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Volumn 244, Issue 2, 1997, Pages 646-652

Examination of the thiamin diphosphate binding site in yeast transketolase by site-directed mutagenesis

Author keywords

Enzyme mechanism; Protein crystallography; Site directed mutagenesis; Thiamin diphosphate; Transketolase

Indexed keywords

COCARBOXYLASE; TRANSKETOLASE;

EID: 0031039575     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1997.t01-1-00646.x     Document Type: Article
Times cited : (42)

References (35)
  • 1
    • 85027779617 scopus 로고
    • A system for collection and on-line integration of X-ray diffraction data from a multiwire area detector
    • Blum, M., Metcalf, P., Harrison, S. C. & Wiley, D. C. (1987) A system for collection and on-line integration of X-ray diffraction data from a multiwire area detector, J. Appl. Crystallogr. 20, 235-242.
    • (1987) J. Appl. Crystallogr. , vol.20 , pp. 235-242
    • Blum, M.1    Metcalf, P.2    Harrison, S.C.3    Wiley, D.C.4
  • 2
    • 0027369409 scopus 로고
    • Reconstitution of holotransketolase is by a thiamin-diphosphate-magnesium complex
    • Booth, C. K. & Nixon, P. F. (1993) Reconstitution of holotransketolase is by a thiamin-diphosphate-magnesium complex, Eur. J. Biochem. 218, 261-265.
    • (1993) Eur. J. Biochem. , vol.218 , pp. 261-265
    • Booth, C.K.1    Nixon, P.F.2
  • 3
    • 0002208132 scopus 로고
    • Crystallographic refinement by simulated annealing: Application to crambin
    • Brünger, A. T., Karplus, M. & Petsko, G. A. (1989) Crystallographic refinement by simulated annealing: application to crambin, Acta Crystallogr. A45, 50-61.
    • (1989) Acta Crystallogr. , vol.A45 , pp. 50-61
    • Brünger, A.T.1    Karplus, M.2    Petsko, G.A.3
  • 4
    • 0026597444 scopus 로고
    • Free R value: A novel statistical quantity for assessing the accuracy of crystal structures
    • Brünger, A. T. (1992) Free R value: a novel statistical quantity for assessing the accuracy of crystal structures, Nature 355, 472-475.
    • (1992) Nature , vol.355 , pp. 472-475
    • Brünger, A.T.1
  • 5
    • 8044227457 scopus 로고
    • Rapid sequencing of plasmid DNA directly from colonies of Saccharomvces cerevisiae
    • Caldwell, G. A. & Becker, J. M. (1993) Rapid sequencing of plasmid DNA directly from colonies of Saccharomvces cerevisiae, Promega Notes 44, 6-9.
    • (1993) Promega Notes , vol.44 , pp. 6-9
    • Caldwell, G.A.1    Becker, J.M.2
  • 6
    • 0016726177 scopus 로고
    • Enzymes of pentose biosynthesis, the quaternary structure and reacting form of transketolase from baker's yeast
    • Cavalieri, S. W., Neet, K. E. & Sable, H. Z. (1975) Enzymes of pentose biosynthesis, The quaternary structure and reacting form of transketolase from baker's yeast, Arch. Biochem. Biophys. 171, 527-532.
    • (1975) Arch. Biochem. Biophys. , vol.171 , pp. 527-532
    • Cavalieri, S.W.1    Neet, K.E.2    Sable, H.Z.3
  • 7
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computing Project, Number 4 (1994) The CCP4 suite: programs for protein crystallography, Acta Crystallogr. D50, 760-763.
    • (1994) Acta Crystallogr. , vol.D50 , pp. 760-763
  • 8
    • 0026601458 scopus 로고
    • Site-directed mutagenesis of virtually any plasmid by eliminating a unique site
    • Deng, W. P. & Nickoloff, J. A. (1992) Site-directed mutagenesis of virtually any plasmid by eliminating a unique site, Anal. Biochem. 200, 81.
    • (1992) Anal. Biochem. , vol.200 , pp. 81
    • Deng, W.P.1    Nickoloff, J.A.2
  • 9
    • 0019888067 scopus 로고
    • Transketolase kinetics. The slow reconstitution of the holoenzyme is due to a rate-limiting dimerization of the subunits
    • Egan, R. M. & Sable, H. Z. (1981) Transketolase kinetics. The slow reconstitution of the holoenzyme is due to a rate-limiting dimerization of the subunits, J. Biol. Chem. 256, 4877-4883.
    • (1981) J. Biol. Chem. , vol.256 , pp. 4877-4883
    • Egan, R.M.1    Sable, H.Z.2
  • 10
    • 79952608525 scopus 로고
    • Accurate bond and angle parameters for X-ray protein structure refinement
    • Engh, R. A. & Huber, R. (1991) Accurate bond and angle parameters for X-ray protein structure refinement, Acta Crystallogr. A47, 392-400.
    • (1991) Acta Crystallogr. , vol.A47 , pp. 392-400
    • Engh, R.A.1    Huber, R.2
  • 11
    • 0024432768 scopus 로고
