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1-deoxy-L-glycero-tetrulose 4-phosphate + 5-amino-6-(D-ribitylamino)uracil
6,7-dimethyl-8-(D-ribityl)lumazine + 2 H2O + phosphate
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (3R)-3,4-dihydroxy-2-butanone 4-phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + 2 H2O + phosphate
-
-
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (3S)-3,4-dihydroxy-2-butanone
?
-
-
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + 5-nitro-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
?
-
-
-
-
?
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione + 3,4-dihydroxy-2-butanone 4-phosphate
6,7-dimethyl-8-ribityllumazine + 2 H2O + phosphate
-
-
-
?
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione + L-3,4-dihydroxybutan-2-one 4-phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + 2 H2O + phosphate
5-amino-6-ribitylamino-2,4-(1H,3H)-pyrimidinedione + 3,4-dihydroxy-2-butanone 4-phosphate
6,7-dimethyl-8-ribityllumazine + 2 H2O + phosphate
-
-
-
?
additional information
?
-
critical involvement of the active-site residues Phe22, His88 and Arg127 in substrate binding and catalysis
-
-
?
1-deoxy-L-glycero-tetrulose 4-phosphate + 5-amino-6-(D-ribitylamino)uracil
6,7-dimethyl-8-(D-ribityl)lumazine + 2 H2O + phosphate
-
-
-
?
1-deoxy-L-glycero-tetrulose 4-phosphate + 5-amino-6-(D-ribitylamino)uracil
6,7-dimethyl-8-(D-ribityl)lumazine + 2 H2O + phosphate
-
-
-
?
1-deoxy-L-glycero-tetrulose 4-phosphate + 5-amino-6-(D-ribitylamino)uracil
6,7-dimethyl-8-(D-ribityl)lumazine + 2 H2O + phosphate
-
-
-
?
1-deoxy-L-glycero-tetrulose 4-phosphate + 5-amino-6-(D-ribitylamino)uracil
6,7-dimethyl-8-(D-ribityl)lumazine + 2 H2O + phosphate
-
-
-
?
1-deoxy-L-glycero-tetrulose 4-phosphate + 5-amino-6-(D-ribitylamino)uracil
6,7-dimethyl-8-(D-ribityl)lumazine + 2 H2O + phosphate
-
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate
penultimate step of riboflavin biosynthesis
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate
-
penultimate step of riboflavin biosynthesis
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
penultimate step of riboflavin biosynthesis
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
penultimate step of riboflavin biosynthesis
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
penultimate step of riboflavin biosynthesis
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
penultimate step of riboflavin biosynthesis
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
-
-
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
penultimate step of riboflavin biosynthesis
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
-
the enzyme is involved in biosynthesis of riboflavin
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
-
-
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
-
penultimate step of riboflavin biosynthesis
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
penultimate step of riboflavin biosynthesis
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
penultimate step of riboflavin biosynthesis
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
-
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
-
-
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
-
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
-
penultimate step of riboflavin biosynthesis
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
-
lumazine synthase/riboflavin synthase complex, the beta subunit carries lumazine synthase activity. Product channeling for subsequent synthesis of riboflavin by riboflavin synthase present in the complex
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
-
the rate enhancement by the enzyme is predominantly achieved by establishing a favourable topological relation of the two substrates, whereas acid/base catalysis may play a secondary role
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
penultimate step of riboflavin biosynthesis
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
-
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
penultimate step of riboflavin biosynthesis
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
-
-
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
-
-
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
-
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
-
penultimate step in the biosynthesis of riboflavin. The type II lumazine synthase is an immunodominant antigen of Brucella abortus
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
-
penultimate step of riboflavin biosynthesis
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
-
the pathogen Brucella spp. expresses two proteins that exhibit lumazine synthase activity, RibH1 and RibH2. RibH1 appears to be the functional lumazine synthase in Brucella spp., whereas RibH2, an enzyme of lower catalytic activity, is a virulence factor presumably acting in response to oxidative stress
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
penultimate step of riboflavin biosynthesis
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
penultimate step of riboflavin biosynthesis
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
-
-
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
-
the enzyme is involved in riboflavin biosynthesis in many plants and microorganisms
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
penultimate step of riboflavin biosynthesis
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
penultimate step of riboflavin biosynthesis
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
penultimate step of riboflavin biosynthesis
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
penultimate step of riboflavin biosynthesis
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
penultimate step of riboflavin biosynthesis
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
penultimate step of riboflavin biosynthesis
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
penultimate step of riboflavin biosynthesis
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
penultimate step of riboflavin biosynthesis
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
penultimate step of riboflavin biosynthesis
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
-
-
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
-
the enzyme is involved in riboflavin biosynthesis
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
penultimate step of riboflavin biosynthesis
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
penultimate step of riboflavin biosynthesis
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
Halalkalibacterium halodurans
-
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
penultimate step of riboflavin biosynthesis
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
penultimate step of riboflavin biosynthesis
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
penultimate step of riboflavin biosynthesis
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
penultimate step of riboflavin biosynthesis
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
-
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
penultimate step of riboflavin biosynthesis
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
-
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
penultimate step of riboflavin biosynthesis
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
the enzyme is involved in biosynthesis of riboflavin
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
penultimate step of riboflavin biosynthesis
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
penultimate step of riboflavin biosynthesis
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
penultimate step of riboflavin biosynthesis
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
penultimate step of riboflavin biosynthesis
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
penultimate step of riboflavin biosynthesis
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
-
-
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
-
penultimate step of riboflavin biosynthesis
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
-
-
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
-
lumazine synthase catalyzes the penultimate step of riboflavin biosynthesis
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
penultimate step of riboflavin biosynthesis
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
penultimate step of riboflavin biosynthesis
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
penultimate step of riboflavin biosynthesis
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
penultimate step of riboflavin biosynthesis
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
penultimate step of riboflavin biosynthesis
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
penultimate step of riboflavin biosynthesis
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
penultimate step of riboflavin biosynthesis
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
penultimate step of riboflavin biosynthesis
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
penultimate step of riboflavin biosynthesis
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
-
-
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
-
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
-
the enzyme is involved in riboflavin biosynthesis
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
penultimate step of riboflavin biosynthesis
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
the enzyme is involved in biosynthesis of riboflavin. Gene disruption of the chromosomal copy of RIB4 leads to riboflavin auxotrophy and loss of enzyme activity
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
-
NMR studies of the binding of phosphonate reaction intermediate analogues to Saccharomyces cerevisiae lumazine synthase. The Lys92 side chain could facilitate the exchange of inorganic phosphate eliminated from the substrate in one reaction, with the organic phosphate-containing substrate necessary for the next reaction
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
-
-
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
-
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
penultimate step of riboflavin biosynthesis
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
penultimate step of riboflavin biosynthesis
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
-
-
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
-
lumazine synthase catalyzes the penultimate step of riboflavin biosynthesis
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
-
penultimate step of riboflavin biosynthesis
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
penultimate step of riboflavin biosynthesis
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
-
penultimate step of riboflavin biosynthesis
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
-
the enzyme is part of the riboflavin biosynthesis gene cluster
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
penultimate step of riboflavin biosynthesis
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
penultimate step of riboflavin biosynthesis
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
penultimate step of riboflavin biosynthesis
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
-
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
-
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
penultimate step of riboflavin biosynthesis
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
penultimate step of riboflavin biosynthesis
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
penultimate step of riboflavin biosynthesis
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
penultimate step of riboflavin biosynthesis
-
-
?
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione + L-3,4-dihydroxybutan-2-one 4-phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + 2 H2O + phosphate
-
-
-
-
?
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione + L-3,4-dihydroxybutan-2-one 4-phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + 2 H2O + phosphate
-
an early optical transient absorbing around 330 nm is interpreted as a Schiff base intermediate obtained by reaction of the position 5 amino group of the heterocyclic substrate with the carbonyl group of 3,4-dihydroxy-2-butanone 4-phosphate. A second transient with an absorption maximum at 445 nm represents an intermediate resulting from the elimination of phosphate from the Schiff base. The rate-determining step is the subsequent formation of the 7-exomethylene type anion of 6,7-dimethyl-8-ribityllumazine
-
-
?
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione + L-3,4-dihydroxybutan-2-one 4-phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + 2 H2O + phosphate
-
-
-
?
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione + L-3,4-dihydroxybutan-2-one 4-phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + 2 H2O + phosphate
-
-
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
1-deoxy-L-glycero-tetrulose 4-phosphate + 5-amino-6-(D-ribitylamino)uracil
6,7-dimethyl-8-(D-ribityl)lumazine + 2 H2O + phosphate
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate
penultimate step of riboflavin biosynthesis
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione + 3,4-dihydroxy-2-butanone 4-phosphate
6,7-dimethyl-8-ribityllumazine + 2 H2O + phosphate
-
-
-
?
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione + L-3,4-dihydroxybutan-2-one 4-phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + 2 H2O + phosphate
-
-
-
-
?
1-deoxy-L-glycero-tetrulose 4-phosphate + 5-amino-6-(D-ribitylamino)uracil
6,7-dimethyl-8-(D-ribityl)lumazine + 2 H2O + phosphate
-
-
-
?
1-deoxy-L-glycero-tetrulose 4-phosphate + 5-amino-6-(D-ribitylamino)uracil
6,7-dimethyl-8-(D-ribityl)lumazine + 2 H2O + phosphate
-
-
-
?
1-deoxy-L-glycero-tetrulose 4-phosphate + 5-amino-6-(D-ribitylamino)uracil
6,7-dimethyl-8-(D-ribityl)lumazine + 2 H2O + phosphate
-
-
-
?
1-deoxy-L-glycero-tetrulose 4-phosphate + 5-amino-6-(D-ribitylamino)uracil
6,7-dimethyl-8-(D-ribityl)lumazine + 2 H2O + phosphate
-
-
-
?
1-deoxy-L-glycero-tetrulose 4-phosphate + 5-amino-6-(D-ribitylamino)uracil
6,7-dimethyl-8-(D-ribityl)lumazine + 2 H2O + phosphate
-
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
penultimate step of riboflavin biosynthesis
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
penultimate step of riboflavin biosynthesis
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
penultimate step of riboflavin biosynthesis
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
penultimate step of riboflavin biosynthesis
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
penultimate step of riboflavin biosynthesis
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
-
the enzyme is involved in biosynthesis of riboflavin
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
-
penultimate step of riboflavin biosynthesis
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
penultimate step of riboflavin biosynthesis
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
penultimate step of riboflavin biosynthesis
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
-
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
-
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
-
penultimate step of riboflavin biosynthesis
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
penultimate step of riboflavin biosynthesis
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
-
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
penultimate step of riboflavin biosynthesis
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
-
penultimate step in the biosynthesis of riboflavin. The type II lumazine synthase is an immunodominant antigen of Brucella abortus
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
-
penultimate step of riboflavin biosynthesis
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
-
the pathogen Brucella spp. expresses two proteins that exhibit lumazine synthase activity, RibH1 and RibH2. RibH1 appears to be the functional lumazine synthase in Brucella spp., whereas RibH2, an enzyme of lower catalytic activity, is a virulence factor presumably acting in response to oxidative stress
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
penultimate step of riboflavin biosynthesis
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
penultimate step of riboflavin biosynthesis
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
-
the enzyme is involved in riboflavin biosynthesis in many plants and microorganisms
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
penultimate step of riboflavin biosynthesis
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
penultimate step of riboflavin biosynthesis
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
penultimate step of riboflavin biosynthesis
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
penultimate step of riboflavin biosynthesis
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
penultimate step of riboflavin biosynthesis
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
penultimate step of riboflavin biosynthesis
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
penultimate step of riboflavin biosynthesis
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
penultimate step of riboflavin biosynthesis
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
-
the enzyme is involved in riboflavin biosynthesis
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
penultimate step of riboflavin biosynthesis
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
penultimate step of riboflavin biosynthesis
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
Halalkalibacterium halodurans
-
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
penultimate step of riboflavin biosynthesis
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
penultimate step of riboflavin biosynthesis
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
penultimate step of riboflavin biosynthesis
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
penultimate step of riboflavin biosynthesis
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
penultimate step of riboflavin biosynthesis
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
the enzyme is involved in biosynthesis of riboflavin
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
penultimate step of riboflavin biosynthesis
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
penultimate step of riboflavin biosynthesis
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
penultimate step of riboflavin biosynthesis
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
penultimate step of riboflavin biosynthesis
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
penultimate step of riboflavin biosynthesis
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
-
penultimate step of riboflavin biosynthesis
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
-
lumazine synthase catalyzes the penultimate step of riboflavin biosynthesis
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
penultimate step of riboflavin biosynthesis
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
penultimate step of riboflavin biosynthesis
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
penultimate step of riboflavin biosynthesis
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
penultimate step of riboflavin biosynthesis
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
penultimate step of riboflavin biosynthesis
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
penultimate step of riboflavin biosynthesis
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
penultimate step of riboflavin biosynthesis
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
penultimate step of riboflavin biosynthesis
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
penultimate step of riboflavin biosynthesis
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
-
-
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
-
the enzyme is involved in riboflavin biosynthesis
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
penultimate step of riboflavin biosynthesis
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
the enzyme is involved in biosynthesis of riboflavin. Gene disruption of the chromosomal copy of RIB4 leads to riboflavin auxotrophy and loss of enzyme activity
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
-
-
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
-
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
penultimate step of riboflavin biosynthesis
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
penultimate step of riboflavin biosynthesis
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
-
lumazine synthase catalyzes the penultimate step of riboflavin biosynthesis
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
-
penultimate step of riboflavin biosynthesis
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
penultimate step of riboflavin biosynthesis
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
-
the enzyme is part of the riboflavin biosynthesis gene cluster
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
penultimate step of riboflavin biosynthesis
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
penultimate step of riboflavin biosynthesis
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
penultimate step of riboflavin biosynthesis
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
-
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
-
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
penultimate step of riboflavin biosynthesis
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
penultimate step of riboflavin biosynthesis
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
penultimate step of riboflavin biosynthesis
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
penultimate step of riboflavin biosynthesis
-
-
?
