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Fiedler, E., Thorell, S., Sandalova, T., Golbik, R., König, S., and Schneider, G. (2002) Snapshot of a key intermediate in enzymatic thiamin catalysis: crystal structure of the α-carbanion of (α,β- dihydroxyethyl)-thiamin diphosphate in the active site of transketolase from Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. USA 99, 591-595.
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Effect of coenzyme modification on the structural and catalytic properties of wild-type transketolase and of the variant E418A from Saccharomyces cerevisiae
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Golbik, R., Meshalkina, L. E., Sandalova, T., Tittmann, K., Fiedler, E., Neef, H., König, S., Kluger, R., Kochetov, G. A., Schneider, G., and Hübner, G. (2005) Effect of coenzyme modification on the structural and catalytic properties of wild-type transketolase and of the variant E418A from Saccharomyces cerevisiae. FEBS J. 272, 1326-1342.
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Studies on the reconstitution of apotransketolase with thiamine pyrophosphate and analogs of the coenzyme
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Kinetic mechanism of active site non-equivalence in transketolase
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Studies of thiamin diphosphate binding to the yeast apotransketolase
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Kinetic study of the H103A mutant yeast transketolase
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Selivanov, V. A., Kovina, M. V., Kochevova, N. V., Meshalkina, L. E., and Kochetov, G. A. (2004) Kinetic study of the H103A mutant yeast transketolase. FEBS Lett. 567, 270-274.
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A circular dichroism study of transketolase from baker's yeast
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Determination of the binding constant of thiamine diphosphate in transketolase from baker's yeast by circular dichroism titration
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Three-dimensional structure of apotransketolase
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Refined structure of transketolase from Saccharomyces cerevisiae at 2.0 Å resolution
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Nikkola, M., Lindqvist, Y., and Schneider, G. (1994) Refined structure of transketolase from Saccharomyces cerevisiae at 2.0 Å resolution. J. Mol. Biol. 238, 387-404.
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Crystallography and mutagenesis of transketolase: Mechanistic implications for enzymatic thiamin catalysis
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Schneider, G., and Lindqvist, Y. (1998) Crystallography and mutagenesis of transketolase: mechanistic implications for enzymatic thiamin catalysis. Biochim. Biophys. Acta 1385, 387-398.
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Donor substrate regulation of transketolase
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Interaction of dihydroxyethylthiamine pyrophosphate with transketolase
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Usmanov, R., Sidorova, N., and Kochetov, G. (1996) Interaction of dihydroxyethylthiamine pyrophosphate with transketolase. Biochem. Mol. Biol. Intern. 38, 307-314.
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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
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Wikner, C., Meshalkina, L., Nilsson, U., Nikkola, M., Lindqvist, Y., Sundström, M., and Schneider, G. (1994) 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. J. Biol. Chem. 269, 32144-32150.
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Chemical modification of tryptophan at the binding site of thiamine-pyrophosphate in transketolase from Baker's yeast
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Charge transfer interactions in transketolase-thiamine pyrophosphate complex
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Kochetov, G. A., and Usmanov, R. A. (1970) Charge transfer interactions in transketolase-thiamine pyrophosphate complex. Biochem. Biophys. Res. Commun. 41, 1134-1140.
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The role of the charge transfer complex in the transketolase catalized reaction
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The number of active sites in a molecule of transketolase
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Kochetov, G. A., Meshalkina, L. E., and Usmanov, R. A. (1976) The number of active sites in a molecule of transketolase. Biochem. Biophys. Res. Commun. 69, 836-843.
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The functional identity of the active centres of transketolase
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Meshalkina, L. E., and Kochetov, G. A. (1979) The functional identity of the active centres of transketolase. Biochim. Biophys. Acta 571, 218-223.
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Meshalkina, L.E.1
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