The Enzyme Database

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EC 2.5.1.9     
Accepted name: riboflavin synthase
Reaction: 2 6,7-dimethyl-8-(1-D-ribityl)lumazine = riboflavin + 4-(1-D-ribitylamino)-5-amino-2,6-dihydroxypyrimidine
For diagram of riboflavin biosynthesis (late stages), click here
Other name(s): heavy riboflavin synthase; light riboflavin synthase; riboflavin synthetase; riboflavine synthase; riboflavine synthetase
Systematic name: 6,7-dimethyl-8-(1-D-ribityl)lumazine:6,7-dimethyl-8-(1-D-ribityl)lumazine 2,3-butanediyltransferase
Comments: A flavoprotein (riboflavin).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9075-82-5
References:
1.  Plaut, G.W.E. Studies on the nature of the enzymic conversion of 6,7-dimethyl-8-ribityllumazine to riboflavin. J. Biol. Chem. 238 (1963) 2225–2243. [PMID: 13944007]
2.  Plaut, G.W.E. and Harvey, R.A. Riboflavin synthetase. Methods Enzymol. 18B (1971) 527–538.
3.  Wacker, H., Harvey, R.A., Winestock, C.H. and Plaut, G.W.E. 4-(1′-D-Ribitylamino)-5-amino-2,6-dihydroxypyrimidine, the second product of the riboflavin synthetase reaction. J. Biol. Chem. 239 (1964) 3493–3497. [PMID: 14245407]
[EC 2.5.1.9 created 1972]
 
 
EC 2.5.1.78     
Accepted name: 6,7-dimethyl-8-ribityllumazine synthase
Reaction: 1-deoxy-L-glycero-tetrulose 4-phosphate + 5-amino-6-(D-ribitylamino)uracil = 6,7-dimethyl-8-(D-ribityl)lumazine + 2 H2O + phosphate
For diagram of riboflavin biosynthesis (late stages), click here and for mechanism, click here
Glossary: 5-amino-6-(D-ribitylamino)uracil = 5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione
6,7-dimethyl-8-(1-D-ribityl)lumazine = 1-deoxy-1-(6,7-dimethyl-2,4-dioxo-3,4-dihydropteridin-8(2H)-yl)-D-ribitol
Other name(s): lumazine synthase; 6,7-dimethyl-8-ribityllumazine synthase 2; 6,7-dimethyl-8-ribityllumazine synthase 1; lumazine synthase 2; lumazine synthase 1; type I lumazine synthase; type II lumazine synthase; RIB4; MJ0303; RibH; Pbls; MbtLS; RibH1 protein; RibH2 protein; RibH1; RibH2
Systematic name: 5-amino-6-(D-ribitylamino)uracil butanedionetransferase
Comments: Involved in riboflavin biosynthesis.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  Kis, K., Volk, R. and Bacher, A. Biosynthesis of riboflavin. Studies on the reaction mechanism of 6,7-dimethyl-8-ribityllumazine synthase. Biochemistry 34 (1995) 2883–2892. [PMID: 7893702]
2.  Garcia-Ramirez, J.J., Santos, M.A. and Revuelta, J.L. The Saccharomyces cerevisiae RIB4 gene codes for 6,7-dimethyl-8-ribityllumazine synthase involved in riboflavin biosynthesis. Molecular characterization of the gene and purification of the encoded protein. J. Biol. Chem. 270 (1995) 23801–23807. [DOI] [PMID: 7559556]
3.  Bacher, A., Fischer, M., Kis, K., Kugelbrey, K., Mörtl, S., Scheuring, J., Weinkauf, S., Eberhardt, S., Schmidt-Bäse, K., Huber, R., Ritsert, K., Cushman, M., Ladenstein, R. Biosynthesis of riboflavin: structure and mechanism of lumazine synthase. Biochem. Soc. Trans. 24 (1996) 89–94. [PMID: 8674771]
4.  Mörtl, S., Fischer, M., Richter, G., Tack, J., Weinkauf, S. and Bacher, A. Biosynthesis of riboflavin. Lumazine synthase of Escherichia coli. J. Biol. Chem. 271 (1996) 33201–33207. [DOI] [PMID: 8969176]
5.  Bacher, A., Eberhardt, S., Fischer, M., Mortl, S., Kis, K., Kugelbrey, K., Scheuring, J. and Schott, K. Biosynthesis of riboflavin: lumazine synthase and riboflavin synthase. Methods Enzymol. 280 (1997) 389–399. [DOI] [PMID: 9211334]
6.  Goldbaum, F.A., Velikovsky, C.A., Baldi, P.C., Mortl, S., Bacher, A. and Fossati, C.A. The 18-kDa cytoplasmic protein of Brucella species - an antigen useful for diagnosis - is a lumazine synthase. J. Med. Microbiol. 48 (1999) 833–839. [DOI] [PMID: 10482294]
7.  Jordan, D.B., Bacot, K.O., Carlson, T.J., Kessel, M. and Viitanen, P.V. Plant riboflavin biosynthesis. Cloning, chloroplast localization, expression, purification, and partial characterization of spinach lumazine synthase. J. Biol. Chem. 274 (1999) 22114–22121. [DOI] [PMID: 10419541]
8.  Zhang, X., Meining, W., Fischer, M., Bacher, A. and Ladenstein, R. X-ray structure analysis and crystallographic refinement of lumazine synthase from the hyperthermophile Aquifex aeolicus at 1.6 Å resolution: determinants of thermostability revealed from structural comparisons. J. Mol. Biol. 306 (2001) 1099–1114. [DOI] [PMID: 11237620]
9.  Fischer, M., Haase, I., Feicht, R., Richter, G., Gerhardt, S., Changeux, J.P., Huber, R. and Bacher, A. Biosynthesis of riboflavin: 6,7-dimethyl-8-ribityllumazine synthase of Schizosaccharomyces pombe. Eur. J. Biochem. 269 (2002) 519–526. [DOI] [PMID: 11856310]
10.  Cushman, M., Yang, D., Gerhardt, S., Huber, R., Fischer, M., Kis, K. and Bacher, A. Design, synthesis, and evaluation of 6-carboxyalkyl and 6-phosphonoxyalkyl derivatives of 7-oxo-8-ribitylaminolumazines as inhibitors of riboflavin synthase and lumazine synthase. J. Org. Chem. 67 (2002) 5807–5816. [DOI] [PMID: 12153285]
11.  Haase, I., Mortl, S., Kohler, P., Bacher, A. and Fischer, M. Biosynthesis of riboflavin in archaea. 6,7-dimethyl-8-ribityllumazine synthase of Methanococcus jannaschii. Eur. J. Biochem. 270 (2003) 1025–1032. [DOI] [PMID: 12603336]
12.  Morgunova, E., Meining, W., Illarionov, B., Haase, I., Jin, G., Bacher, A., Cushman, M., Fischer, M. and Ladenstein, R. Crystal structure of lumazine synthase from Mycobacterium tuberculosis as a target for rational drug design: binding mode of a new class of purinetrione inhibitors. Biochemistry 44 (2005) 2746–2758. [DOI] [PMID: 15723519]
13.  Morgunova, E., Saller, S., Haase, I., Cushman, M., Bacher, A., Fischer, M. and Ladenstein, R. Lumazine synthase from Candida albicans as an anti-fungal target enzyme: structural and biochemical basis for drug design. J. Biol. Chem. 282 (2007) 17231–17241. [DOI] [PMID: 17446177]
[EC 2.5.1.78 created 2010]
 
 


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