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(1R)-1,2-dideoxy-1-fluoro-1-(5-nitro-2,6-dioxo-1,2,3,6-tetrahydropyrimidin-4-yl)-D-ribo-hexitol
-
-
(1S)-1,2-dideoxy-1-fluoro-1-(5-nitro-2,6-dioxo-1,2,3,6-tetrahydropyrimidin-4-yl)-D-ribo-hexitol
(E)-3-hydroxy-4-(2-(5-nitro-2,6-dioxo-1,2,3,6-tetrahydropyrimidine-4-yl)vinyl)benzoic acid
(E)-4-(2-(5-nitro-2,6-dioxo-1,2,3,6-tetrahydropyrimidine-4-yl)vinyl)benzoate
-
-
(E)-4-(2-(5-nitro-2,6-dioxo-1,2,3,6-tetrahydropyrimidine-4-yl)vinyl)benzoic acid
-
-
(E)-5-nitro-6-(2-hydroxystyryl)pyrimidine-2,4(1H,3H)-dione
(E)-5-nitro-6-(3-(pyridin-3-yl)vinyl)pyrimidine-2,4(1H,3H)-dione
-
-
(E)-5-nitro-6-(3-nitrostyryl)pyrimidine-2,4(1H,3H)-dione
(E)-5-nitro-6-(4-bromostyryl)pyrimidine-2,4(1H,3H)-dione
-
-
(E)-5-nitro-6-(4-nitrostyryl)pyrimidine-2,4(1H,3H)-dione
(E)-5-nitro-6-[2-(1H-pyrrol-2-yl)vinyl]pyrimidine-2,4(1H,3H)-dione
(E)-6-(2,3,4-trimethoxystyryl)-5-nitropyrimidine-2,4(1H,3H)-dione
-
-
(E)-6-(2,3-dihydroxystyryl)-5-nitropyrimidine-2,4(1H,3H)-dione
(E)-6-(2,3-dimethoxystyryl)-5-nitropyrimidine-2,4(1H,3H)-dione
(E)-6-(2-(3H-indol-3-yl)vinyl)-5-nitropyrimidine-2,4(1H,3H)-dione
(E)-6-(2-(naphthalen-2-yl)vinyl)-5-nitropyrimidine-2,4(1H,3H)-dione
(E)-6-(2-fluoro-3-methoxystyryl)-5-nitropyrimidine-2,4(1H,3H)-dione
(E)-6-(2-fluorostyryl)-5-nitropyrimidine-2,4(1H,3H)-dione
-
-
(E)-6-(2-hydroxy-3-nitrostyryl)-3-nitropyrimidine-2,4(1H,3H)-dione
-
-
(E)-6-(2-hydroxy-5-nitrostyryl)-5-nitropyrimidine-2,4(1H,3H)-dione
-
-
(E)-6-(2-methoxy-5-nitrostyryl)-5-nitropyrimidine-2,4(1H,3H)-dione
(E)-6-(2-methoxystyryl)-5-nitropyrimidine-2,4(1H,3H)-dione
(E)-6-(2-nitrostyryl)-5-nitropyrimidine-2,4(1H,3H)-dione
-
-
(E)-6-(3,4,5-trimethoxystyryl)-5-nitropyrimidine-2,4(1H,3H)-dione
-
-
(E)-6-(3,4-dimethoxystyryl)-5-nitropyrimidine-2,4(1H,3H)-dione
-
-
(E)-6-(3-hydroxy-4-methoxystyryl)-5-nitropyrimidine-2,4(1H,3H)-dione
-
-
(E)-6-(3-hydroxy-4-nitrostyryl)-5-nitropyrimidine-2,4(1H,3H)-dione
(E)-6-(3-hydroxystyryl)-5-nitropyrimidine-2,4(1H,3H)-dione
-
competitive
(E)-6-(4-chlorostyryl)-5-nitropyrimidine-2,4(1H,3H)-dione
-
-
(E)-6-(4-fluorostyryl)-5-nitropyrimidine-2,4(1H,3H)-dione
-
-
(E)-6-(4-hydroxy-3-nitrostyryl)-5-nitropyrimidine-2,4(1H,3H)-dione
-
-
(E)-6-(4-hydroxystyryl)-5-nitropyrimidine-2,4(1H,3H)-dione
-
-
1,3,6,8-tetrahydroxynaphthyridine
-
-
1,3,7-trihydro-9-D-ribityl-2,4,8-purinetrione
1-deoxy-1-(2,4,6,7-tetraoxo-1,3,4,5,6,7-hexahydropteridin-8(2H)-yl)-D-ribitol
1-deoxy-1-(2,6,8-trioxo-1,2,3,6,7,8-hexahydro-9H-purin-9-yl)-D-ribitol
1-deoxy-1-[(2,6-dioxo-5-[[5-(phosphonooxy)pentanoyl]amino]-1,2,3,6-tetrahydropyrimidin-4-yl)amino]-D-ribitol
-
-
1-deoxy-1-[2,4,6,7-tetraoxo-5-[4-(phosphonooxy)butyl]-1,3,4,5,6,7-hexahydropteridin-8(2H)-yl]-D-ribitol
-
-
1-deoxy-1-[2,4,6,7-tetraoxo-5-[5-(phosphonooxy)pentyl]-1,3,4,5,6,7-hexahydropteridin-8(2H)-yl]-D-ribitol
-
-
1-deoxy-1-[2,6,8-trioxo-7-[4-(phosphonooxy)butyl]-1,2,3,6,7,8-hexahydro-9H-purin-9-yl]-D-ribitol
1-deoxy-1-[2,6,8-trioxo-7-[5-(phosphonooxy)pentyl]-1,2,3,6,7,8-hexahydro-9H-purin-9-yl]-D-ribitol
1-deoxy-1-[2,6,8-trioxo-7-[6-(phosphonooxy)hexyl]-1,2,3,6,7,8-hexahydro-9H-purin-9-yl]-D-ribitol
1-deoxy-1-[[2,6-dioxo-5-(4-phosphonobutyl)-1,2,3,6-tetrahydropyrimidin-4-yl]amino]-D-ribitol
-
-
1-deoxy-1-[[2,6-dioxo-5-(5-phosphonopentyl)-1,2,3,6-tetrahydropyrimidin-4-yl]amino]-D-ribitol
-
-
1-deoxy-1-[[2,6-dioxo-5-(6-phosphonohexyl)-1,2,3,6-tetrahydropyrimidin-4-yl]amino]-D-ribitol
-
-
1-[(5-amino-2,6-dioxo-1,2,3,6-tetrahydropyrimidin-4-yl)(methyl)amino]-1-deoxy-D-ribitol hydrochloride
2,4-dioxo-6-[[(2R,3R,4R)-2,3,4,5-tetrahydroxypentyl]sulfanyl]-1,2,3,4-tetrahydropyrimidin-5-aminium chloride
2,5,8,11-tetraaza-5,11-dihydro-4,10-dihydroxyperylene-1,3,6,7,9,12-hexaone
-
-
2-(2-oxo-1,2-dihydrobenzo[cd]indole-6-sulfonamido)acetic acid
-
possible lead compound for inhibitor screening
3-(1,3,7,9-tetrahydro-9-D-ribityl-2,6,8-trioxopurin-7-yl)-1-propanol
-
-
3-(1,3,7,9-tetrahydro-9-D-ribityl-2,6,8-trioxopurin-7-yl)propane 1-phosphate
3-(1,3,7-trihydro-9-D-ribityl-2,6,8-purinetrion-7-yl)butane 1-phosphate
-
highly specific binding of the purinetrione inhibitor to the Mycobacterium tuberculosis enzyme with dissociation constants in micromolar range
3-(1,3,7-trihydro-9-D-ribityl-2,6,8-purinetrione-7-yl)butane 1-phosphate
3-(1,3,7-trihydro-9-D-ribityl-2,6,8-purinetrione-7-yl)pentane 1-phosphate
3-(1,3,7-trihydro-9-D-ribityl-2,6,8-purinetrione-7-yl)propane 1-phosphate
-
highly specific binding of the purinetrione inhibitor to the Mycobacterium tuberculosis enzyme with dissociation constants in micromolar range
3-(1,3-dihydro-9-D-ribityl-2,4,8-purinetrione-7-yl)propane 1-phosphate
-
association constants and thermodynamic parameters of binding of different inhibitors to lumazine synthase
3-(7-hydroxy-8-ribityllumazine-6-yl)propionic acid
3-[4,6-dioxo-4,5,6,7-tetrahydro-1-D-ribityl-1H-pyrazolo[3,4-d]pyrimidin-3-yl]propyl 1-phosphate
4-(1,3,7,9-tetrahydro-9-D-ribityl-2,6,8-trioxopurin-7-yl)butane 1-phosphate
4-(1,5,6,7-tetrahydro-6,7-dioxo-8-D-ribityllumazin-5-yl)butane 1-phosphate
4-(2-oxo-1,2-dihydrobenzo[cd]indole-6-sulfonamido)butyl dihydrogen phosphate
-
mixed inhibition
4-(6,7(5H,8H)-dioxo-8-D-ribityllumazine-5-yl)butane 1-phosphate
-
association constants and thermodynamic parameters of binding of different inhibitors to lumazine synthase
4-(6-chloro-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)butyl dihydrogen phosphate
-
molecular modeling of binding to luminazine synthase. The main forces stabilizing the complex with the enzyme involve pi-pi stacking interactions with Trp27 and hydrogen bonding of the phosphates with Arg128, the backbone nitrogens of Gly85 and Gln86, and the side chain hydroxyl of Thr87
4-(6-chloro-2,4-dioxo-1,2,3,4-tetrahydropyrimidine-5-yl)-butyl phosphate
-
association constants and thermodynamic parameters of binding of different inhibitors to lumazine synthase
4-(6-chloro-2,4-dioxo-1,2,3,4-tetrahydropyrimidine-5-yl)-n-butyl 1-phosphate
-
competitive
4-(6-chloro-2,4-dioxo-1,2,3,4-tetrahydropyrimidine-5-yl)butyl 1-phosphate
-
association constants and thermodynamic parameters of binding
4-[2,4,7-trioxo-8-[(2S,3S,4R)-2,3,4,5-tetrahydroxypentyl]-1,2,3,4,7,8-hexahydropteridin-6-yl]butanoic acid
-
uncompetitive, comparison with inhibition of Escherichia coli riboflavin synthase
4-[2,4,7-trioxo-8-[(2S,3S,4R)-2,3,4,5-tetrahydroxypentyl]-1,2,3,4,7,8-hexahydropteridin-6-yl]butyl dihydrogen phosphate
-
competitive, comparison with inhibition of Escherichia coli riboflavin synthase
4-[2,4,7-trioxo-8-[(2S,3S,4R)-2,3,4,5-tetrahydroxypentyl]-1,2,3,4,7,8-hexahydropteridin-6-yl]propyl dihydrogen phosphate
-
uncompetitive, comparison with inhibition of Escherichia coli riboflavin synthase
4-[4,6-dioxo-4,5,6,7-tetrahydro1-D-ribityl-1H-pyrazolo[3,4-d]-pyrimidin-3-yl]butyl 1-phosphate
5-(1,3,7,9-tetrahydro-9-D-ribityl-2,6,8-trioxopurin-7-yl)-1,1-difluoropentane 1-phosphonate
5-(1,3,7-trihydro-9-d-ribityl-2,4,8-purinetrione-7-yl)1,1-difluoropentane-1-phosphate
-
association constants and thermodynamic parameters of binding
5-(1,3,7-trihydro-9-D-ribityl-2,4,8-purinetrione-7-yl)pentane1-phosphate
-
association constants and thermodynamic parameters of binding
5-(1,5,6,7-tetrahydro-6,7-dioxo-8-D-ribityllumazin-5-yl)pentane 1-phosphate
5-(4-phosphonobutyryl)amino-6-D-ribitylaminouracil
-
comparison with inhibition of Escherichia coli riboflavin synthase
5-(5-phosphonopentyl)amino-6-D-ribitylaminouracil
-
comparison with inhibition of Escherichia coli riboflavin synthase
5-(5-phosphonoxyvaleryl)amino-6-D-ribitylaminouracil
-
mixed inhibition, comparison with inhibition of Escherichia coli riboflavin synthase
5-(6-chloro-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-5-oxopentyl phosphate
-
competitive
5-(6-chloro-2,4-dioxo-1,2,3,4-tetrahydropyrimidine-5-yl)-n-pentyl 1-phosphonate
-
competitive
5-(6-D-ribitylamino-2,4(1H,3H)pyrimidinedione-5-yl)-1-pentyl-phosphonic acid
-
-
5-(hexyl 6-dihydrogen phosphate)-6-([(2S,3S,4R)-2,3,4,5-tetrahydroxypentyl]amino)pyrimidine-2,4(1H,3H)-dione
-
mixed inhibition, comparison with inhibition of Escherichia coli riboflavin synthase
5-(pentyl 6-dihydrogen phosphate)-6-([(2S,3S,4R)-2,3,4,5-tetrahydroxypentyl]amino)pyrimidine-2,4(1H,3H)-dione
-
mixed inhibition, comparison with inhibition of Escherichia coli riboflavin synthase
5-nitro-6-(D-ribitylamino)-2,4(1H,3H)-pyrimidinedione
5-nitro-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
