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2.5.1.9: riboflavin synthase

This is an abbreviated version!
For detailed information about riboflavin synthase, go to the full flat file.

Word Map on EC 2.5.1.9

Reaction

2 6,7-dimethyl-8-(1-D-ribityl)lumazine =

riboflavin
+
4-(1-D-ribitylamino)-5-amino-2,6-dihydroxypyrimidine

Synonyms

heavy riboflavin synthase, light riboflavin synthase, lumazine synthase/riboflavin synthase complex, RibD, RibE1, riboflavin synthase, riboflavin synthetase, riboflavine synthase, riboflavine synthetase, synthase, riboflavin

ECTree

     2 Transferases
         2.5 Transferring alkyl or aryl groups, other than methyl groups
             2.5.1 Transferring alkyl or aryl groups, other than methyl groups (only sub-subclass identified to date)
                2.5.1.9 riboflavin synthase

Crystallization

Crystallization on EC 2.5.1.9 - riboflavin synthase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
detailed structure determination and analysis of enzyme complexed with heavy atoms, three-dimensional structure model
-
from 1.3 M sodium/potassium phosphate, pH 8.7, 0.35 mM 5-nitroso-6-(1'-D-ribitylamino)-2,4(1H,3H)-pyrimidinedione, X-ray structure determination and analysis
-
large crystals by vapour diffusion method, initial solution: 0.7 M sodium/potassium phosphate, pH 8.7, 0.3 mM 5-nitroso-6-ribitylamino-2,4(1H,3H)-pyrimidinedione, protein 2 mg/ml, reservoir solution: 1.3 M sodium/potassium phosphate, pH 8.7, X-ray structure determination and analysis
-
hanging drop vapor diffusion method, using 12% (w/v) PEG 8000, 10% (w/v) glycerol, 0.5 M potassium chloride
modeling for the binding of two molecules of inhibitor 5-(4-phosphonobutyryl)amino-6-D-ribitylaminouracil in the active site
-
molecular modeling of inhibitors to the active site
-
purified recombinant homodimeric N-terminal enzyme domain in complex with riboflavin, 7 mg/ml protein in 70 mM sodium potassium phosphate, pH 7.0, and 100 mM sodium chloride, X-ray diffraction structure determination and analysis at 2.6 A resolution, molecular modeling
structure determination by multiwavelength anomalous diffraction method, modeling
-
crystals of wild-type enzyme are grown at 18°C using the sitting drop vapor diffusion method by mixing equal amounts of protein (6 mg/ml) in 100 mM potassium phosphate, pH 7.0, containing 30 mM Tris and 2 mM dithiothreitol with a reservoir solution containing 0.1 M HEPES, pH 7.0, and 40% 2-methyl-2,4-pentanediol. Crystal structures of the enzyme and its complex with the substrate analog inhibitor, 6,7-dioxo-8-ribityllumazine
crystallization of enzyme complexed with 6-carboxyethyl-7-oxo-8-ribityllumazine, sitting drop vapour diffusion method against equal amounts of reservoir solution containing 0.1 M bicine, pH 9.0, 65% v/v 2-mehyl-2,4-pentanediol, enzyme solution: 9 mg/ml, 20 mM TrisHCl, pH 7.0, 0.1 M KCl, 10 molar excess of solid 8, X-ray structure determination and analysis, structure model building and refinement, overview