PMID:11342130

Citation	Liao, DI, Calabrese, JC, Wawrzak, Z, Viitanen, PV and Jordan, DB (2001) Crystal structure of 3,4-dihydroxy-2-butanone 4-phosphate synthase of riboflavin biosynthesis. Structure 9:11-8
Abstract	3,4-Dihydroxy-2-butanone-4-phosphate synthase catalyzes a commitment step in the biosynthesis of riboflavin. On the enzyme, ribulose 5-phosphate is converted to 3,4-dihydroxy-2-butanone 4-phosphate and formate in steps involving enolization, ketonization, dehydration, skeleton rearrangement, and formate elimination. The enzyme is absent in humans and an attractive target for the discovery of antimicrobials for pathogens incapable of acquiring sufficient riboflavin from their hosts. The homodimer of 23 kDa subunits requires Mg(2+) for activity.
Links	PubMed
Keywords	Aspartic Acid/chemistry; Binding Sites; Catalysis; Crystallography, X-Ray; Cysteine/chemistry; Dimerization; Escherichia coli/enzymology; Glutamic Acid/chemistry; Histidine/chemistry; Intramolecular Transferases/chemistry; Magnesium/chemistry; Models, Chemical; Models, Molecular; Protein Structure, Secondary; Riboflavin/biosynthesis; Riboflavin/chemistry; Riboflavin Synthase/chemistry
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