5-nitro-6-[(D-ribityl)methyl]pyrimidine-2,4-dione
-
-
5-nitro-6-[[(2R,3R,4R)-2,3,4,5 tetrahydroxypentyl]sulfanyl]pyrimidine-2,4(1H,3H)-dione
5-nitroso-6-(D-ribitylamino)-2,4(1H,3H)-pyrimidinedione
-
-
5-nitroso-6-ribityl-amino-2,4(1H,3H)pyrimidinedione
-
-
5-[4,6-dioxo-4,5,6,7-tetrahydro-1-D-ribityl-1H-pyrazolo[3,4-d]pyrimidin-3-yl]pentyl 1-phosphate
6,7-dioxo-5H-8-ribitylaminolumazine
-
-
6-(1,3,7-trihydro-9-d-ribityl-2,4,8-purinetrione-7-yl)hexane 1-phosphate
-
association constants and thermodynamic parameters of binding
6-carboxyethyl-7-oxo-8-ribityllumazine
-
-
6-methyl-7-methylidene-8-[(2S,3S,4R)-2,3,4,5-tetrahydroxypentyl]-7,8-dihydropyrido[2,3-d]pyrimidine-2,4(1H,3H)-dione
-
mixed inhibition, comparison with inhibition of Escherichia coli riboflavin synthase
8-[[(2S,3S,4R)-2,3,4,5-tetrahydroxypentyl]amino]tetrahydropteridine-2,4,6,7(1H,3H)-tetrone
9-[(2S,3S,4R)-2,3,4,5-tetrahydroxypentyl]-7,9-dihydro-1H-purine-2,6,8(3H)-trione
-
comparison with inhibition of Escherichia coli riboflavin synthase
ethyl [(2,4-dioxo-6-[[(2S,3S,4R)-2,3,4,5-tetrahydroxypentyl]amino]-1,2,3,4-tetrahydropyrimidin-5-yl)amino](oxo)acetate
N-6-(ribitylamino)pyrimidine-2,4(1H,3H)-dion-5-ylpropionamide
N-6-(ribitylamino)pyrimidine-2,4(1H,3H)-dione-5-ylisobutyramide
N-[2,4-dioxo-6-(ribitylamino)-1,2,3,4-tetrahydropyrimidin-5-yl]oxalamic acid ethyl ester
(1S)-1,2-dideoxy-1-fluoro-1-(5-nitro-2,6-dioxo-1,2,3,6-tetrahydropyrimidin-4-yl)-D-ribo-hexitol
-
-
(1S)-1,2-dideoxy-1-fluoro-1-(5-nitro-2,6-dioxo-1,2,3,6-tetrahydropyrimidin-4-yl)-D-ribo-hexitol
-
-
(E)-3-hydroxy-4-(2-(5-nitro-2,6-dioxo-1,2,3,6-tetrahydropyrimidine-4-yl)vinyl)benzoic acid
-
-
(E)-3-hydroxy-4-(2-(5-nitro-2,6-dioxo-1,2,3,6-tetrahydropyrimidine-4-yl)vinyl)benzoic acid
-
-
(E)-5-nitro-6-(2-hydroxystyryl)pyrimidine-2,4(1H,3H)-dione
-
competitive
(E)-5-nitro-6-(2-hydroxystyryl)pyrimidine-2,4(1H,3H)-dione
-
competitive
(E)-5-nitro-6-(3-nitrostyryl)pyrimidine-2,4(1H,3H)-dione
-
-
(E)-5-nitro-6-(3-nitrostyryl)pyrimidine-2,4(1H,3H)-dione
-
-
(E)-5-nitro-6-(4-nitrostyryl)pyrimidine-2,4(1H,3H)-dione
-
-
(E)-5-nitro-6-(4-nitrostyryl)pyrimidine-2,4(1H,3H)-dione
-
-
(E)-5-nitro-6-[2-(1H-pyrrol-2-yl)vinyl]pyrimidine-2,4(1H,3H)-dione
-
-
(E)-5-nitro-6-[2-(1H-pyrrol-2-yl)vinyl]pyrimidine-2,4(1H,3H)-dione
-
-
(E)-6-(2,3-dihydroxystyryl)-5-nitropyrimidine-2,4(1H,3H)-dione
-
-
(E)-6-(2,3-dihydroxystyryl)-5-nitropyrimidine-2,4(1H,3H)-dione
-
-
(E)-6-(2,3-dimethoxystyryl)-5-nitropyrimidine-2,4(1H,3H)-dione
-
-
(E)-6-(2,3-dimethoxystyryl)-5-nitropyrimidine-2,4(1H,3H)-dione
-
-
(E)-6-(2-(3H-indol-3-yl)vinyl)-5-nitropyrimidine-2,4(1H,3H)-dione
-
-
(E)-6-(2-(3H-indol-3-yl)vinyl)-5-nitropyrimidine-2,4(1H,3H)-dione
-
-
(E)-6-(2-(naphthalen-2-yl)vinyl)-5-nitropyrimidine-2,4(1H,3H)-dione
-
-
(E)-6-(2-(naphthalen-2-yl)vinyl)-5-nitropyrimidine-2,4(1H,3H)-dione
-
-
(E)-6-(2-fluoro-3-methoxystyryl)-5-nitropyrimidine-2,4(1H,3H)-dione
-
-
(E)-6-(2-fluoro-3-methoxystyryl)-5-nitropyrimidine-2,4(1H,3H)-dione
-
-
(E)-6-(2-methoxy-5-nitrostyryl)-5-nitropyrimidine-2,4(1H,3H)-dione
-
-
(E)-6-(2-methoxy-5-nitrostyryl)-5-nitropyrimidine-2,4(1H,3H)-dione
-
-
(E)-6-(2-methoxystyryl)-5-nitropyrimidine-2,4(1H,3H)-dione
-
-
(E)-6-(2-methoxystyryl)-5-nitropyrimidine-2,4(1H,3H)-dione
-
-
(E)-6-(3-hydroxy-4-nitrostyryl)-5-nitropyrimidine-2,4(1H,3H)-dione
-
-
(E)-6-(3-hydroxy-4-nitrostyryl)-5-nitropyrimidine-2,4(1H,3H)-dione
-
-
1,3,7-trihydro-9-D-ribityl-2,4,8-purinetrione
-
association constants and thermodynamic parameters of binding of different inhibitors to lumazine synthase
1,3,7-trihydro-9-D-ribityl-2,4,8-purinetrione
-
association constants and thermodynamic parameters of binding
1-deoxy-1-(2,4,6,7-tetraoxo-1,3,4,5,6,7-hexahydropteridin-8(2H)-yl)-D-ribitol
-
-
1-deoxy-1-(2,4,6,7-tetraoxo-1,3,4,5,6,7-hexahydropteridin-8(2H)-yl)-D-ribitol
-
-
1-deoxy-1-(2,6,8-trioxo-1,2,3,6,7,8-hexahydro-9H-purin-9-yl)-D-ribitol
-
-
1-deoxy-1-(2,6,8-trioxo-1,2,3,6,7,8-hexahydro-9H-purin-9-yl)-D-ribitol
-
-
1-deoxy-1-[2,6,8-trioxo-7-[4-(phosphonooxy)butyl]-1,2,3,6,7,8-hexahydro-9H-purin-9-yl]-D-ribitol
-
-
1-deoxy-1-[2,6,8-trioxo-7-[4-(phosphonooxy)butyl]-1,2,3,6,7,8-hexahydro-9H-purin-9-yl]-D-ribitol
-
-
1-deoxy-1-[2,6,8-trioxo-7-[5-(phosphonooxy)pentyl]-1,2,3,6,7,8-hexahydro-9H-purin-9-yl]-D-ribitol
-
-
1-deoxy-1-[2,6,8-trioxo-7-[5-(phosphonooxy)pentyl]-1,2,3,6,7,8-hexahydro-9H-purin-9-yl]-D-ribitol
-
-
1-deoxy-1-[2,6,8-trioxo-7-[6-(phosphonooxy)hexyl]-1,2,3,6,7,8-hexahydro-9H-purin-9-yl]-D-ribitol
-
-
1-deoxy-1-[2,6,8-trioxo-7-[6-(phosphonooxy)hexyl]-1,2,3,6,7,8-hexahydro-9H-purin-9-yl]-D-ribitol
-
-
1-[(5-amino-2,6-dioxo-1,2,3,6-tetrahydropyrimidin-4-yl)(methyl)amino]-1-deoxy-D-ribitol hydrochloride
-
-
1-[(5-amino-2,6-dioxo-1,2,3,6-tetrahydropyrimidin-4-yl)(methyl)amino]-1-deoxy-D-ribitol hydrochloride
-
-
2,4-dioxo-6-[[(2R,3R,4R)-2,3,4,5-tetrahydroxypentyl]sulfanyl]-1,2,3,4-tetrahydropyrimidin-5-aminium chloride
-
inhibition of both lumazine synthase and riboflavin synthase
2,4-dioxo-6-[[(2R,3R,4R)-2,3,4,5-tetrahydroxypentyl]sulfanyl]-1,2,3,4-tetrahydropyrimidin-5-aminium chloride
-
inhibition of both lumazine synthase and riboflavin synthase
2,4-dioxo-6-[[(2R,3R,4R)-2,3,4,5-tetrahydroxypentyl]sulfanyl]-1,2,3,4-tetrahydropyrimidin-5-aminium chloride
-
inhibition of both lumazine synthase and riboflavin synthase
3-(1,3,7,9-tetrahydro-9-D-ribityl-2,6,8-trioxopurin-7-yl)propane 1-phosphate
-
-
3-(1,3,7,9-tetrahydro-9-D-ribityl-2,6,8-trioxopurin-7-yl)propane 1-phosphate
-
-
3-(1,3,7-trihydro-9-D-ribityl-2,6,8-purinetrione-7-yl)butane 1-phosphate
-
competitive
3-(1,3,7-trihydro-9-D-ribityl-2,6,8-purinetrione-7-yl)butane 1-phosphate
-
competitive
3-(1,3,7-trihydro-9-D-ribityl-2,6,8-purinetrione-7-yl)butane 1-phosphate
-
competitive
3-(1,3,7-trihydro-9-D-ribityl-2,6,8-purinetrione-7-yl)pentane 1-phosphate
-
competitive
3-(1,3,7-trihydro-9-D-ribityl-2,6,8-purinetrione-7-yl)pentane 1-phosphate
-
competitive
3-(1,3,7-trihydro-9-D-ribityl-2,6,8-purinetrione-7-yl)pentane 1-phosphate
-
competitive
3-(7-hydroxy-8-ribityllumazine-6-yl)propionic acid
-
-
3-(7-hydroxy-8-ribityllumazine-6-yl)propionic acid
binding structure, overview
3-[4,6-dioxo-4,5,6,7-tetrahydro-1-D-ribityl-1H-pyrazolo[3,4-d]pyrimidin-3-yl]propyl 1-phosphate
-
competitive
3-[4,6-dioxo-4,5,6,7-tetrahydro-1-D-ribityl-1H-pyrazolo[3,4-d]pyrimidin-3-yl]propyl 1-phosphate
-
competitive
3-[4,6-dioxo-4,5,6,7-tetrahydro-1-D-ribityl-1H-pyrazolo[3,4-d]pyrimidin-3-yl]propyl 1-phosphate
-
mixed type inhibition
4-(1,3,7,9-tetrahydro-9-D-ribityl-2,6,8-trioxopurin-7-yl)butane 1-phosphate
-
-
4-(1,3,7,9-tetrahydro-9-D-ribityl-2,6,8-trioxopurin-7-yl)butane 1-phosphate
-
-
4-(1,5,6,7-tetrahydro-6,7-dioxo-8-D-ribityllumazin-5-yl)butane 1-phosphate
-
-
4-(1,5,6,7-tetrahydro-6,7-dioxo-8-D-ribityllumazin-5-yl)butane 1-phosphate
-
-
4-[4,6-dioxo-4,5,6,7-tetrahydro1-D-ribityl-1H-pyrazolo[3,4-d]-pyrimidin-3-yl]butyl 1-phosphate
-
competitive
4-[4,6-dioxo-4,5,6,7-tetrahydro1-D-ribityl-1H-pyrazolo[3,4-d]-pyrimidin-3-yl]butyl 1-phosphate
-
competitive
5-(1,3,7,9-tetrahydro-9-D-ribityl-2,6,8-trioxopurin-7-yl)-1,1-difluoropentane 1-phosphonate
-
-
5-(1,3,7,9-tetrahydro-9-D-ribityl-2,6,8-trioxopurin-7-yl)-1,1-difluoropentane 1-phosphonate
-
-
5-(1,5,6,7-tetrahydro-6,7-dioxo-8-D-ribityllumazin-5-yl)pentane 1-phosphate
-
-
5-(1,5,6,7-tetrahydro-6,7-dioxo-8-D-ribityllumazin-5-yl)pentane 1-phosphate
-
-
5-nitro-6-(D-ribitylamino)-2,4(1H,3H)-pyrimidinedione
-
-
5-nitro-6-(D-ribitylamino)-2,4(1H,3H)-pyrimidinedione
-
-
5-nitro-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
crystallization data
5-nitro-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
crystallization data
5-nitro-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
crystallization data; crystallization data
5-nitro-6-styryluracil
-
-
5-nitro-6-styryluracil
-
-
5-nitro-6-[[(2R,3R,4R)-2,3,4,5 tetrahydroxypentyl]sulfanyl]pyrimidine-2,4(1H,3H)-dione
-
inhibition of both lumazine synthase and riboflavin synthase
5-nitro-6-[[(2R,3R,4R)-2,3,4,5 tetrahydroxypentyl]sulfanyl]pyrimidine-2,4(1H,3H)-dione
-
inhibition of both lumazine synthase and riboflavin synthase
5-nitro-6-[[(2R,3R,4R)-2,3,4,5 tetrahydroxypentyl]sulfanyl]pyrimidine-2,4(1H,3H)-dione
-
inhibition of both lumazine synthase and riboflavin synthase
5-[4,6-dioxo-4,5,6,7-tetrahydro-1-D-ribityl-1H-pyrazolo[3,4-d]pyrimidin-3-yl]pentyl 1-phosphate
-
competitive
5-[4,6-dioxo-4,5,6,7-tetrahydro-1-D-ribityl-1H-pyrazolo[3,4-d]pyrimidin-3-yl]pentyl 1-phosphate
-
