Donor substrate regulation of transketolase

European Journal of Biochemistry

Volumn 271, Issue 21, 2004, Pages 4189-4194

  Esakova, Olga A ^a   Meshalkina, Ludmilla E ^a   Golbik, Ralph ^b   Hübner, Gerhard ^b   Kochetov, German A ^a  

^a MOSCOW STATE UNIVERSITY   (Russian Federation)

^b MARTIN LUTHER UNIVERSITY HALLE WITTENBERG   (Germany)

Author keywords

2 ( , dihydroxyethyl) thiamin diphosphate; Regulation of enzyme activity; Spectrophotometric titration; Thiamin diphosphate; Transketolase

Indexed keywords

2 (ALPHA,BETA DIHYDROXYETHYL)THIAMINE DIPHOSPHATE; COCARBOXYLASE; MAGNESIUM ION; PYRIDYLTHIAMINE DIPHOSPHATE; TRANSKETOLASE; UNCLASSIFIED DRUG;

ARTICLE; BINDING AFFINITY; COENZYME; ENZYME ACTIVE SITE; ENZYME BINDING; ENZYME KINETICS; ENZYME REGULATION; ENZYME SUBSTRATE; PRIORITY JOURNAL; PROTEIN INTERACTION;

BINDING SITES; BUFFERS; DOSE-RESPONSE RELATIONSHIP, DRUG; GENE EXPRESSION REGULATION, ENZYMOLOGIC; HYDROGEN-ION CONCENTRATION; IONS; KINETICS; MAGNESIUM; MAGNESIUM CHLORIDE; MODELS, CHEMICAL; PROTEIN BINDING; RECOMBINANT PROTEINS; SACCHAROMYCES CEREVISIAE; SPECTROPHOTOMETRY; TEMPERATURE; THIAMINE PYROPHOSPHATE; TIME FACTORS; TRANSKETOLASE;

EID: 8644283470     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.2004.04357.x     Document Type: Article

References (26)

