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Assay
≥95% (GC)
form
liquid
optical activity
[α]/D 78±4°, c = 1 in H2O
storage temp.
−20°C
SMILES string
OC[C@@H](C(C)=O)O
InChI
1S/C4H8O3/c1-3(6)4(7)2-5/h4-5,7H,2H2,1H3/t4-/m0/s1
InChI key
SEYLPRWNVFCVRQ-BYPYZUCNSA-N
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Regulatory Information
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Journal of molecular biology, 341(4), 1085-1096 (2004-08-27)
A synthetic gene specifying a putative 3,4-dihydroxy-2-butanone 4-phosphate synthase of Candida albicans directed the synthesis of a 22.5 kDa peptide in a recombinant Escherichia coli strain. The recombinant protein was purified to apparent homogeneity by two chromatographic steps and was
Journal of molecular biology, 253(1), 151-167 (1995-10-13)
The lumazine synthase/riboflavin synthase of Bacillus subtilis is a bifunctional enzyme complex catalysing the formation of riboflavin from 5-amino-6-(D-ribitylamino)-2,4(1H,3H)-pyrimidinedione and L-3,4-dihydroxy-2-butanone-4-phosphate via 6,7-dimethyl-8-ribityllumazine. The complex is composed of 3 alpha (riboflavin synthase) subunits and 60 beta (lumazine synthase) subunits and
Biosynthesis of riboflavin. The structure of the purine precursor.
The Journal of biological chemistry, 248(17), 6227-6231 (1973-09-10)
The FEBS journal, 280(11), 2537-2563 (2013-04-05)
The xylene ring of riboflavin (vitamin B2 ) is assembled from two molecules of 3,4-dihydroxy-2-butanone 4-phosphate by a mechanistically complex process that is jointly catalyzed by lumazine synthase and riboflavin synthase. In Bacillaceae, these enzymes form a structurally unique complex comprising
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