competitive
8-[[(2S,3S,4R)-2,3,4,5-tetrahydroxypentyl]amino]tetrahydropteridine-2,4,6,7(1H,3H)-tetrone
-
competitive
8-[[(2S,3S,4R)-2,3,4,5-tetrahydroxypentyl]amino]tetrahydropteridine-2,4,6,7(1H,3H)-tetrone
-
competitive
ethyl [(2,4-dioxo-6-[[(2S,3S,4R)-2,3,4,5-tetrahydroxypentyl]amino]-1,2,3,4-tetrahydropyrimidin-5-yl)amino](oxo)acetate
-
competitive
ethyl [(2,4-dioxo-6-[[(2S,3S,4R)-2,3,4,5-tetrahydroxypentyl]amino]-1,2,3,4-tetrahydropyrimidin-5-yl)amino](oxo)acetate
-
partial inhibition
ethyl [(2,4-dioxo-6-[[(2S,3S,4R)-2,3,4,5-tetrahydroxypentyl]amino]-1,2,3,4-tetrahydropyrimidin-5-yl)amino](oxo)acetate
mixed type inhibition
N-6-(ribitylamino)pyrimidine-2,4(1H,3H)-dion-5-ylpropionamide
-
partial inhibition, inhibition of both lumazine synthase and riboflavin synthase
N-6-(ribitylamino)pyrimidine-2,4(1H,3H)-dion-5-ylpropionamide
-
competitive, inhibition of both lumazine synthase and riboflavin synthase (EC 2.5.1.9)
N-6-(ribitylamino)pyrimidine-2,4(1H,3H)-dion-5-ylpropionamide
-
competitive, inhibition of both lumazine synthase and riboflavin synthase
N-6-(ribitylamino)pyrimidine-2,4(1H,3H)-dione-5-ylisobutyramide
-
partial inhibition, inhibition of both lumazine synthase and riboflavin synthase
N-6-(ribitylamino)pyrimidine-2,4(1H,3H)-dione-5-ylisobutyramide
-
partial inhibition, inhibition of both lumazine synthase and riboflavin synthase (EC 2.5.1.9)
N-6-(ribitylamino)pyrimidine-2,4(1H,3H)-dione-5-ylisobutyramide
-
competitive, inhibition of both lumazine synthase and riboflavin synthase
N-[2,4-dioxo-6-(ribitylamino)-1,2,3,4-tetrahydropyrimidin-5-yl]oxalamic acid ethyl ester
-
competitive, inhibition of both lumazine synthase and riboflavin synthase
N-[2,4-dioxo-6-(ribitylamino)-1,2,3,4-tetrahydropyrimidin-5-yl]oxalamic acid ethyl ester
-
partial inhibition, inhibition of both lumazine synthase and riboflavin synthase (EC 2.5.1.9)
N-[2,4-dioxo-6-(ribitylamino)-1,2,3,4-tetrahydropyrimidin-5-yl]oxalamic acid ethyl ester
-
mixed type inhibition, inhibition of both lumazine synthase and riboflavin synthase
additional information
-
incorporation of an amide into 5-phosphonoalkyl-6-D-ribitylaminopyrimidinedione lumazine synthase inhibitors results in an unexpected reversal of selectivity for riboflavin synthase versus lumazine synthase
-
additional information
-
certain purinetriones bearing phosphate side chains can inhibit both lumazine synthase as well as riboflavin synthase, and molecular modeling with 3-(1,3,7,9-tetrahydro-9-D-ribityl-2,6,8-trioxopurin-7-yl)propane 1-phosphate suggests possible binding modes to each enzyme. Antibiotics that would inhibit both lumazine synthase and riboflavin synthase would be less likely to suffer from the development of antibiotic resistance by the organisms that they are supposed to treat, since pathogenic microorganisms would have to simultaneously select for mutations in both enzymes in order to escape the cytotoxic effects of the antibiotics
-
additional information
-
no inhibition: 5-amino-6-[(D-ribityl)methyl]pyrimidine-2,4-dione hydrochloride, 5-nitro-6-(N-methyl)ribitylpyrimidine-2,4-dione
-
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0.13
(3S)-3,4-dihydroxy-2-butanone
-
native enzyme complex, pH 7.0, 37°C
0.0025 - 0.72
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
0.005
5-nitro-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
native enzyme complex, pH 7.0, 37°C
0.0052 - 3.14
L-3,4-dihydroxybutan-2-one 4-phosphate
additional information
additional information
-
0.0025
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
isoform RibH1, pH 7.0, 37°C
0.003
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
pH 7.0, 37°C, mutant enzyme W27F
0.003
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
pH 7.0, 37°C, mutant enzyme W27Y
0.004
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
-
0.004
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
pH 7.0, 37°C
0.0041
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
pH 7.0, 37°C, mutant enzyme T80V
0.0042
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
-
0.0042
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
pH 7.0, 37°C, mutant enzyme A56S
0.005
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
pH 7.0, 37°C, wild-type enzyme
0.00612
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
pH 7.0, 37°C, mutant enzyme F22W
0.00857
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
pH 7.0, 37°C, wild-type enzyme
0.01
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
37°C, pH 7.0
0.01
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
pH 7.0, 37°C, mutant enzyme D138A
0.0107
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
pH 7.0, 37°C, mutant enzyme F22V
0.011
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
pH 7.0, 37°C, mutant enzyme S142L
0.0115
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
pH 7.0, 37°C, mutant enzyme K135A
0.0119
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
pH 7.0, 37°C, mutant enzyme N23S
0.0125
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
37°C, pH 7.0
0.0138
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
pH 7.0, 37°C, mutant enzyme K131R
0.02
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
-
0.02
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
isoform RibH2, pH 7.0, 37°C
0.0345
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
pH 7.0, 37°C, mutant enzyme F57S
0.0355
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
pH 7.0, 37°C, mutant enzyme K131N
0.056
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
pH 7.0, 37°C, mutant enzyme H88K
0.0849
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
pH 7.0, 37°C, mutant enzyme R127H
0.09
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
-
0.14
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
pH 7.0, 37°C, mutant enzyme F22S
0.147
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
pH 7.0, 37°C, mutant enzyme H88A
0.173
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
pH 7.0, 37°C, mutant enzyme E58Q
0.23
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
pH 7.0, 37°C, mutant enzyme W27I
0.278
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
pH 7.0, 37°C, mutant enzyme F113S
0.4
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
pH 7.0, 37°C, mutant enzyme W27H
0.43
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
pH 7.0, 37°C, mutant enzyme W27G
0.46
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
pH 7.0, 37°C, mutant enzyme W27S
0.72
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
pH 7.0, 37°C, mutant enzyme F22D
0.0052
L-3,4-dihydroxybutan-2-one 4-phosphate
-
pH 7.0, 37°C, Tris buffer
0.0052
L-3,4-dihydroxybutan-2-one 4-phosphate
-
pH 7.0, 37°C, Tris buffer
0.0067
L-3,4-dihydroxybutan-2-one 4-phosphate
-
pH 7.0, 37°C, MOPS buffer
0.0067
L-3,4-dihydroxybutan-2-one 4-phosphate
-
pH 7.0, 37°C, MOPS buffer
0.015
L-3,4-dihydroxybutan-2-one 4-phosphate
isoform RibH1, pH 7.0, 37°C
0.026
L-3,4-dihydroxybutan-2-one 4-phosphate
-
-
0.026
L-3,4-dihydroxybutan-2-one 4-phosphate
-
37°C, pH 7.0
0.042
L-3,4-dihydroxybutan-2-one 4-phosphate
-
pH 7.0, 37°C, mutant enzyme H88K
0.042
L-3,4-dihydroxybutan-2-one 4-phosphate
-
pH 7.0, 37°C, mutant enzyme T80V
0.05
L-3,4-dihydroxybutan-2-one 4-phosphate
-
pH 7.0, 37°C, mutant enzyme K131R
0.05
L-3,4-dihydroxybutan-2-one 4-phosphate
-
pH 7.0, 37°C, phosphate buffer
0.05
L-3,4-dihydroxybutan-2-one 4-phosphate
-
pH 7.0, 37°C, phosphate buffer
0.052
L-3,4-dihydroxybutan-2-one 4-phosphate
37°C, pH 7.0
0.0546
L-3,4-dihydroxybutan-2-one 4-phosphate
-
pH 7.0, 37°C, wild-type enzyme
0.0581
L-3,4-dihydroxybutan-2-one 4-phosphate
-
pH 7.0, 37°C, mutant enzyme N23S
0.0598
L-3,4-dihydroxybutan-2-one 4-phosphate
-
pH 7.0, 37°C, mutant enzyme F22W
0.06
L-3,4-dihydroxybutan-2-one 4-phosphate
-
pH 7.0, 37°C, mutant enzyme H88A
0.062
L-3,4-dihydroxybutan-2-one 4-phosphate
-
-
0.0636
L-3,4-dihydroxybutan-2-one 4-phosphate
-
pH 7.0, 37°C, mutant enzyme D138A
0.065
L-3,4-dihydroxybutan-2-one 4-phosphate
pH 7.0, 37°C, mutant enzyme W27F
0.0665
L-3,4-dihydroxybutan-2-one 4-phosphate
-
pH 7.0, 37°C, mutant enzyme F113S
0.067
L-3,4-dihydroxybutan-2-one 4-phosphate
pH 7.0, 37°C, wild-type enzyme
0.0702
L-3,4-dihydroxybutan-2-one 4-phosphate
-
pH 7.0, 37°C, mutant enzyme A56S
0.08
L-3,4-dihydroxybutan-2-one 4-phosphate
-
pH 7.0, 37°C, mutant enzyme F57S
0.086
L-3,4-dihydroxybutan-2-one 4-phosphate
pH 7.0, 37°C, mutant enzyme W27Y
0.09
