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Volumn 78, Issue 1, 2005, Pages 8-13

Effects of transketolase cofactors on its conformation and stability

Author keywords

Circular dichroism spectroscopy; Conformation; Differential scanning calorimetry; Fluorescence spectroscopy; Folding; Thiamine diphosphate; Transketolase

Indexed keywords

CALCIUM ION; COCARBOXYLASE; DIVALENT CATION; HOLOENZYME; MAGNESIUM ION; TRANSKETOLASE; TRYPTOPHAN;

EID: 23444455100     PISSN: 00243205     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.lfs.2004.12.055     Document Type: Article
Times cited : (13)

References (24)
  • 1
    • 70349629097 scopus 로고
    • Mechanism of action of transketolase: I. Properties of the crystalline yeast enzyme
    • A.G. Datta, and E. Racker Mechanism of action of transketolase: I. Properties of the crystalline yeast enzyme Journal of Biological Chemistry 236 1961 617 623
    • (1961) Journal of Biological Chemistry , vol.236 , pp. 617-623
    • Datta, A.G.1    Racker, E.2
  • 2
    • 0019888067 scopus 로고
    • Transketolase kinetics. the slow reconstitution of the holoenzyme is due to rate-limiting dimerization of the subunits
    • R.M. Egan, and H.Z. Sable Transketolase kinetics. The slow reconstitution of the holoenzyme is due to rate-limiting dimerization of the subunits Journal of Biological Chemistry 256 1981 4877 4883
    • (1981) Journal of Biological Chemistry , vol.256 , pp. 4877-4883
    • Egan, R.M.1    Sable, H.Z.2
  • 4
    • 0030042763 scopus 로고    scopus 로고
    • Methods to estimate the conformation of proteins and polypeptides from circular dichroism data
    • N.J. Greenfield Methods to estimate the conformation of proteins and polypeptides from circular dichroism data Analytical Biochemistry 235 1996 1 10
    • (1996) Analytical Biochemistry , vol.235 , pp. 1-10
    • Greenfield, N.J.1
  • 5
    • 0015497426 scopus 로고
    • Studies on the reconstitution of apotransketolase with thiamine pyrophosphate and analogs of the coenzyme
    • P.C. Heinrich, H. Steffen, P. Janser, and O. Wiss Studies on the reconstitution of apotransketolase with thiamine pyrophosphate and analogs of the coenzyme European Journal of Biochemistry 30 1972 533 541
    • (1972) European Journal of Biochemistry , vol.30 , pp. 533-541
    • Heinrich, P.C.1    Steffen, H.2    Janser, P.3    Wiss, O.4
  • 6
    • 0015515486 scopus 로고
    • Chemical modification of tryptophan at the binding site of thiamine-pyrophosphate in transketolase from Baker's yeast
    • C.P. Heinrich, K. Noack, and O. Wiss Chemical modification of tryptophan at the binding site of thiamine-pyrophosphate in transketolase from Baker's yeast Biochemical and Biophysical Research Communications 49 1972 1427 1432
    • (1972) Biochemical and Biophysical Research Communications , vol.49 , pp. 1427-1432
    • Heinrich, C.P.1    Noack, K.2    Wiss, O.3
  • 7
    • 0020393767 scopus 로고
    • Transketolase from yeast, rat liver, and pig liver
    • G.A. Kochetov Transketolase from yeast, rat liver, and pig liver Methods in Enzymology 90 1982 209 223
    • (1982) Methods in Enzymology , vol.90 , pp. 209-223
    • Kochetov, G.A.1
  • 8
    • 0015627192 scopus 로고
    • Reconstruction of holotransketolase from the apoenzyme and coenzyme
    • G.A. Kochetov, and A.E. Izotova Reconstruction of holotransketolase from the apoenzyme and coenzyme Biokhimiia 38 1973 552 560 (in Russian)
    • (1973) Biokhimiia , vol.38 , pp. 552-560
    • Kochetov, G.A.1    Izotova, A.E.2
  • 12
    • 0026762799 scopus 로고
    • Three-dimensional structure of transketolase, a thiamine diphosphate dependent enzyme, at 2.5 a resolution
    • Y. Lindqvist, G. Schneider, U. Ermler, and M. Sundström Three-dimensional structure of transketolase, a thiamine diphosphate dependent enzyme, at 2.5 A resolution EMBO Journal 11 1992 2373 2379