1. Kochetov, G.A. (1982) Transketolase from yeast, rat liver and pig liver. Methods Enzymol. 90, 209-223.
2. Kochetov, G.A., Tikhomirova, N.K. & Philippov, P.P. (1975) The binding of thiamine pyrophosphate with transketolase in equilibrium conditions. Biochem. Biophys. Res. Commun. 63, 924-930.
3. Kochetov, G.A., Meshalkina, L.E. & Usmanov, R.A. (1976) The number of active sites in a molecule of transketolase. Biochem. Biophys. Res. Commun. 69, 836-843.
4. Meshalkina, L.E. & Kochetov, G.A. (1979) The functional identity of the active centers of transketolase. Biochim. Biophys. Acta 571, 218-223.
5. Selivanov, V.A., Kovina, M.V., Kochevova, N.V., Meshalkina, L.E. & Kochetov, G.A. (2003) Studies of thiamine diphosphate binding to the yeast apotransketolase. J. Mol. Catal., B Enzym. 26, 33-40.
6. Heinrich, P.C., Steffen, H., Janser, P. & Wiss, O. (1972) Studies on the reconstitution of apotransketolase with thiamine pyrophosphate and analogs of the coenzyme. Eur. J. Biochem. 30, 533-541.
7. Heinrich, P.C. & Schmidt, D. (1973) Determination of the binding constant of thiamine diphosphate in transketolase from bakers yeast by circular dichroism titration. Experientia 29, 1226-1227.
8. Kochetov, G.A. & Izotova, A.E. (1973) Reconstitution of holotransketolase from apotransketolase and thiamine diphosphate. Biokhimiya (Russian) 38, 552-559.
9. Kovina, M.V., Selivanov, V.A., Kochevova, N.V. & Kochetov, G.A. (1997) Kinetic mechanism of active site non-equivalence in transketolase. FEBS Lett. 418, 11-14.
10. Lindqvist, Y., Schneider, G., Ermler, U. & Sundström, M. (1992) Three dimensional structure of transketolase, a thiamine diphosphate dependent enzyme, at 2.5 Å resolution. EMBO J. 11, 218-223.
11. Nikkola, M., Lindqvist, Y. & Schneider, G. (1994) Refined structure of transketolase from Saccharomyces cerevisiae of 2.0 Å resolution. J. Mol. Biol. 238, 387-404.
12. Sundström, M., Lindqvist, Y. & Schneider, G. (1992) Three-dimensional structure of apotransketolase. Flexible loops at the active site enable cofactor binding. FEBS Lett. 313, 229-231.
13. Fiedler, E., Thorell, S., Sandalova, T., Golbik, R., König, S. & Schneider, G. (2002) Snapshot of a key intermediate in enzymatic thiamin catalysis: crystal structure of the α-carbanion of (α,β- dihydroxyethyl)-thiamine diphosphate in the active site of transketolase from Saccharomyces cerevisiae. Proc. Natl Acad. Sci. USA 99, 591-595.
14. Usmanov, R., Sidorova, N. & Kochetov, G. (1996) Interaction of dihydroxyethylthiamine pyrophosphate with transketolase. Biochem. Mol. Biol. Int. 38, 307-314.
15. Schellenberger, A., Wendler, K., Creutzburg, P. & Hübner, G. (1967) On the theory of thiamine pyrophosphate action. V. The function of both pyrimidine-N-atoms. Hoppe-Seyler's Z. Physiol. Chem. 348, 501-505.
16. Wikner, C., Meshalkina, L., Nilsson, U., Nikkola, M., Lindqvist, Y., Sundström, M. & Schneider, G. (1994) Analysis of an invariant cofactor-protein interaction in thiamine diphosphate-dependent enzymes by site-directed mutagenesis. J. Biol. Chem. 269, 32144-32150.
17. Heinrich, C.P., 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.
18. Ullrich, J. & Mannschreck, A. (1967) Studies on the properties of 2-alpha-hydroxyethyl-thiamine pyrophosphate ('active acetaldehyde'). Eur. J. Biochem. 1, 110-116.
19. Meshalkina, L.E., Usmanov, R.A. & Kochetov, G.A. (1991) The role of the amino group and pyrimidine ring nitrogen atoms of thiamine pyrophosphate in the transketolase reaction. In Biochemistry and Physiology of Thiamine Diphosphate Enzymes (Bisswanger, H. & Ullrich, J., eds), pp. 343-352. Verlag Chemie, Weinheim.
20. i. Biochem. J. 129, 197-202.
21. Golbik, R., Neef, H., Hübner, G., König, S., Seliger, B., Meshalkina, L., Kochetov, G. & Schellenberger, A. (1991) Function of the aminopyrimidine part in thiamine pyrophosphate enzymes. Bioorg. Chem. 19, 10-17.
22. Hennig, J., Kern, G., Neef, H., Bisswanger, H. & Hübner, G. (1996) Determination of the binding constants of thiamine diphosphate and analogues as coenzymes of pyruvate dehydrogenase complex from E. coli. In Biochemistry and Physiology of Thiamine Diphosphate Enzymes (Bisswanger, H. & Ullrich, J., eds), pp. 235-242. Verlag Chemie, Weinheim.
23. Hübner, G., Kern, G., Hennig, J., Neef, H. & Bisswanger, H. (1996) A novel mechanism of substrate regulation of enzymes by tight binding of reaction intermediates formed with a reversible bound cofactor. In Biochemistry and Physiology of Thiamine Diphosphate Enzymes (Bisswanger, H. & Ullrich, J., eds), pp. 243-251. Verlag Chemie, Weinheim.
24. König, S., Schellenberger, A., Neef, H. & Schneider, G. (1994) Specificity of coenzyme binding in thiamin diphosphate-dependent enzymes. Crystal structures of yeast transketolase in complex with analogs of thiamine diphosphate. J. Biol. Chem. 269, 10879-10882.
25. Egan, R.M. & Sable, H.Z. (1981) Transketolase kinetics. The slow reconstitution of the holoenzyme is due to rate-limiting dimerization of the subunits. J. Biol. Chem. 256, 4877-4883.
26. Kovina, M.V. & Kochetov, G.A. (1998) Cooperativity and flexibility of active sites in homodimeric transketolase. FEBS Lett. 440, 81-84.