L-3,4-dihydroxybutan-2-one 4-phosphate
-
-
0.0905
L-3,4-dihydroxybutan-2-one 4-phosphate
-
pH 7.0, 37°C, mutant enzyme S142L
0.124
L-3,4-dihydroxybutan-2-one 4-phosphate
-
pH 7.0, 37°C, mutant enzyme F22V
0.125
L-3,4-dihydroxybutan-2-one 4-phosphate
-
-
0.137
L-3,4-dihydroxybutan-2-one 4-phosphate
-
pH 7.0, 37°C, mutant enzyme F22S
0.137
L-3,4-dihydroxybutan-2-one 4-phosphate
pH 7.0, 37°C, mutant enzyme W27I
0.145
L-3,4-dihydroxybutan-2-one 4-phosphate
pH 7.0, 37°C, mutant enzyme W27H
0.146
L-3,4-dihydroxybutan-2-one 4-phosphate
-
pH 7.0, 37°C, mutant enzyme E58Q
0.167
L-3,4-dihydroxybutan-2-one 4-phosphate
-
pH 7.0, 37°C, mutant enzyme K135A
0.168
L-3,4-dihydroxybutan-2-one 4-phosphate
pH 7.0, 37°C, mutant enzyme W27G
0.187
L-3,4-dihydroxybutan-2-one 4-phosphate
pH 7.0, 37°C, mutant enzyme W27S
0.225
L-3,4-dihydroxybutan-2-one 4-phosphate
-
pH 7.0, 37°C
0.283
L-3,4-dihydroxybutan-2-one 4-phosphate
-
pH 7.0, 37°C, mutant enzyme K131N
0.45
L-3,4-dihydroxybutan-2-one 4-phosphate
isoform RibH2, pH 7.0, 37°C
0.675
L-3,4-dihydroxybutan-2-one 4-phosphate
-
pH 7.0, 37°C, mutant enzyme F22D
3.14
L-3,4-dihydroxybutan-2-one 4-phosphate
-
pH 7.0, 37°C, mutant enzyme R127H
additional information
additional information
steady-state kinetics, and kinetic modelling of the interaction of the single enzymes and identification of rate-limiting steps in the biosynthetic pathway, detailed overview
-
additional information
additional information
-
steady-state kinetics, and kinetic modelling of the interaction of the single enzymes and identification of rate-limiting steps in the biosynthetic pathway, detailed overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.0003 - 0.0557
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
0.056 - 0.076
5-nitro-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
0.0022 - 0.076
L-3,4-dihydroxybutan-2-one 4-phosphate
0.0003
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
isoform RibH2, pH 7.0, 37°C
0.0022
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
pH 7.0, 37°C, mutant enzyme H88K
0.003
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
pH 7.0, 37°C
0.0038
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
pH 7.0, 37°C, mutant enzyme F113S
0.0054
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
pH 7.0, 37°C, mutant enzyme K131N
0.0067
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
pH 7.0, 37°C, mutant enzyme H88A
0.0081
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
pH 7.0, 37°C, mutant enzyme F22D
0.0122
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
pH 7.0, 37°C, mutant enzyme K135A
0.0122
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
pH 7.0, 37°C, mutant enzyme N23S
0.0147
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
pH 7.0, 37°C, mutant enzyme F22V
0.0166
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
pH 7.0, 37°C, mutant enzyme K131R
0.0244
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
pH 7.0, 37°C, mutant enzyme F22W
0.0244
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
pH 7.0, 37°C, mutant enzyme F57S
0.0263
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
pH 7.0, 37°C, mutant enzyme F22S
0.0307
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
pH 7.0, 37°C, mutant enzyme T80V
0.0347
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
pH 7.0, 37°C, mutant enzyme S142L
0.0389
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
pH 7.0, 37°C, mutant enzyme R127H
0.0391
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
pH 7.0, 37°C, mutant enzyme E58Q
0.04
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
isoform RibH1, pH 7.0, 37°C
0.0453
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
pH 7.0, 37°C, mutant enzyme A56S
0.051
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
pH 7.0, 37°C, mutant enzyme D138A
0.0557
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
pH 7.0, 37°C, wild-type enzyme
0.056
5-nitro-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
native enzyme complex, pH 7.0, 37°C
0.076
5-nitro-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
hollow beta60 capsid, pH 7.0, 37°C
0.0022
L-3,4-dihydroxybutan-2-one 4-phosphate
-
pH 7.0, 37°C, mutant enzyme H88K
0.0038
L-3,4-dihydroxybutan-2-one 4-phosphate
-
pH 7.0, 37°C, mutant enzyme F113S
0.0054
L-3,4-dihydroxybutan-2-one 4-phosphate
-
pH 7.0, 37°C, mutant enzyme K131N
0.0067
L-3,4-dihydroxybutan-2-one 4-phosphate
-
pH 7.0, 37°C, mutant enzyme H88A
0.0081
L-3,4-dihydroxybutan-2-one 4-phosphate
-
pH 7.0, 37°C, mutant enzyme F22D
0.0122
L-3,4-dihydroxybutan-2-one 4-phosphate
-
pH 7.0, 37°C, mutant enzyme K135A
0.0122
L-3,4-dihydroxybutan-2-one 4-phosphate
-
pH 7.0, 37°C, mutant enzyme N23S
0.0147
L-3,4-dihydroxybutan-2-one 4-phosphate
-
pH 7.0, 37°C, mutant enzyme F22V
0.0166
L-3,4-dihydroxybutan-2-one 4-phosphate
-
pH 7.0, 37°C, mutant enzyme K131R
0.0244
L-3,4-dihydroxybutan-2-one 4-phosphate
-
pH 7.0, 37°C, mutant enzyme F22W
0.0244
L-3,4-dihydroxybutan-2-one 4-phosphate
-
pH 7.0, 37°C, mutant enzyme F57S
0.0263
L-3,4-dihydroxybutan-2-one 4-phosphate
-
pH 7.0, 37°C, mutant enzyme F22S
0.0307
L-3,4-dihydroxybutan-2-one 4-phosphate
-
pH 7.0, 37°C, mutant enzyme T80V
0.0347
L-3,4-dihydroxybutan-2-one 4-phosphate
-
pH 7.0, 37°C, mutant enzyme S142L
0.0389
L-3,4-dihydroxybutan-2-one 4-phosphate
-
pH 7.0, 37°C, mutant enzyme R127H
0.0391
L-3,4-dihydroxybutan-2-one 4-phosphate
-
pH 7.0, 37°C, mutant enzyme E58Q
0.0453
L-3,4-dihydroxybutan-2-one 4-phosphate
-
pH 7.0, 37°C, mutant enzyme A56S
0.051
L-3,4-dihydroxybutan-2-one 4-phosphate
-
pH 7.0, 37°C, mutant enzyme D138A
0.0557
L-3,4-dihydroxybutan-2-one 4-phosphate
-
pH 7.0, 37°C, wild-type enzyme
0.056
L-3,4-dihydroxybutan-2-one 4-phosphate
-
native enzyme complex, pH 7.0, 37°C
0.076
L-3,4-dihydroxybutan-2-one 4-phosphate
-
hollow beta60 capsid, pH 7.0, 37°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.113
(1R)-1,2-dideoxy-1-fluoro-1-(5-nitro-2,6-dioxo-1,2,3,6-tetrahydropyrimidin-4-yl)-D-ribo-hexitol
-
pH 7.0, 37°C, variable concentration of 5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
0.074 - 0.221
(1S)-1,2-dideoxy-1-fluoro-1-(5-nitro-2,6-dioxo-1,2,3,6-tetrahydropyrimidin-4-yl)-D-ribo-hexitol
0.13 - 0.197
(E)-3-hydroxy-4-(2-(5-nitro-2,6-dioxo-1,2,3,6-tetrahydropyrimidine-4-yl)vinyl)benzoic acid
0.041
(E)-4-(2-(5-nitro-2,6-dioxo-1,2,3,6-tetrahydropyrimidine-4-yl)vinyl)benzoate
-
pH 7.0, 27°C
0.035
(E)-4-(2-(5-nitro-2,6-dioxo-1,2,3,6-tetrahydropyrimidine-4-yl)vinyl)benzoic acid
-
pH 7.0, 27°C
0.095 - 0.21
(E)-5-nitro-6-(2-hydroxystyryl)pyrimidine-2,4(1H,3H)-dione
0.026
(E)-5-nitro-6-(3-(pyridin-3-yl)vinyl)pyrimidine-2,4(1H,3H)-dione
-
pH 7.0, 27°C
0.011 - 0.042
(E)-5-nitro-6-(3-nitrostyryl)pyrimidine-2,4(1H,3H)-dione
0.026
(E)-5-nitro-6-(4-bromostyryl)pyrimidine-2,4(1H,3H)-dione
-
pH 7.0, 27°C
0.0037 - 0.013
(E)-5-nitro-6-(4-nitrostyryl)pyrimidine-2,4(1H,3H)-dione
0.013 - 0.03
(E)-5-nitro-6-[2-(1H-pyrrol-2-yl)vinyl]pyrimidine-2,4(1H,3H)-dione
0.048
(E)-6-(2,3,4-trimethoxystyryl)-5-nitropyrimidine-2,4(1H,3H)-dione
-
pH 7.0, 27°C
0.0049 - 0.012
(E)-6-(2,3-dihydroxystyryl)-5-nitropyrimidine-2,4(1H,3H)-dione
0.0096 - 0.243
(E)-6-(2,3-dimethoxystyryl)-5-nitropyrimidine-2,4(1H,3H)-dione
0.07 - 0.141
(E)-6-(2-(3H-indol-3-yl)vinyl)-5-nitropyrimidine-2,4(1H,3H)-dione
0.011 - 0.094
(E)-6-(2-(naphthalen-2-yl)vinyl)-5-nitropyrimidine-2,4(1H,3H)-dione
0.024 - 0.151
(E)-6-(2-fluoro-3-methoxystyryl)-5-nitropyrimidine-2,4(1H,3H)-dione
0.0078
(E)-6-(2-fluorostyryl)-5-nitropyrimidine-2,4(1H,3H)-dione
-
pH 7.0, 27°C
0.042
(E)-6-(2-hydroxy-3-nitrostyryl)-3-nitropyrimidine-2,4(1H,3H)-dione
-
pH 7.0, 27°C
0.031
(E)-6-(2-hydroxy-5-nitrostyryl)-5-nitropyrimidine-2,4(1H,3H)-dione
-
pH 7.0, 27°C
0.023 - 0.085
(E)-6-(2-methoxy-5-nitrostyryl)-5-nitropyrimidine-2,4(1H,3H)-dione
0.028 - 0.205
(E)-6-(2-methoxystyryl)-5-nitropyrimidine-2,4(1H,3H)-dione
0.016
(E)-6-(2-nitrostyryl)-5-nitropyrimidine-2,4(1H,3H)-dione
-
pH 7.0, 27°C
0.017
(E)-6-(3,4,5-trimethoxystyryl)-5-nitropyrimidine-2,4(1H,3H)-dione
-
pH 7.0, 27°C
0.032
(E)-6-(3,4-dimethoxystyryl)-5-nitropyrimidine-2,4(1H,3H)-dione
-
pH 7.0, 27°C
0.052
(E)-6-(3-hydroxy-4-methoxystyryl)-5-nitropyrimidine-2,4(1H,3H)-dione
-
pH 7.0, 27°C
0.012 - 0.094
(E)-6-(3-hydroxy-4-nitrostyryl)-5-nitropyrimidine-2,4(1H,3H)-dione
0.0071
(E)-6-(3-hydroxystyryl)-5-nitropyrimidine-2,4(1H,3H)-dione
-
pH 7.0, 27°C
0.045
(E)-6-(4-chlorostyryl)-5-nitropyrimidine-2,4(1H,3H)-dione
-
pH 7.0, 27°C
0.086
