Biology:3,4-dihydroxy-2-butanone-4-phosphate synthase
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Short description: Class of enzymes
| DHBP_synthase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 crystal structure of 3,4-dihydroxy-2-butanone 4-phosphate synthase gold derivative | |||||||||
| Identifiers | |||||||||
| Symbol | DHBP_synthase | ||||||||
| Pfam | PF00926 | ||||||||
| InterPro | IPR000422 | ||||||||
| SCOP2 | 1iez / SCOPe / SUPFAM | ||||||||
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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
- ↑ "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.
- ↑ "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.
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