    • A common structural motif in thiamin pyrophosphate-binding enzymes
    • Hawkins, C. F., Borges, A. & Perham, R. N. (1989) A common structural motif in thiamin pyrophosphate-binding enzymes, FEBS Lett. 255, 77-82.
    • (1989) FEBS Lett. , vol.255 , pp. 77-82
    • Hawkins, C.F.1    Borges, A.2    Perham, R.N.3
  • 12
    • 0015515486 scopus 로고
    • Chemical modification of tryptophan at the binding site of thiamine pyrophosphate in transketolase from baker's yeast
    • Heinrich, P. C., Noack, K. & Wiss, O. (1972) Chemical modification of tryptophan at the binding site of thiamine pyrophosphate in transketolase from baker's yeast, Biochem. Biophys. Res. Commun. 49, 1427-1432.
    • (1972) Biochem. Biophys. Res. Commun. , vol.49 , pp. 1427-1432
    • Heinrich, P.C.1    Noack, K.2    Wiss, O.3
  • 14
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones, T. A., Zou, J.-Y., Cowan, S. & Kjeldgaard, M. (1991) Improved methods for building protein models in electron density maps and the location of errors in these models, Acta Crystallogr. A47, 110-119.
    • (1991) Acta Crystallogr. , vol.A47 , pp. 110-119
    • Jones, T.A.1    Zou, J.-Y.2    Cowan, S.3    Kjeldgaard, M.4
  • 15
    • 0000641606 scopus 로고
    • Thiamine pyrophosphate induced changes in the optical activity of baker's yeast transketolase
    • Kochetov, G. A., Usmanov, R. A. & Merzlov, V. P. (1970) Thiamine pyrophosphate induced changes in the optical activity of baker's yeast transketolase, FEBS Lett. 9, 265-266.
    • (1970) FEBS Lett. , vol.9 , pp. 265-266
    • Kochetov, G.A.1    Usmanov, R.A.2    Merzlov, V.P.3
  • 16
    • 0020393767 scopus 로고
    • Transketolase from yeast, rat liver and pig liver
    • Kochetov, G. A. (1982) Transketolase from yeast, rat liver and pig liver, Methods Enzymol. 90, 209-223.
    • (1982) Methods Enzymol. , vol.90 , pp. 209-223
    • Kochetov, G.A.1
  • 17
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P. J. (1991) MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures, J. Appl. Crystallogr. 24, 946-950.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 18
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski, R. A., McArthur, M. W., Moss, D. S. & Thornton, J. M. (1993) PROCHECK: a program to check the stereochemical quality of protein structures, J. Appl. Crystallogr. 26., 282-291.
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 282-291
    • Laskowski, R.A.1    McArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 19
    • 0026762799 scopus 로고
    • Three-dimensional structure of transketolase, a thiamine pyrophosphate containing enzyme at 2.5 Å resolution
    • Lindqvist, Y., Schneider, G., Ermler, U. & Sundström, M. (1992) Three-dimensional structure of transketolase, a thiamine pyrophosphate containing enzyme at 2.5 Å resolution, EMBO J. 11, 2373-2379.
    • (1992) EMBO J. , vol.11 , pp. 2373-2379
    • Lindqvist, Y.1    Schneider, G.2    Ermler, U.3    Sundström, M.4
  • 20
    • 0028057108 scopus 로고
    • Raster3D Version 2.0. A program for photorealistic molecular graphics
    • Merrit, E. A. & Murphy, M. E. P. (1994) Raster3D Version 2.0. A program for photorealistic molecular graphics, Acta Crystallogr. D50, 869-873.
    • (1994) Acta Crystallogr. , vol.D50 , pp. 869-873
    • Merrit, E.A.1    Murphy, M.E.P.2
  • 21
    • 0027918180 scopus 로고
    • A thiamin diphosphate binding fold revealed by comparison of the crystal structures of transketolase, pyruvate oxidase and pyruvate decarboxylase
    • Muller, Y. A., Lindqvist, Y., Furey, W., Schulz, G. E., Jordan, F. & Schneider, G. (1993) A thiamin diphosphate binding fold revealed by comparison of the crystal structures of transketolase, pyruvate oxidase and pyruvate decarboxylase, Structure 1, 95-103.
    • (1993) Structure , vol.1 , pp. 95-103
    • Muller, Y.A.1    Lindqvist, Y.2    Furey, W.3    Schulz, G.E.4    Jordan, F.5    Schneider, G.6
  • 23
    • 0028305456 scopus 로고
    • Cristallographic refinement of transketolase from Saccharomyces cerevisiae at 2.0 Å resolution
    • Nikkola, M., Lindqvist, Y. & Schneider, G. (1994) Cristallographic refinement of transketolase from Saccharomyces cerevisiae at 2.0 Å resolution, J. Mol. Biol. 238, 387-404.
    • (1994) J. Mol. Biol. , vol.238 , pp. 387-404
    • Nikkola, M.1    Lindqvist, Y.2    Schneider, G.3
  • 24
    • 0031029945 scopus 로고    scopus 로고
