden, R. (1993). Hydrogen bonding, hydrophobicity, packing, and protein folding. Annu. Rev. Biomol. Struct. 22, 381-415.
    • (1993) Annu. Rev. Biomol. Struct. , vol.22 , pp. 381-415
    • Rose, G.D.1    Wolfenden, R.2
  • 43
    • 0028774720 scopus 로고
    • The crystal structure of citrate synthase from the thermophilic archeon Thermoplasma acidophilum
    • Russell, R. J. M., Hough, D. W., Danson, M. J. & Taylor, G. L. (1994). The crystal structure of citrate synthase from the thermophilic archeon Thermoplasma acidophilum. Structure, 2, 1157-1167.
    • (1994) Structure , vol.2 , pp. 1157-1167
    • Russell, R.J.M.1    Hough, D.W.2    Danson, M.J.3    Taylor, G.L.4
  • 44
    • 0024972479 scopus 로고
    • Capping and α-helix stability
    • Serrano, L. & Fersht, A. R. (1989). Capping and α-helix stability. Nature, 342, 296-299.
    • (1989) Nature , vol.342 , pp. 296-299
    • Serrano, L.1    Fersht, A.R.2
  • 45
    • 0026654252 scopus 로고
    • Mutational studies of protein structures and their stabilities
    • Shortle, D. (1992). Mutational studies of protein structures and their stabilities. Quart. Rev. Biophys. 25, 205-250.
    • (1992) Quart. Rev. Biophys. , vol.25 , pp. 205-250
    • Shortle, D.1
  • 46
    • 0027494760 scopus 로고
    • Structure of isocitrate dehydrogenase with isocitrate, nicotinamide adenine dinucleotide phosphate, and calcium at 2.5-Å resolution: A pseudo-Michaelis ternary complex
    • Stoddard, B. L., Dean, A. M. & Koshland, D. E. (1993). Structure of isocitrate dehydrogenase with isocitrate, nicotinamide adenine dinucleotide phosphate, and calcium at 2.5-Å resolution: a pseudo-Michaelis ternary complex. Biochemistry, 32, 9310-9316.
    • (1993) Biochemistry , vol.32 , pp. 9310-9316
    • Stoddard, B.L.1    Dean, A.M.2    Koshland, D.E.3
  • 47
    • 0028786432 scopus 로고
    • Contribution of hydrophobic residues to the stability of human lysozyme: Calorimetric studies and X-ray structural analysis of the five isoleucine to valine mutants
    • Takano, K., Ogasahara, K., Kaneda, H., Yamagata, Y., Fujii, S., Kanaya, E., Kikuchi, M., Oobatake, M. & Yutani, K. (1995). Contribution of hydrophobic residues to the stability of human lysozyme: calorimetric studies and X-ray structural analysis of the five isoleucine to valine mutants. J. Mol. Biol. 254, 62-76.
    • (1995) J. Mol. Biol. , vol.254 , pp. 62-76
    • Takano, K.1    Ogasahara, K.2    Kaneda, H.3    Yamagata, Y.4    Fujii, S.5    Kanaya, E.6    Kikuchi, M.7    Oobatake, M.8    Yutani, K.9
  • 48
    • 0028586827 scopus 로고
    • The effect of ion pairs on the thermal stability of D-glyceraldehyde 3-phosphate dehydrogenase from the hyperthermophilic bacterium Thermotoga maritima
    • Tomschy, A., Böhm, G. & Jaenicke, R. (1994). The effect of ion pairs on the thermal stability of D-glyceraldehyde 3-phosphate dehydrogenase from the hyperthermophilic bacterium Thermotoga maritima. Protein Eng. 7, 1471-1478.
    • (1994) Protein Eng. , vol.7 , pp. 1471-1478
    • Tomschy, A.1    Böhm, G.2    Jaenicke, R.3
  • 49
    • 0029564595 scopus 로고
    • Are buried salt bridges important for protein stability and conformational specificity
    • Waldburger, C. D., Schildbach, J. F. & Sauer, R. T. (1995). Are buried salt bridges important for protein stability and conformational specificity. Nature Struct. Biol. 2, 122-128.
    • (1995) Nature Struct. Biol. , vol.2 , pp. 122-128
    • Waldburger, C.D.1    Schildbach, J.F.2    Sauer, R.T.3
  • 51
    • 0002458980 scopus 로고
    • Pressure points in the biosynthetic pathway for branched amino-acids
    • Singh, B. K., Flores, H. E. & Shannon, J. C., eds, American Society of Plant Physiologists, Rockville, MD
    • Wittenbach, V., Rayner, D. & Schloss, J. (1992). Pressure points in the biosynthetic pathway for branched amino-acids. In Biosynthesis and Molecular Regulation of Amino Acids in Plants (Singh, B. K., Flores, H. E. & Shannon, J. C., eds), pp. 69-88, American Society of Plant Physiologists, Rockville, MD.
    • (1992) Biosynthesis and Molecular Regulation of Amino Acids in Plants , pp. 69-88
    • Wittenbach, V.1    Rayner, D.2    Schloss, J.3
  • 52
    • 0025108577 scopus 로고
    • Purification, catalytic properties and thermal stability of threo-Ds-3-isopropylmalate dehydrogenase coded by leuB gene from an extreme thermophile, Thermus thermophilus strain HB8
    • Yamada, T., Akutsu, N., Miyazaki, K., Kakinuma, K., Yoshida, M. & Oshima, T. (1990). Purification, catalytic properties and thermal stability of threo-Ds-3-isopropylmalate dehydrogenase coded by leuB gene from an extreme thermophile, Thermus thermophilus strain HB8. J. Biochem. 108, 449-456.
    • (1990) J. Biochem. , vol.108 , pp. 449-456
    • Yamada, T.1    Akutsu, N.2    Miyazaki, K.3    Kakinuma, K.4    Yoshida, M.5    Oshima, T.6
  • 53
    • 13244249836 scopus 로고
    • The structure of Pyrococcus furiosus glutamate dehydrogenase reveals a key role for ion-pair networks in maintaining enzyme stability at extreme temperatures
    • P. J., B., S. E., S.
    • Yip, K. S. P., Stillman, T. J., Britton, K. L., Artymuik, P. J., P. J., B., S. E., S., Engel, P. C., Pasquo, A., Chiraluce, R., Consalvi, V., Scandurra, R. & Rice, D. W. (1995). The structure of Pyrococcus furiosus glutamate dehydrogenase reveals a key role for ion-pair networks in maintaining enzyme stability at extreme temperatures. Structure, 3, 1147-1158.
    • (1995) Structure , vol.3 , pp. 1147-1158
    • Yip, K.S.P.1    Stillman, T.J.2    Britton, K.L.3    Artymuik, P.J.4    Engel, P.C.5    Pasquo, A.6    Chiraluce, R.7    Consalvi, V.8    Scandurra, R.9    Rice, D.W.10
  • 54
    • 0028901535 scopus 로고
    • Modeling substrate binding in Thermus thermophilus isopropylmalate dehydrogenase
    • Zhang, T. & Koshland, D. E. (1995). Modeling substrate binding in Thermus thermophilus isopropylmalate dehydrogenase. Protein Sci., 84-92.
    • (1995) Protein Sci. , pp. 84-92
    • Zhang, T.1    Koshland, D.E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.