Pre-steady-state kinetic analysis of riboflavin synthase using a pentacyclic reaction intermediate as substrate

Biological Chemistry

Volumn 386, Issue 2, 2005, Pages 127-136

  Illarionov, Boris ^a,b   Haase, Ilka ^a   Fischer, Markus ^a   Bacher, Adelbert ^a   Schramek, Nicholas ^a  

^a TECHNICAL UNIVERSITY OF MUNICH   (Germany)

^b INSTITUTE OF BIOPHYSICS   (Russian Federation)

Author keywords

Enzyme kinetics; Flavines; Pteridines; Quenched flow; Riboflavin biosynthesis; Stopped flow

Indexed keywords

MUTANT PROTEIN; RIBOFLAVIN; RIBOFLAVIN SYNTHASE;

ARTICLE; CATALYSIS; CHEMICAL REACTION KINETICS; CONTROLLED STUDY; DECOMPOSITION; ENZYME KINETICS; ENZYME MECHANISM; ENZYME SUBSTRATE; PRIORITY JOURNAL; STEADY STATE; WILD TYPE;

ESCHERICHIA COLI; KINETICS; MUTATION; PTERIDINES; RIBOFLAVIN SYNTHASE;

EID: 14944378004     PISSN: 14316730     EISSN: None     Source Type: Journal    
DOI: 10.1515/BC.2005.016     Document Type: Article

References (28)