    • Examination of substrate binding in thiamin diphosphate dependent transketolase by protein crystallography and site-directed mutagenesis
    • Nilsson, U., Meshalkina, L., Lindqvist, Y. & Schneider, G. (1997) Examination of substrate binding in thiamin diphosphate dependent transketolase by protein crystallography and site-directed mutagenesis, J. Biol. Chem. 272, 1864-1869.
    • (1997) J. Biol. Chem. , vol.272 , pp. 1864-1869
    • Nilsson, U.1    Meshalkina, L.2    Lindqvist, Y.3    Schneider, G.4
  • 25
    • 0027196884 scopus 로고
    • Crystal structure of transketolase in complex with thiamine thiazolone diphosphate, an analogue of the reaction intermediate, at 2.3 Å resolution
    • Nilsson, U., Lindqvist, Y., Kluger, R. & Schneider, G. (1993) Crystal structure of transketolase in complex with thiamine thiazolone diphosphate, an analogue of the reaction intermediate, at 2.3 Å resolution, FEBS Lett. 326, 145-148.
    • (1993) FEBS Lett. , vol.326 , pp. 145-148
    • Nilsson, U.1    Lindqvist, Y.2    Kluger, R.3    Schneider, G.4
  • 27
    • 0026874436 scopus 로고
    • A high-speed data collection system for large unit cell crystals using an imaging plate as a detector
    • Sato, M., Yamamoto, M., Imada, K. & Katsube, Y. J. (1992) A high-speed data collection system for large unit cell crystals using an imaging plate as a detector, J. Appl. Crystallogr. 25, 348-357.
    • (1992) J. Appl. Crystallogr. , vol.25 , pp. 348-357
    • Sato, M.1    Yamamoto, M.2    Imada, K.3    Katsube, Y.J.4
  • 28
    • 0024829321 scopus 로고
    • Preliminary crystallographic data for transketolase from yeast
    • Schneider, G., Sundström, M. & Lindqvist, Y. (1989) Preliminary crystallographic data for transketolase from yeast, J. Biol. Chem. 264, 21619-21620.
    • (1989) J. Biol. Chem. , vol.264 , pp. 21619-21620
    • Schneider, G.1    Sundström, M.2    Lindqvist, Y.3
  • 30
    • 0027432273 scopus 로고
    • Parameters affecting lithium-acetate mediated transformation of Saccharomyces cerevisiae and developement of a rapid and simplified procedure
    • Soni, R., Carmichael, J. P. & Murray, J. A. H. (1993) Parameters affecting lithium-acetate mediated transformation of Saccharomyces cerevisiae and developement of a rapid and simplified procedure, Curr. Genet. 24, 455-459.
    • (1993) Curr. Genet. , vol.24 , pp. 455-459
    • Soni, R.1    Carmichael, J.P.2    Murray, J.A.H.3
  • 31
    • 0029067816 scopus 로고
    • Transketolase A of Escherichia coli K12. Purification and properties of the enzyme from recombinant strains
    • Sprenger, G. A., Schörken, U., Sprenger, G. & Sahm, H. (1995) Transketolase A of Escherichia coli K12. Purification and properties of the enzyme from recombinant strains, Eur. J. Biochem. 230, 525-532.
    • (1995) Eur. J. Biochem. , vol.230 , pp. 525-532
    • Sprenger, G.A.1    Schörken, U.2    Sprenger, G.3    Sahm, H.4
  • 32
    • 0027515306 scopus 로고
    • Yeast TKL1 gene encodes a transketolase that is required for efficient glycolysis and biosynthesis of aromatic amino acids
    • Sundström, M., Lindqvist, Y., Schneider, G., Hellmann, U. & Ronne, H. (1993a) Yeast TKL1 gene encodes a transketolase that is required for efficient glycolysis and biosynthesis of aromatic amino acids, J. Biol. Chem. 268, 24346-24352.
    • (1993) J. Biol. Chem. , vol.268 , pp. 24346-24352
    • Sundström, M.1    Lindqvist, Y.2    Schneider, G.3    Hellmann, U.4    Ronne, H.5
  • 33
    • 0026495331 scopus 로고
    • Three-dimensional structure of apotransketolase
    • Sundström, M., Lindqvist, Y. & Schneider, G. (1993b) Three-dimensional structure of apotransketolase, FEBS Lett. 313, 229-231.
    • (1993) FEBS Lett. , vol.313 , pp. 229-231
    • Sundström, M.1    Lindqvist, Y.2    Schneider, G.3
  • 35
    • 0028575439 scopus 로고
    • Analysis of an invariant cofactor-protein interaction in thiamin diphosphate dependent enzymes by site-directed mutagenesis
    • Wikner, C., Meshalkina, L., Nilsson, U., Nikkola, M., Lindqvist, Y. & Schneider, G. (1994) Analysis of an invariant cofactor-protein interaction in thiamin diphosphate dependent enzymes by site-directed mutagenesis, J. Biol. Chem. 269, 32144-32150.
    • (1994) J. Biol. Chem. , vol.269 , pp. 32144-32150
    • Wikner, C.1    Meshalkina, L.2    Nilsson, U.3    Nikkola, M.4    Lindqvist, Y.5    Schneider, G.6


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