(E)-6-(4-fluorostyryl)-5-nitropyrimidine-2,4(1H,3H)-dione
-
pH 7.0, 27°C
0.087
(E)-6-(4-hydroxy-3-nitrostyryl)-5-nitropyrimidine-2,4(1H,3H)-dione
-
pH 7.0, 27°C
0.012
(E)-6-(4-hydroxystyryl)-5-nitropyrimidine-2,4(1H,3H)-dione
-
pH 7.0, 27°C
0.35
1,3,6,8-tetrahydroxynaphthyridine
-
pH 7.0, 37°C
0.0014 - 0.0078
1-deoxy-1-(2,4,6,7-tetraoxo-1,3,4,5,6,7-hexahydropteridin-8(2H)-yl)-D-ribitol
0.0091 - 0.046
1-deoxy-1-(2,6,8-trioxo-1,2,3,6,7,8-hexahydro-9H-purin-9-yl)-D-ribitol
0.83
1-deoxy-1-[(2,6-dioxo-5-[[5-(phosphonooxy)pentanoyl]amino]-1,2,3,6-tetrahydropyrimidin-4-yl)amino]-D-ribitol
-
pH 7.0, 37°C, variable concentration of L-3,4-dihydroxybutan-2-one 4-phosphate
0.000036
1-deoxy-1-[2,4,6,7-tetraoxo-5-[4-(phosphonooxy)butyl]-1,3,4,5,6,7-hexahydropteridin-8(2H)-yl]-D-ribitol
-
pH 7.0, 37°C
0.000012
1-deoxy-1-[2,4,6,7-tetraoxo-5-[5-(phosphonooxy)pentyl]-1,3,4,5,6,7-hexahydropteridin-8(2H)-yl]-D-ribitol
-
pH 7.0, 37°C
0.0000041 - 0.17
1-deoxy-1-[2,6,8-trioxo-7-[4-(phosphonooxy)butyl]-1,2,3,6,7,8-hexahydro-9H-purin-9-yl]-D-ribitol
0.0000047 - 0.852
1-deoxy-1-[2,6,8-trioxo-7-[5-(phosphonooxy)pentyl]-1,2,3,6,7,8-hexahydro-9H-purin-9-yl]-D-ribitol
0.0783 - 0.175
1-deoxy-1-[2,6,8-trioxo-7-[6-(phosphonooxy)hexyl]-1,2,3,6,7,8-hexahydro-9H-purin-9-yl]-D-ribitol
0.44
1-deoxy-1-[[2,6-dioxo-5-(4-phosphonobutyl)-1,2,3,6-tetrahydropyrimidin-4-yl]amino]-D-ribitol
-
pH 7.0, 37°C, variable concentration of L-3,4-dihydroxybutan-2-one 4-phosphate
0.18
1-deoxy-1-[[2,6-dioxo-5-(5-phosphonopentyl)-1,2,3,6-tetrahydropyrimidin-4-yl]amino]-D-ribitol
-
pH 7.0, 37°C, variable concentration of L-3,4-dihydroxybutan-2-one 4-phosphate
0.13
1-deoxy-1-[[2,6-dioxo-5-(6-phosphonohexyl)-1,2,3,6-tetrahydropyrimidin-4-yl]amino]-D-ribitol
-
pH 7.0, 37°C, variable concentration of L-3,4-dihydroxybutan-2-one 4-phosphate
0.18 - 0.492
1-[(5-amino-2,6-dioxo-1,2,3,6-tetrahydropyrimidin-4-yl)(methyl)amino]-1-deoxy-D-ribitol hydrochloride
0.00016 - 0.031
2,4-dioxo-6-[[(2R,3R,4R)-2,3,4,5-tetrahydroxypentyl]sulfanyl]-1,2,3,4-tetrahydropyrimidin-5-aminium chloride
0.022 - 0.066
2,5,8,11-tetraaza-5,11-dihydro-4,10-dihydroxyperylene-1,3,6,7,9,12-hexaone
0.07
2-(2-oxo-1,2-dihydrobenzo[cd]indole-6-sulfonamido)acetic acid
-
pH 7.0, 27°C
0.0026
3-(1,3,7,9-tetrahydro-9-D-ribityl-2,6,8-trioxopurin-7-yl)-1-propanol
-
pH 7.0, 37°C, variable concentration of 5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
0.0045 - 0.0414
3-(1,3,7,9-tetrahydro-9-D-ribityl-2,6,8-trioxopurin-7-yl)propane 1-phosphate
0.000002 - 0.000015
3-(1,3,7-trihydro-9-D-ribityl-2,6,8-purinetrione-7-yl)butane 1-phosphate
0.0000008 - 0.00003
3-(1,3,7-trihydro-9-D-ribityl-2,6,8-purinetrione-7-yl)pentane 1-phosphate
0.0000037 - 0.000101
3-[4,6-dioxo-4,5,6,7-tetrahydro-1-D-ribityl-1H-pyrazolo[3,4-d]pyrimidin-3-yl]propyl 1-phosphate
0.0041 - 0.168
4-(1,3,7,9-tetrahydro-9-D-ribityl-2,6,8-trioxopurin-7-yl)butane 1-phosphate
0.000036 - 0.15
4-(1,5,6,7-tetrahydro-6,7-dioxo-8-D-ribityllumazin-5-yl)butane 1-phosphate
0.038
4-(2-oxo-1,2-dihydrobenzo[cd]indole-6-sulfonamido)butyl dihydrogen phosphate
-
pH 7.0, 27°C
0.000023
4-(6-chloro-2,4-dioxo-1,2,3,4-tetrahydropyrimidine-5-yl)-n-butyl 1-phosphate
-
pH 7.0, temperature not specified in the publication
0.084
4-[2,4,7-trioxo-8-[(2S,3S,4R)-2,3,4,5-tetrahydroxypentyl]-1,2,3,4,7,8-hexahydropteridin-6-yl]butanoic acid
-
pH 7.5, 37°C, recombinant beta60 capsid
0.16
4-[2,4,7-trioxo-8-[(2S,3S,4R)-2,3,4,5-tetrahydroxypentyl]-1,2,3,4,7,8-hexahydropteridin-6-yl]butyl dihydrogen phosphate
-
pH 7.5, 37°C, recombinant beta60 capsid
0.12
4-[2,4,7-trioxo-8-[(2S,3S,4R)-2,3,4,5-tetrahydroxypentyl]-1,2,3,4,7,8-hexahydropteridin-6-yl]propyl dihydrogen phosphate
-
pH 7.5, 37°C, recombinant beta60 capsid
0.0000013 - 0.0000041
4-[4,6-dioxo-4,5,6,7-tetrahydro1-D-ribityl-1H-pyrazolo[3,4-d]-pyrimidin-3-yl]butyl 1-phosphate
0.06 - 0.132
5-(1,3,7,9-tetrahydro-9-D-ribityl-2,6,8-trioxopurin-7-yl)-1,1-difluoropentane 1-phosphonate
0.000012 - 0.027
5-(1,5,6,7-tetrahydro-6,7-dioxo-8-D-ribityllumazin-5-yl)pentane 1-phosphate
0.86
5-(4-phosphonobutyryl)amino-6-D-ribitylaminouracil
-
pH 7.5, 37°C, recombinant beta60 capsid
1
5-(5-phosphonopentyl)amino-6-D-ribitylaminouracil
-
pH 7.5, 37°C, recombinant beta60 capsid
0.83
5-(5-phosphonoxyvaleryl)amino-6-D-ribitylaminouracil
-
pH 7.5, 37°C, recombinant beta60 capsid
0.00014
5-(6-chloro-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-5-oxopentyl phosphate
-
pH 7.0, temperature not specified in the publication
0.00043
5-(6-chloro-2,4-dioxo-1,2,3,4-tetrahydropyrimidine-5-yl)-n-pentyl 1-phosphonate
-
pH 7.0, temperature not specified in the publication
0.13
5-(hexyl 6-dihydrogen phosphate)-6-([(2S,3S,4R)-2,3,4,5-tetrahydroxypentyl]amino)pyrimidine-2,4(1H,3H)-dione
-
pH 7.5, 37°C, recombinant beta60 capsid
0.18
5-(pentyl 6-dihydrogen phosphate)-6-([(2S,3S,4R)-2,3,4,5-tetrahydroxypentyl]amino)pyrimidine-2,4(1H,3H)-dione
-
pH 7.5, 37°C, recombinant beta60 capsid
0.015 - 0.143
5-nitro-6-styryluracil
0.264
5-nitro-6-[(D-ribityl)methyl]pyrimidine-2,4-dione
-
pH 7.0, 37°C, variable concentration of 5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
0.002 - 0.026
5-nitro-6-[[(2R,3R,4R)-2,3,4,5 tetrahydroxypentyl]sulfanyl]pyrimidine-2,4(1H,3H)-dione
0.0000047 - 0.0000077
5-[4,6-dioxo-4,5,6,7-tetrahydro-1-D-ribityl-1H-pyrazolo[3,4-d]pyrimidin-3-yl]pentyl 1-phosphate
0.094
6-methyl-7-methylidene-8-[(2S,3S,4R)-2,3,4,5-tetrahydroxypentyl]-7,8-dihydropyrido[2,3-d]pyrimidine-2,4(1H,3H)-dione
-
pH 7.5, 37°C, recombinant beta60 capsid
0.0014 - 0.0078
8-[[(2S,3S,4R)-2,3,4,5-tetrahydroxypentyl]amino]tetrahydropteridine-2,4,6,7(1H,3H)-tetrone
0.046
9-[(2S,3S,4R)-2,3,4,5-tetrahydroxypentyl]-7,9-dihydro-1H-purine-2,6,8(3H)-trione
-
pH 7.5, 37°C, recombinant beta60 capsid
0.0011 - 0.607
ethyl [(2,4-dioxo-6-[[(2S,3S,4R)-2,3,4,5-tetrahydroxypentyl]amino]-1,2,3,4-tetrahydropyrimidin-5-yl)amino](oxo)acetate
0.017
riboflavin
pH 7.0, 37°C, wild-type enzyme
0.074
(1S)-1,2-dideoxy-1-fluoro-1-(5-nitro-2,6-dioxo-1,2,3,6-tetrahydropyrimidin-4-yl)-D-ribo-hexitol
-
pH 7.0, 37°C, variable concentration of 5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
0.221
(1S)-1,2-dideoxy-1-fluoro-1-(5-nitro-2,6-dioxo-1,2,3,6-tetrahydropyrimidin-4-yl)-D-ribo-hexitol
-
pH 7.0, 37°C, variable concentration of 5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
0.13
(E)-3-hydroxy-4-(2-(5-nitro-2,6-dioxo-1,2,3,6-tetrahydropyrimidine-4-yl)vinyl)benzoic acid
-
pH 7.0, 27°C
0.197
(E)-3-hydroxy-4-(2-(5-nitro-2,6-dioxo-1,2,3,6-tetrahydropyrimidine-4-yl)vinyl)benzoic acid
-
pH 7.0, 27°C
0.095
(E)-5-nitro-6-(2-hydroxystyryl)pyrimidine-2,4(1H,3H)-dione
-
pH 7.0, 27°C
0.21
(E)-5-nitro-6-(2-hydroxystyryl)pyrimidine-2,4(1H,3H)-dione
-
pH 7.0, 27°C
0.011
(E)-5-nitro-6-(3-nitrostyryl)pyrimidine-2,4(1H,3H)-dione
-
pH 7.0, 27°C
0.042
(E)-5-nitro-6-(3-nitrostyryl)pyrimidine-2,4(1H,3H)-dione
-
pH 7.0, 27°C
0.0037
(E)-5-nitro-6-(4-nitrostyryl)pyrimidine-2,4(1H,3H)-dione
-
pH 7.0, 27°C
0.013
(E)-5-nitro-6-(4-nitrostyryl)pyrimidine-2,4(1H,3H)-dione
-
pH 7.0, 27°C
0.013
(E)-5-nitro-6-[2-(1H-pyrrol-2-yl)vinyl]pyrimidine-2,4(1H,3H)-dione
-
pH 7.0, 27°C
0.03
(E)-5-nitro-6-[2-(1H-pyrrol-2-yl)vinyl]pyrimidine-2,4(1H,3H)-dione
-
pH 7.0, 27°C
0.0049
(E)-6-(2,3-dihydroxystyryl)-5-nitropyrimidine-2,4(1H,3H)-dione
-
pH 7.0, 27°C
0.012
(E)-6-(2,3-dihydroxystyryl)-5-nitropyrimidine-2,4(1H,3H)-dione
-
pH 7.0, 27°C
0.0096
(E)-6-(2,3-dimethoxystyryl)-5-nitropyrimidine-2,4(1H,3H)-dione
-
pH 7.0, 27°C
0.243
(E)-6-(2,3-dimethoxystyryl)-5-nitropyrimidine-2,4(1H,3H)-dione
-
pH 7.0, 27°C
0.07
(E)-6-(2-(3H-indol-3-yl)vinyl)-5-nitropyrimidine-2,4(1H,3H)-dione
-
pH 7.0, 27°C
0.141
(E)-6-(2-(3H-indol-3-yl)vinyl)-5-nitropyrimidine-2,4(1H,3H)-dione
-
pH 7.0, 27°C
0.011
(E)-6-(2-(naphthalen-2-yl)vinyl)-5-nitropyrimidine-2,4(1H,3H)-dione
-
pH 7.0, 27°C
0.094
(E)-6-(2-(naphthalen-2-yl)vinyl)-5-nitropyrimidine-2,4(1H,3H)-dione
-
pH 7.0, 27°C
0.024
(E)-6-(2-fluoro-3-methoxystyryl)-5-nitropyrimidine-2,4(1H,3H)-dione
-
pH 7.0, 27°C
0.151
(E)-6-(2-fluoro-3-methoxystyryl)-5-nitropyrimidine-2,4(1H,3H)-dione
-
pH 7.0, 27°C
0.023
(E)-6-(2-methoxy-5-nitrostyryl)-5-nitropyrimidine-2,4(1H,3H)-dione
-
pH 7.0, 27°C
0.085
(E)-6-(2-methoxy-5-nitrostyryl)-5-nitropyrimidine-2,4(1H,3H)-dione
-
pH 7.0, 27°C
0.028
(E)-6-(2-methoxystyryl)-5-nitropyrimidine-2,4(1H,3H)-dione
-
pH 7.0, 27°C
0.205
(E)-6-(2-methoxystyryl)-5-nitropyrimidine-2,4(1H,3H)-dione
-
pH 7.0, 27°C
0.012
(E)-6-(3-hydroxy-4-nitrostyryl)-5-nitropyrimidine-2,4(1H,3H)-dione