1. Bacher, A. (1991). Biosynthesis of flavins. In: Chemistry and Biochemistry of Flavoenzymes, Vol. 1, F. Müller, ed. (Boca Raton, USA: CRC Press), pp. 215-259.
2. Bacher, A., and Mailänder, B. (1976). Biosynthesis of riboflavin. Structure of the purine precursor and origin of the ribityl side chain. In: Flavins and Flavoproteins, T.P. Singer, ed. (Amsterdam, The Netherlands: Elsevier), pp. 733-736.
3. Bacher, A., Eberhardt, S., and Richter, G. (1996). Biosynthesis of riboflavin. In: Escherichia coli and Salmonella typhimurium, Vol. 1, F.C. Neidhardt, J.L. Ingraham, K.B. Low, B. Magasanik, M. Schaechter, and H.E. Umbarger, eds. (Washington, DC, USA: American Society for Microbiology), pp. 657-664.
4. Bacher, A., Eberhardt, S., Fischer, M., Mörtl, S., Kis, K., Kugelbrey, K., Scheuring, J., and Schott, K. (1997). Biosynthesis of riboflavin: lumazine synthase and riboflavin synthase. Methods Enzymol. 280, 389-399.
5. Bacher, A., Eberhardt, S., Fischer, M., Kis, K., and Richter, G. (2000). Biosynthesis of vitamin B2 (riboflavin). Annu. Rev. Nutr. 20, 153-167.
6. Beach, R., and Plaut, G.W. (1969). The formation of riboflavin from 6,7-dimethyl-8-ribityllumazine in acid media. Tetrahedron Lett. 40, 3489-3492.
7. Beach, R.L., and Plaut, G.W. (1970). Stereospecificity of the enzymatic synthesis of the o-xylene ring of riboflavin. J. Am. Chem. Soc. 92, 2913-2916.
8. Eberhardt, S., Zingler, N., Kemter, K., Richter, G., Cushman, M., and Bacher, A. (2001). Domain structure of riboflavin synthase. Eur. J. Biochem. 268, 4315-4323.
9. Gerhardt, S., Schott, A.K., Kairies, N., Cushman, M., Illarionov, B., Eisenreich, W., Bacher, A., Huber, R., Steinbacher, S., and Fischer, M. (2002). Studies on the reaction mechanism of riboflavin synthase: X-ray crystal structure of a complex with 6-carboxyethyl-7-oxo-8-ribityllumazine. Structure 10, 1371-1381.
10. Giglione, C., Boularot, A., and Meinnel, T. (2004). Protein N-terminal methionine excision. Cell. Mol. Life Sci. 61, 1455-1474.
11. Harvey, R.A., and Plaut, G.W. (1966). Riboflavin synthetase from yeast. Properties of complexes of the enzyme with lumazine derivatives and riboflavin. J. Biol. Chem. 241, 2120-2136.
12. Illarionov, B., Eisenreich, W., and Bacher, A. (2001a). A pentacyclic reaction intermediate of riboflavin synthase. Proc. Natl. Acad. Sci. USA 98, 7224-7229.
13. Illarionov, B., Kemter, K., Eberhardt, S., Richter, G., Cushman, M., and Bacher, A. (2001b). Riboflavin synthase of Escherichia coli. Effect of single amino acid substitutions on reaction rate and ligand binding properties. J. Biol. Chem. 276, 11524-11530.
14. Illarionov, B., Haase, I., Bacher, A., Fischer, M., and Schramek, N. (2003). Presteady-state kinetic analysis of riboflavin synthase. J. Biol. Chem. 278, 47700-47706.
15. Kuzmic, P. (1996). Program DYNAFIT for the analysis of enzyme kinetic data: application to HIV proteinase. Anal. Biochem. 237, 260-273.
16. Liao, D.I., Wawrzak, Z., Calabrese, J.C., Viitanen, P.V., and Jordan, D.B. (2001). Crystal structure of riboflavin synthase. Structure 9, 399-408.
17. Meining, W., Eberhardt, S., Bacher, A., and Ladenstein, R. (2003). The structure of the N-terminal domain of riboflavin synthase in complex with riboflavin at 2.6 Å resolution. J. Mol. Biol. 331, 1053-1063.
18. Paterson, T., and Wood, H.C.S. (1969). Deuterium exchange of C-methyl protons in 6,7-dimethyl-8-D-ribityl-lumazine, and studies of the mechanism of riboflavine biosynthesis. Chem. Commun. 1969, 290-291.
19. Paterson, T., and Wood, H.C. (1972). The biosynthesis of pteridines. VI. Studies of the mechanism of riboflavin biosynthesis. J. Chem. Soc. 8, 1051-1056.
20. Plaut, G.W.E. (1963). Studies on the nature of the enzymic conversion of 6,7-dimethyl-8-ribityllumazine to riboflavin. J. Biol. Chem. 238, 2225-2243.
21. Plaut, G.W.E., and Beach, R. (1967). In: Flavins and Flavoproteins, T.P. Singer, ed. (Amsterdam, The Netherlands: Elsevier), pp. 737-746.
22. Plaut, G.W., Smith, C.M., and Alworth, W.L. (1974). Biosynthesis of water-soluble vitamins. Annu. Rev. Biochem. 43, 899-922.
23. Römisch, W., Eisenreich, W., Richter, G., and Bacher, A. (2002). Rapid one-pot synthesis of riboflavin isotopomers. J. Org. Chem. 67, 8890 8894.
24. Rowan, T., and Wood, H.C.S. (1963). The biosynthesis of riboflavin. Proc. Chem. Soc. 21-22.
25. Rowan, T., and Wood, H.C. (1968). The biosynthesis of pteridines. V. The synthesis of riboflavin from pteridine precursors. J. Chem. Soc. 4, 452-458.
26. Schott, K., Kellermann, J., Lottspeich, F., and Bacher, A. (1990). Riboflavin synthases of Bacillus subtilis. Purification and amino acid sequence of the a subunit. J. Biol. Chem. 265, 4204-4209.
27. 13C in the xylene ring. Z. Naturforsch. C 42, 425-429.
28. Truffault, V., Coles, M., Diercks, T., Abelmann, K., Eberhardt, S., Lüttgen, H., Bacher, A., and Kessler, H. (2001). The solution structure of the N-terminal domain of riboflavin synthase. J. Mol. Biol. 309, 949-960.