EC 4.1.99.12 - 3,4-dihydroxy-2-butanone-4-phosphate synthase

  IntEnz view ENZYME view

IntEnz Enzyme Nomenclature
EC 4.1.99.12

Names

Accepted name:
3,4-dihydroxy-2-butanone-4-phosphate synthase
Other names:
DHBP synthase
L-3,4-dihydroxybutan-2-one-4-phosphate synthase
Systematic name:
D-ribulose 5-phosphate formate-lyase (L-3,4-dihydroxybutan-2-one 4-phosphate-forming)

Reaction

Cofactor

Comments:

Requires a divalent cation, preferably Mg2+, for activity [1]. The reaction involves an intramolecular skeletal rearrangement, with the bonds in D-ribulose 5-phosphate that connect C-3 and C-5 to C-4 being broken, C-4 being removed as formate and reconnection of C-3 and C-5 [1]. The phosphorylated four-carbon product (L-3,4-dihydroxybutan-2-one 4-phosphate) is an intermediate in the biosynthesis of riboflavin [1].

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , DIAGRAM , DIAGRAM , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0008686
UniProtKB/Swiss-Prot: (246) [show] [UniProt]

References

  1. Volk, R. and Bacher, A.
    Studies on the 4-carbon precursor in the biosynthesis of riboflavin. Purification and properties of L-3,4-dihydroxy-2-butanone-4-phosphate synthase.
    J. Biol. Chem. 265: 19479-19485 (1990). [PMID: 2246238]
  2. Liao, D.I., Calabrese, J.C., Wawrzak, Z., Viitanen, P.V. and Jordan, D.B.
    Crystal structure of 3,4-dihydroxy-2-butanone 4-phosphate synthase of riboflavin biosynthesis.
    Structure 9: 11-18 (2001). [PMID: 11342130]
  3. Kelly, M.J., Ball, L.J., Krieger, C., Yu, Y., Fischer, M., Schiffmann, S., Schmieder, P., Küöhne, R., Bermel, W., Bacher, A., Richter, G. and Oschkinat, H.
    The NMR structure of the 47-kDa dimeric enzyme 3,4-dihydroxy-2-butanone-4-phosphate synthase and ligand binding studies reveal the location of the active site.
    Proc. Natl. Acad. Sci. USA 98: 13025-13030 (2001). [PMID: 11687623]
  4. Liao, D.I., Zheng, Y.J., Viitanen, P.V. and Jordan, D.B.
    Structural definition of the active site and catalytic mechanism of 3,4-dihydroxy-2-butanone-4-phosphate synthase.
    Biochemistry 41: 1795-1806 (2002). [PMID: 11827524]
  5. Fischer, M., Römisch, W., Schiffmann, S., Kelly, M., Oschkinat, H., Steinbacher, S., Huber, R., Eisenreich, W., Richter, G. and Bacher, A.
    Biosynthesis of riboflavin in archaea studies on the mechanism of 3,4-dihydroxy-2-butanone-4-phosphate synthase of Methanococcus jannaschii.
    J. Biol. Chem. 277: 41410-41416 (2002). [PMID: 12200440]
  6. Steinbacher, S., Schiffmann, S., Richter, G., Huber, R., Bacher, A. and Fischer, M.
    Structure of 3,4-dihydroxy-2-butanone 4-phosphate synthase from Methanococcus jannaschii in complex with divalent metal ions and the substrate ribulose 5-phosphate: implications for the catalytic mechanism.
    J. Biol. Chem. 278: 42256-42265 (2003). [PMID: 12904291]
  7. Steinbacher, S., Schiffmann, S., Bacher, A. and Fischer, M.
    Metal sites in 3,4-dihydroxy-2-butanone 4-phosphate synthase from Methanococcus jannaschii in complex with the substrate ribulose 5-phosphate.
    Acta Crystallogr. D Biol. Crystallogr. 60: 1338-1340 (2004). [PMID: 15213409]
  8. Echt, S., Bauer, S., Steinbacher, S., Huber, R., Bacher, A. and Fischer, M.
    Potential anti-infective targets in pathogenic yeasts: structure and properties of 3,4-dihydroxy-2-butanone 4-phosphate synthase of Candida albicans.
    J. Mol. Biol. 341: 1085-1096 (2004). [PMID: 15328619]

[EC 4.1.99.12 created 2007]