-
pH 7.0, 27°C
0.094
(E)-6-(3-hydroxy-4-nitrostyryl)-5-nitropyrimidine-2,4(1H,3H)-dione
-
pH 7.0, 27°C
0.0014
1-deoxy-1-(2,4,6,7-tetraoxo-1,3,4,5,6,7-hexahydropteridin-8(2H)-yl)-D-ribitol
-
pH 7.0, 37°C
0.0078
1-deoxy-1-(2,4,6,7-tetraoxo-1,3,4,5,6,7-hexahydropteridin-8(2H)-yl)-D-ribitol
-
pH 7.0, 37°C
0.0091
1-deoxy-1-(2,6,8-trioxo-1,2,3,6,7,8-hexahydro-9H-purin-9-yl)-D-ribitol
-
pH 7.0, 37°C, variable concentration of 5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
0.046
1-deoxy-1-(2,6,8-trioxo-1,2,3,6,7,8-hexahydro-9H-purin-9-yl)-D-ribitol
-
pH 7.0, 37°C, variable concentration of L-3,4-dihydroxybutan-2-one 4-phosphate
0.0000041
1-deoxy-1-[2,6,8-trioxo-7-[4-(phosphonooxy)butyl]-1,2,3,6,7,8-hexahydro-9H-purin-9-yl]-D-ribitol
-
pH 7.0, 37°C
0.17
1-deoxy-1-[2,6,8-trioxo-7-[4-(phosphonooxy)butyl]-1,2,3,6,7,8-hexahydro-9H-purin-9-yl]-D-ribitol
-
pH 7.0, 37°C
0.0000047
1-deoxy-1-[2,6,8-trioxo-7-[5-(phosphonooxy)pentyl]-1,2,3,6,7,8-hexahydro-9H-purin-9-yl]-D-ribitol
-
pH 7.0, 37°C
0.0047
1-deoxy-1-[2,6,8-trioxo-7-[5-(phosphonooxy)pentyl]-1,2,3,6,7,8-hexahydro-9H-purin-9-yl]-D-ribitol
-
pH 7.0, 37°C, variable concentration of 5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
0.27
1-deoxy-1-[2,6,8-trioxo-7-[5-(phosphonooxy)pentyl]-1,2,3,6,7,8-hexahydro-9H-purin-9-yl]-D-ribitol
-
pH 7.0, 37°C
0.271
1-deoxy-1-[2,6,8-trioxo-7-[5-(phosphonooxy)pentyl]-1,2,3,6,7,8-hexahydro-9H-purin-9-yl]-D-ribitol
-
pH 7.0, 37°C, variable concentration of 5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
0.852
1-deoxy-1-[2,6,8-trioxo-7-[5-(phosphonooxy)pentyl]-1,2,3,6,7,8-hexahydro-9H-purin-9-yl]-D-ribitol
-
pH 7.0, 37°C, variable concentration of L-3,4-dihydroxybutan-2-one 4-phosphate
0.0783
1-deoxy-1-[2,6,8-trioxo-7-[6-(phosphonooxy)hexyl]-1,2,3,6,7,8-hexahydro-9H-purin-9-yl]-D-ribitol
-
pH 7.0, 37°C, variable concentration of 5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
0.17
1-deoxy-1-[2,6,8-trioxo-7-[6-(phosphonooxy)hexyl]-1,2,3,6,7,8-hexahydro-9H-purin-9-yl]-D-ribitol
-
pH 7.0, 37°C, variable concentration of 5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
0.175
1-deoxy-1-[2,6,8-trioxo-7-[6-(phosphonooxy)hexyl]-1,2,3,6,7,8-hexahydro-9H-purin-9-yl]-D-ribitol
-
pH 7.0, 37°C, variable concentration of L-3,4-dihydroxybutan-2-one 4-phosphate
0.18
1-[(5-amino-2,6-dioxo-1,2,3,6-tetrahydropyrimidin-4-yl)(methyl)amino]-1-deoxy-D-ribitol hydrochloride
-
pH 7.0, 37°C, variable concentration of 5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
0.341
1-[(5-amino-2,6-dioxo-1,2,3,6-tetrahydropyrimidin-4-yl)(methyl)amino]-1-deoxy-D-ribitol hydrochloride
-
pH 7.0, 37°C, variable concentration of 5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
0.492
1-[(5-amino-2,6-dioxo-1,2,3,6-tetrahydropyrimidin-4-yl)(methyl)amino]-1-deoxy-D-ribitol hydrochloride
-
pH 7.0, 37°C, variable concentration of L-3,4-dihydroxybutan-2-one 4-phosphate
0.00016
2,4-dioxo-6-[[(2R,3R,4R)-2,3,4,5-tetrahydroxypentyl]sulfanyl]-1,2,3,4-tetrahydropyrimidin-5-aminium chloride
-
pH 7.0, 27°C
0.0026
2,4-dioxo-6-[[(2R,3R,4R)-2,3,4,5-tetrahydroxypentyl]sulfanyl]-1,2,3,4-tetrahydropyrimidin-5-aminium chloride
-
pH 7.0, 27°C
0.031
2,4-dioxo-6-[[(2R,3R,4R)-2,3,4,5-tetrahydroxypentyl]sulfanyl]-1,2,3,4-tetrahydropyrimidin-5-aminium chloride
-
pH 7.0, 27°C
0.022
2,5,8,11-tetraaza-5,11-dihydro-4,10-dihydroxyperylene-1,3,6,7,9,12-hexaone
-
pH 7.0, 37°C, phosphate buffer
0.066
2,5,8,11-tetraaza-5,11-dihydro-4,10-dihydroxyperylene-1,3,6,7,9,12-hexaone
-
pH 7.0, 37°C, Tris buffer
0.0045
3-(1,3,7,9-tetrahydro-9-D-ribityl-2,6,8-trioxopurin-7-yl)propane 1-phosphate
-
pH 7.0, 37°C, variable concentration of 5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
0.0414
3-(1,3,7,9-tetrahydro-9-D-ribityl-2,6,8-trioxopurin-7-yl)propane 1-phosphate
-
pH 7.0, 37°C, variable concentration of 5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
0.000002
3-(1,3,7-trihydro-9-D-ribityl-2,6,8-purinetrione-7-yl)butane 1-phosphate
-
pH 7.0, 27°C
0.000014
3-(1,3,7-trihydro-9-D-ribityl-2,6,8-purinetrione-7-yl)butane 1-phosphate
-
pH 7.0, 27°C
0.000015
3-(1,3,7-trihydro-9-D-ribityl-2,6,8-purinetrione-7-yl)butane 1-phosphate
-
pH 7.0, 27°C
0.0000008
3-(1,3,7-trihydro-9-D-ribityl-2,6,8-purinetrione-7-yl)pentane 1-phosphate
-
pH 7.0, 27°C
0.0000009
3-(1,3,7-trihydro-9-D-ribityl-2,6,8-purinetrione-7-yl)pentane 1-phosphate
-
pH 7.0, 27°C
0.00003
3-(1,3,7-trihydro-9-D-ribityl-2,6,8-purinetrione-7-yl)pentane 1-phosphate
-
pH 7.0, 27°C
0.0000037
3-[4,6-dioxo-4,5,6,7-tetrahydro-1-D-ribityl-1H-pyrazolo[3,4-d]pyrimidin-3-yl]propyl 1-phosphate
-
pH 7.0, 27°C
0.00004
3-[4,6-dioxo-4,5,6,7-tetrahydro-1-D-ribityl-1H-pyrazolo[3,4-d]pyrimidin-3-yl]propyl 1-phosphate
-
pH 7.0, 27°C
0.000101
3-[4,6-dioxo-4,5,6,7-tetrahydro-1-D-ribityl-1H-pyrazolo[3,4-d]pyrimidin-3-yl]propyl 1-phosphate
-
pH 7.0, 27°C
0.0041
4-(1,3,7,9-tetrahydro-9-D-ribityl-2,6,8-trioxopurin-7-yl)butane 1-phosphate
-
pH 7.0, 37°C, variable concentration of 5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
0.168
4-(1,3,7,9-tetrahydro-9-D-ribityl-2,6,8-trioxopurin-7-yl)butane 1-phosphate
-
pH 7.0, 37°C, variable concentration of 5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
0.000036
4-(1,5,6,7-tetrahydro-6,7-dioxo-8-D-ribityllumazin-5-yl)butane 1-phosphate
-
pH 7.0, 37°C
0.15
4-(1,5,6,7-tetrahydro-6,7-dioxo-8-D-ribityllumazin-5-yl)butane 1-phosphate
-
pH 7.0, 37°C
0.0000013
4-[4,6-dioxo-4,5,6,7-tetrahydro1-D-ribityl-1H-pyrazolo[3,4-d]-pyrimidin-3-yl]butyl 1-phosphate
-
pH 7.0, 27°C
0.0000041
4-[4,6-dioxo-4,5,6,7-tetrahydro1-D-ribityl-1H-pyrazolo[3,4-d]-pyrimidin-3-yl]butyl 1-phosphate
-
pH 7.0, 27°C
0.06
5-(1,3,7,9-tetrahydro-9-D-ribityl-2,6,8-trioxopurin-7-yl)-1,1-difluoropentane 1-phosphonate
-
pH 7.0, 37°C, variable concentration of 5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
0.132
5-(1,3,7,9-tetrahydro-9-D-ribityl-2,6,8-trioxopurin-7-yl)-1,1-difluoropentane 1-phosphonate
-
pH 7.0, 37°C, variable concentration of 5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
0.000012
5-(1,5,6,7-tetrahydro-6,7-dioxo-8-D-ribityllumazin-5-yl)pentane 1-phosphate
-
pH 7.0, 37°C
0.027
5-(1,5,6,7-tetrahydro-6,7-dioxo-8-D-ribityllumazin-5-yl)pentane 1-phosphate
-
pH 7.0, 37°C
0.015
5-nitro-6-styryluracil
-
pH 7.0, 27°C
0.143
5-nitro-6-styryluracil
-
pH 7.0, 27°C
0.002
5-nitro-6-[[(2R,3R,4R)-2,3,4,5 tetrahydroxypentyl]sulfanyl]pyrimidine-2,4(1H,3H)-dione
-
pH 7.0, 27°C
0.011
5-nitro-6-[[(2R,3R,4R)-2,3,4,5 tetrahydroxypentyl]sulfanyl]pyrimidine-2,4(1H,3H)-dione
-
pH 7.0, 27°C
0.026
5-nitro-6-[[(2R,3R,4R)-2,3,4,5 tetrahydroxypentyl]sulfanyl]pyrimidine-2,4(1H,3H)-dione
-
pH 7.0, 27°C
0.0000047
5-[4,6-dioxo-4,5,6,7-tetrahydro-1-D-ribityl-1H-pyrazolo[3,4-d]pyrimidin-3-yl]pentyl 1-phosphate
-
pH 7.0, 27°C
0.0000077
5-[4,6-dioxo-4,5,6,7-tetrahydro-1-D-ribityl-1H-pyrazolo[3,4-d]pyrimidin-3-yl]pentyl 1-phosphate
-
pH 7.0, 27°C
0.0014
8-[[(2S,3S,4R)-2,3,4,5-tetrahydroxypentyl]amino]tetrahydropteridine-2,4,6,7(1H,3H)-tetrone
-
pH 7.0, 27°C
0.0078
8-[[(2S,3S,4R)-2,3,4,5-tetrahydroxypentyl]amino]tetrahydropteridine-2,4,6,7(1H,3H)-tetrone
-
pH 7.0, 27°C
0.0011
ethyl [(2,4-dioxo-6-[[(2S,3S,4R)-2,3,4,5-tetrahydroxypentyl]amino]-1,2,3,4-tetrahydropyrimidin-5-yl)amino](oxo)acetate
pH 7.0, 27°C
0.004
ethyl [(2,4-dioxo-6-[[(2S,3S,4R)-2,3,4,5-tetrahydroxypentyl]amino]-1,2,3,4-tetrahydropyrimidin-5-yl)amino](oxo)acetate
-
pH 7.0, 27°C
0.607
ethyl [(2,4-dioxo-6-[[(2S,3S,4R)-2,3,4,5-tetrahydroxypentyl]amino]-1,2,3,4-tetrahydropyrimidin-5-yl)amino](oxo)acetate
-
pH 7.0, 27°C
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60-mer
sequence determinants responsible for the icosahedral quaternary structure
60-mer
-
the spherical protein consists of 60 identical subunits with strict icosahedral 532 symmetry
60-mer
sequence determinants responsible for the icosahedral quaternary structure
60-mer
-
60 * 16156, calculated from sequence
60-mer
60 * 15645, the enzyme can form capsids with icosahedral 532 symmetry consisting of 60 subunits, electrospray mass spectrometry
60-mer
60 * 16000, the enzyme can form capsids with icosahedral 532 symmetry consisting of 60 subunits, SDS-PAGE
60-mer
-
60 * 15500, subunit of mature enzyme, SDS-PAGE
60-mer
-
60 * 16534, subunit of mature enzyme, calculated from sequence
60-mer
-
60 * 16536, subunit of mature enzyme, electrospray ionization mass spectrometry
60-mer
-
sequence determinants responsible for the icosahedral quaternary structure
?
