Isotopic and other studies on the molecular origins of substrate regulation of some pyruvate decarboxylases: A reconsideration

Isotopes in Environmental and Health Studies

Volumn 43, Issue 1, 2007, Pages 1-16

  Schowen, Richard L ^a  

^a UNIVERSITY OF KANSAS   (United States)

Author keywords

Isotope effects; Kinetics; Mechanisms; Models; Review

Indexed keywords

CYSTEINE; ISOTOPE; PYRUVATE DECARBOXYLASE; PYRUVIC ACID DERIVATIVE; SACCHAROMYCES CEREVISIAE PROTEIN;

ISOTOPIC ANALYSIS; KINETICS; MOLECULAR ANALYSIS; SUBSTRATE;

CHEMICAL MODEL; CHEMICAL STRUCTURE; CHEMISTRY; DECARBOXYLATION; ENZYME ACTIVATION; KINETICS; METABOLISM; REVIEW;

CYSTEINE; DECARBOXYLATION; ENZYME ACTIVATION; ISOTOPES; KINETICS; MODELS, CHEMICAL; MODELS, MOLECULAR; PYRUVATE DECARBOXYLASE; PYRUVATES; SACCHAROMYCES CEREVISIAE PROTEINS;

SACCHAROMYCES CEREVISIAE;

EID: 34247603464     PISSN: 10256016     EISSN: 14772639     Source Type: Journal    
DOI: 10.1080/10256010600990393     Document Type: Review

References (21)

1. Schowen, R. L. (1998) Thiamin-dependent enzymes. Comprehensive Biological Catalysis, 3, pp. 217-266. Academic Press, London
2. Alvarez, F. J., Ermer, J., Hübner, G., Schellenberger, A. and Schowen, R. L. (1991) Catalytic power of pyruvate decarboxylase. Rate-limiting events and microscopic rate constants from primary carbon and secondary hydrogen isotope effects. J. Am. Chem. Soc., 113, pp. 8402-8409.
3. Alvarez, F. J., Ermer, J., Hübner, G., Schellenberger, A. and Schowen, R. L. (1995) The linkage of catalysis and regulation in enzyme action. Solvent isotope effects as probes of protonic sites in the yeast pyruvate decarboxylase mechanism. J. Am. Chem. Soc., 117, pp. 1678-1683.
4. Sun, S., Duggleby, R. G. and Schowen, R. L. (1995) The linkage of catalysis and regulation in enzyme action. Carbon isotope effects, solvent isotope effects and proton inventories for the unregulated pyruvate decarboxylase of Zymomonas mobilis. J. Am. Chem. Soc., 117, pp. 7317-7322.
5. Kluger, R. and Smyth, T. (1981) Interaction of pyruvate-thiamin diphosphate adducts with pyruvate decarboxylase. Catalysis through "closed" transition states. J. Am. Chem. Soc, 103, pp. 1214-1216.
6. Baburina, I., Gao, Y., Hu, Z., Jordan, F., Hohmann, S. and Furey, W. (1994) Substrate activation of brewers' yeast pyruvate decarboxylase is abolished by mutation of cysteine 221 to serine. Biochemistry, 33, pp. 5630-5635.
7. Hong, J., Sun, S., Stewart, B. H., Schowen, K. B. and Schowen, R. L. (1996) The linkage of catalysis and regulation in the action of pyruvate decarboxylases. Biochemistry and Physiology of Thiamin Diphosphate Enzymes, pp. 70-81. Intemann Wissenschaftlicher Verlag, Prien
8. Muller, Y. A. and Schulz, G. E. (1993) Structure of the thiamine- and flavin-dependent enzyme pyruvate oxidase. Science, 259, pp. 965-977.
9. Lindqvist, Y., Schneider, G., Ermler, U. and Sundstrom, M. (1992) Three-dimensional structure of transketolase, a thiamine diphosphate dependent enzyme, at 2.5 A resolution. EMBO J., 11, pp. 2373-2379.
10. Hübner, G., König, S. and Schellenberger, A. (1988) The functional role of thiol groups of pyruvate decarboxylase from brewer's yeast. Biomed. Biochim. Acta, 47, pp. 9-18.
11. Quinn, D. M. (2006) Theory and practice of solvent isotope effects. Isotope Effects in Chemistry and Biology, lor and Francis, Boca Raton
12. Lu, G., Dobritzsch, D., Baumann, S., Schneider, G. and König, S. (2000) The structural basis of substrate activation in yeast pyruvate decarboxylase. A crystallographic and kinetic study. Eur. J. Biochem., 267, pp. 861-868.
13. Arjunan, P., Umland, T., Dyda, F., Swaminathan, S., Furey, W., Sax, M., Farrenkopf, B., Gao, Y., Zhang, D. and Jordan, F. (1996) Crystal structure of the thiamin diphosphate-dependent enzyme pyruvate decarboxylase from the yeast Saccharomyces cerevisiae at 2.3 A resolution. J. Mol. Biol., 256, pp. 590-600.
14. Dobritzsch, D., König, S., Schneider, G. and Lu, G. (1998) High resolution crystal structure of pyruvate decarboxylase from. Zymomonas mobilis. J. Biol. Chem., 273, pp. 20196-20204.
15. Lu, G., Dobritzsch, D., König, S. and Schneider, G. (1997) Novel tetramer assembly of pyruvate decarboxylase from brewer's yeast observed in a new crystal form. FEBS Lett., 403, pp. 249-253.
16. Frank, R. A.W., Titman, C. M., Pratap, J. V., Luisi, B. F. and Perham, R. N. (2004) A Molecular switch and proton wire synchronize the active sites in thiamine enzymes. Science, 306, pp. 872-876.
17. Jordan, F. (2004) Biochemistry: How active sites communicate in thiamin enzymes. Science, 306, pp. 818-820.
18. Sergienko, E. and Jordan, F. (2002) New model for activation of yeast pyruvate decarboxylase by substrate consistent with the alternating sites mechanism: Demonstration of the existence of two active forms of the enzyme. Biochemistry, 41, pp. 3952-3967.
19. Wei, W., Liu, M. and Jordan, F. (2002) Solvent kinetic isotope effects monitor changes in hydrogen bonding at the active center of yeast pyruvate decarboxylase concomitant with substrate activation: The substituent at position 221 can control the state of activation. Biochemistry, 41, pp. 451-461.
20. Wang, J., Golbik, R., Seliger, B., Spinka, M., Tittmann, K., Hübner, G. and Jordan, F. (2001) Consequences of a modified putative substrate-activation site on catalysis by yeast pyruvate decarboxylase. Biochemistry, 40, pp. 1755-1763.
21. Jordan, F., Nemeria, N. S. and Sergienko, E. (2005) Multiple modes of active center communication in thiamin diphosphate-dependent enzymes. Acc. Chem. Res., 38, pp. 755-763.