    • (1992) EMBO Journal , vol.11 , pp. 2373-2379
    • Lindqvist, Y.1    Schneider, G.2    Ermler, U.3    Sundström, M.4
  • 13
    • 0001303106 scopus 로고
    • The role of bivalent cations in the interaction of thiamin diphosphate with apotransketolase from baker yeast
    • L.E. Meshalkina, and G.A. Kochetov The role of bivalent cations in the interaction of thiamin diphosphate with apotransketolase from baker yeast Doklady Akademii Nauk USSR 248 1979 1482 1486
    • (1979) Doklady Akademii Nauk USSR , vol.248 , pp. 1482-1486
    • Meshalkina, L.E.1    Kochetov, G.A.2
  • 14
    • 0028305456 scopus 로고
    • Refined structure of transketolase from Saccharomyces cerevisiae at 2.0 a resolution
    • M. Nikkola, Y. Lindqvist, and G. Schneider Refined structure of transketolase from Saccharomyces cerevisiae at 2.0 A resolution Journal of Molecular Biology 238 1994 387 404
    • (1994) Journal of Molecular Biology , vol.238 , pp. 387-404
    • Nikkola, M.1    Lindqvist, Y.2    Schneider, G.3
  • 17
    • 0026495331 scopus 로고
    • Three-dimensional structure of apotransketolase
    • M. Sundström, Y. Lindqvist, and G. Schneider Three-dimensional structure of apotransketolase FEBS Letters 313 1992 229 231
    • (1992) FEBS Letters , vol.313 , pp. 229-231
    • Sundström, M.1    Lindqvist, Y.2    Schneider, G.3
  • 19
    • 0014718113 scopus 로고
    • Protein denaturation. C. Theoretical models for the mechanism of denaturation
    • C. Tanford Protein denaturation. C. Theoretical models for the mechanism of denaturation Advances in Protein Chemistry 24 1970 91 95
    • (1970) Advances in Protein Chemistry , vol.24 , pp. 91-95
    • Tanford, C.1
  • 20
    • 0000512387 scopus 로고
    • The unfolding of beta-lactoglobulin at pH 3 by urea, formamide, and other organic substances
    • C. Tanford, and P.K. De The unfolding of beta-lactoglobulin at pH 3 by urea, formamide, and other organic substances Journal of Biological Chemistry 236 1961 1711 1715
    • (1961) Journal of Biological Chemistry , vol.236 , pp. 1711-1715
    • Tanford, C.1    De, P.K.2
  • 21
    • 0014061953 scopus 로고
    • Studies on the properties of 2-alpha-hydroxyethyl-thiamine pyrophosphate ("active acetaldehyde")
    • J. Ullrich, and A. Mannschreck Studies on the properties of 2-alpha-hydroxyethyl-thiamine pyrophosphate ("active acetaldehyde") European Journal of Biochemistry 1 1967 110 116
    • (1967) European Journal of Biochemistry , vol.1 , pp. 110-116
    • Ullrich, J.1    Mannschreck, A.2
  • 22
    • 0018131742 scopus 로고
    • Study of different conformational states of transketolase by the method of perturbation UV-spectrophotometry
    • R.A. Usmanov, and G.A. Kochetov Study of different conformational states of transketolase by the method of perturbation UV-spectrophotometry Biokhimiia 43 1978 1796 1804 (in Russian)
    • (1978) Biokhimiia , vol.43 , pp. 1796-1804
    • Usmanov, R.A.1    Kochetov, G.A.2
  • 24
    • 0028575439 scopus 로고
    • Analysis of an invariant cofactor-protein interaction in thiamin diphosphate-dependent enzymes by site-directed mutagenesis. Glutamic acid 418 in transketolase is essential for catalysis
    • C. Wikner, L. Meshalkina, U. Nilsson, M. Nikkola, Y. Lindqvist, M. Sundström, and G. Schneider Analysis of an invariant cofactor-protein interaction in thiamin diphosphate-dependent enzymes by site-directed mutagenesis. Glutamic acid 418 in transketolase is essential for catalysis Journal of Biological Chemistry 269 1994 32144 32150
    • (1994) Journal of Biological Chemistry , vol.269 , pp. 32144-32150
    • Wikner, C.1    Meshalkina, L.2    Nilsson, U.3    Nikkola, M.4    Lindqvist, Y.5    Sundström, M.6    Schneider, G.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.