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

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Short description: Class of enzymes
DHBP_synthase
PDB 1g58 EBI.jpg
crystal structure of 3,4-dihydroxy-2-butanone 4-phosphate synthase gold derivative
Identifiers
SymbolDHBP_synthase
PfamPF00926
InterProIPR000422
SCOP21iez / SCOPe / SUPFAM

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. "Biosynthesis of riboflavin: 3,4-dihydroxy-2-butanone-4-phosphate synthase". Vitamins and Coenzymes Part J. Methods in Enzymology. 280. 1997. pp. 374–82. doi:10.1016/S0076-6879(97)80128-0. ISBN 9780121821814. 
  2. "Riboflavin synthesis genes ribE, ribB, ribH, ribA reside in the lux operon of Photobacterium leiognathi". Biochemical and Biophysical Research Communications 284 (3): 587–95. June 2001. doi:10.1006/bbrc.2001.5013. PMID 11396941. 
This article incorporates text from the public domain Pfam and InterPro: IPR000422