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

DHBP_synthase
crystal structure of 3,4-dihydroxy-2-butanone 4-phosphate synthase gold derivative
Identifiers
SymbolDHBP_synthase
PfamPF00926
InterProIPR000422
SCOP21iez / SCOPe / SUPFAM
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

The enzyme 3,4-dihydroxy-2-butanone 4-phosphate synthase (DHBP synthase) (RibB) EC 4.1.99.12 catalyses the conversion of D-ribulose 5-phosphate to formate and 3,4-dihydroxy-2-butanone 4-phosphate, the latter serving as the biosynthetic precursor for the xylene ring of riboflavin.[1] In Photobacterium leiognathi, the riboflavin synthesis genes ribB (DHBP synthase), ribE (riboflavin synthase), ribH (lumazine synthase) and ribA (GTP cyclohydrolase II) all reside in the lux operon.[2] RibB is sometimes found as a bifunctional enzyme with GTP cyclohydrolase II that catalyses the first committed step in the biosynthesis of riboflavin. No sequences with significant homology to DHBP synthase are found in the metazoa.

References

  1. ^ Richter G, Krieger C, Volk R, Kis K, Ritz H, Götze E, Bacher A (1997). "Biosynthesis of riboflavin: 3,4-dihydroxy-2-butanone-4-phosphate synthase". Vitamins and Coenzymes Part J. Methods in Enzymology. Vol. 280. pp. 374–82. doi:10.1016/S0076-6879(97)80128-0. ISBN 9780121821814. PMID 9211332.
  2. ^ Lin JW, Chao YF, Weng SF (June 2001). "Riboflavin synthesis genes ribE, ribB, ribH, ribA reside in the lux operon of Photobacterium leiognathi". Biochemical and Biophysical Research Communications. 284 (3): 587–95. doi:10.1006/bbrc.2001.5013. PMID 11396941.
This article incorporates text from the public domain Pfam and InterPro: IPR000422