x * 35000, SDS-PAGE
?
x * 25070, LcLS1, sequence calculation
?
x * 25410, LcLS2, sequence calculation
?
-
x * 19000, calculated from sequence
?
x * 16008, calculated, x * 17000-18000, SDS-PAGE, x * 18100, MALDI-TOF
decamer
the d5-symmetric protein is a dimer of pentamers
decamer
-
10 * 18000, it is demonstrated by means of solution light scattering and X-ray structural analyses that the enzyme assembles as a very stable dimer of pentamers. A mechanism for dissociation/unfolding of this macromolecular assembly is postulated
decamer
-
a head-to-head oriented dimer of pentamers. pH plays a critical role in the structure of the interface between pentamers in Brucella spp. RibH2
decamer
10 * 17300, calculated, isoform RibH2
decamer
10 * 19548, His-tagged enzyme, (alpha5)2, a dimer of homopentamers with one in five subunits containing a product molecule from the catalytic reaction
pentamer
the lumazine protein folds into two closely similar domains, the enzyme forms a dodecamer of pentamers, electrostatic model calculations
pentamer
the lumazine protein folds into two closely similar domains
pentamer
-
5 * 16800, calculated, isoform RibH1
pentamer
-
5 * 16800, calculated, isoform RibH1
pentamer
-
5 * 17599, calculated from sequence
pentamer
5 * 17200, calculated, isoform RibH1
pentamer
-
5 * 18598, calculated from sequence
pentamer
5 * 18600, calculated from sequence
pentamer
the lumazine protein folds into two closely similar domains, the enzyme forms a dodecamer of pentamers, electrostatic model calculations
pentamer
5 * 17188, calculated from sequence
pentamer
5 * 17189, electrospray MS
additional information
lumazine synthase is found in different species in two different quaternary structures, pentameric and icosahedral, built from practically the same structural monomeric unit. The icosahedral structure is best described as a capsid of twelve pentamers. Despite this noticeable difference, the active sites are virtually identical in all structurally studied members. The main regions involved in the catalysis are located at the interface between adjacent subunits in the pentamer. Combined analysis that includes sequence-structure and evolutionary studies to find the sequence determinants of the different quaternary assemblies of this enzyme. The positions involved in icosahedral contacts suffer a larger increase in constraints than the rest. Eight sequence sites that would be the most important icosahedral sequence determinants are identified
additional information
lumazine synthase is found in different species in two different quaternary structures, pentameric and icosahedral, built from practically the same structural monomeric unit. The icosahedral structure is best described as a capsid of twelve pentamers. Despite this noticeable difference, the active sites are virtually identical in all structurally studied members. The main regions involved in the catalysis are located at the interface between adjacent subunits in the pentamer. Combined analysis that includes sequence-structure and evolutionary studies to find the sequence determinants of the different quaternary assemblies of this enzyme. The positions involved in icosahedral contacts suffer a larger increase in constraints than the rest. Eight sequence sites that would be the most important icosahedral sequence determinants are identified
additional information
-
lumazine synthase is found in different species in two different quaternary structures, pentameric and icosahedral, built from practically the same structural monomeric unit. The icosahedral structure is best described as a capsid of twelve pentamers. Despite this noticeable difference, the active sites are virtually identical in all structurally studied members. The main regions involved in the catalysis are located at the interface between adjacent subunits in the pentamer. Combined analysis that includes sequence-structure and evolutionary studies to find the sequence determinants of the different quaternary assemblies of this enzyme. The positions involved in icosahedral contacts suffer a larger increase in constraints than the rest. Eight sequence sites that would be the most important icosahedral sequence determinants are identified
-
additional information
lumazine synthase is found in different species in two different quaternary structures, pentameric and icosahedral, built from practically the same structural monomeric unit. The icosahedral structure is best described as a capsid of twelve pentamers. Despite this noticeable difference, the active sites are virtually identical in all structurally studied members. The main regions involved in the catalysis are located at the interface between adjacent subunits in the pentamer. Combined analysis that includes sequence-structure and evolutionary studies to find the sequence determinants of the different quaternary assemblies of this enzyme. The positions involved in icosahedral contacts suffer a larger increase in constraints than the rest. Eight sequence sites that would be the most important icosahedral sequence determinants are identified
additional information
lumazine synthase is found in different species in two different quaternary structures, pentameric and icosahedral, built from practically the same structural monomeric unit. The icosahedral structure is best described as a capsid of twelve pentamers. Despite this noticeable difference, the active sites are virtually identical in all structurally studied members. The main regions involved in the catalysis are located at the interface between adjacent subunits in the pentamer. Combined analysis that includes sequence-structure and evolutionary studies to find the sequence determinants of the different quaternary assemblies of this enzyme. The positions involved in icosahedral contacts suffer a larger increase in constraints than the rest. Eight sequence sites that would be the most important icosahedral sequence determinants are identified
additional information
-
enzyme AaLS consists of 60 identical subunits that form an icosahedral capsid architecture with 15.4 nm exterior and 9 nm interior diameters
additional information
structure analysis and comparisons, overview
additional information
lumazine synthase is found in different species in two different quaternary structures, pentameric and icosahedral, built from practically the same structural monomeric unit. The icosahedral structure is best described as a capsid of twelve pentamers. Despite this noticeable difference, the active sites are virtually identical in all structurally studied members. The main regions involved in the catalysis are located at the interface between adjacent subunits in the pentamer. Combined analysis that includes sequence-structure and evolutionary studies to find the sequence determinants of the different quaternary assemblies of this enzyme. The positions involved in icosahedral contacts suffer a larger increase in constraints than the rest. Eight sequence sites that would be the most important icosahedral sequence determinants are identified
additional information
lumazine synthase is found in different species in two different quaternary structures, pentameric and icosahedral, built from practically the same structural monomeric unit. The icosahedral structure is best described as a capsid of twelve pentamers. Despite this noticeable difference, the active sites are virtually identical in all structurally studied members. The main regions involved in the catalysis are located at the interface between adjacent subunits in the pentamer. Combined analysis that includes sequence-structure and evolutionary studies to find the sequence determinants of the different quaternary assemblies of this enzyme. The positions involved in icosahedral contacts suffer a larger increase in constraints than the rest. Eight sequence sites that would be the most important icosahedral sequence determinants are identified
additional information
lumazine synthase is found in different species in two different quaternary structures, pentameric and icosahedral, built from practically the same structural monomeric unit. The icosahedral structure is best described as a capsid of twelve pentamers. Despite this noticeable difference, the active sites are virtually identical in all structurally studied members. The main regions involved in the catalysis are located at the interface between adjacent subunits in the pentamer. Combined analysis that includes sequence-structure and evolutionary studies to find the sequence determinants of the different quaternary assemblies of this enzyme. The positions involved in icosahedral contacts suffer a larger increase in constraints than the rest. Eight sequence sites that would be the most important icosahedral sequence determinants are identified
additional information
lumazine synthase is found in different species in two different quaternary structures, pentameric and icosahedral, built from practically the same structural monomeric unit. The icosahedral structure is best described as a capsid of twelve pentamers. Despite this noticeable difference, the active sites are virtually identical in all structurally studied members. The main regions involved in the catalysis are located at the interface between adjacent subunits in the pentamer. Combined analysis that includes sequence-structure and evolutionary studies to find the sequence determinants of the different quaternary assemblies of this enzyme. The positions involved in icosahedral contacts suffer a larger increase in constraints than the rest. Eight sequence sites that would be the most important icosahedral sequence determinants are identified
additional information
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the bifunctional lumazine synthase/riboflavin synthase (EC 2.5.1.9) complex is composed of 3 alpha (riboflavin synthase) subunits and 60 beta (lumazine synthase) subunits and has a relative mass of 1 MDa. The 60 beta subunits are arranged in an icosahedral capsid enclosing the alpha trimer in the central core. Hollow, icosahedral capsids consisting of 60 beta subunits can be obtained by inhibitor-driven renaturation of isolated beta subunits. They catalyse the formation of 6,7-dimethyl-8-ribityllumazine at the same rate as the native alpha3beta60 complex and can be crystallised in two different hexagonal and one monoclinic form
additional information
structure analysis and comparisons, overview
additional information
lumazine synthase is found in different species in two different quaternary structures, pentameric and icosahedral, built from practically the same structural monomeric unit. The icosahedral structure is best described as a capsid of twelve pentamers. Despite this noticeable difference, the active sites are virtually identical in all structurally studied members. The main regions involved in the catalysis are located at the interface between adjacent subunits in the pentamer. Combined analysis that includes sequence-structure and evolutionary studies to find the sequence determinants of the different quaternary assemblies of this enzyme. The positions involved in icosahedral contacts suffer a larger increase in constraints than the rest. Eight sequence sites that would be the most important icosahedral sequence determinants are identified
additional information
lumazine synthase is found in different species in two different quaternary structures, pentameric and icosahedral, built from practically the same structural monomeric unit. The icosahedral structure is best described as a capsid of twelve pentamers. Despite this noticeable difference, the active sites are virtually identical in all structurally studied members. The main regions involved in the catalysis are located at the interface between adjacent subunits in the pentamer. Combined analysis that includes sequence-structure and evolutionary studies to find the sequence determinants of the different quaternary assemblies of this enzyme. The positions involved in icosahedral contacts suffer a larger increase in constraints than the rest. Eight sequence sites that would be the most important icosahedral sequence determinants are identified
additional information
structure analysis and comparisons, overview
additional information
structure analysis and comparisons, overview
additional information
Brucella spp. lumazine synthase arranges in icosahedric capsids similar to those formed by the lumazine synthases of other bacteria
additional information
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BLS folds as a decamer in the recombinant BLS-Stx2B chimera, i.e. a chimera consisting of the B subunit of Shiga toxin type 2 and Brucella sp. lumazine synthase
additional information
the recombinant enzyme polymerizes and exists in different forms, including as a dimer and pentamer, overview
additional information
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the recombinant enzyme polymerizes and exists in different forms, including as a dimer and pentamer, overview
additional information
lumazine synthase is found in different species in two different quaternary structures, pentameric and icosahedral, built from practically the same structural monomeric unit. The icosahedral structure is best described as a capsid of twelve pentamers. Despite this noticeable difference, the active sites are virtually identical in all structurally studied members. The main regions involved in the catalysis are located at the interface between adjacent subunits in the pentamer. Combined analysis that includes sequence-structure and evolutionary studies to find the sequence determinants of the different quaternary assemblies of this enzyme. The positions involved in icosahedral contacts suffer a larger increase in constraints than the rest. Eight sequence sites that would be the most important icosahedral sequence determinants are identified
additional information
lumazine synthase is found in different species in two different quaternary structures, pentameric and icosahedral, built from practically the same structural monomeric unit. The icosahedral structure is best described as a capsid of twelve pentamers. Despite this noticeable difference, the active sites are virtually identical in all structurally studied members. The main regions involved in the catalysis are located at the interface between adjacent subunits in the pentamer. Combined analysis that includes sequence-structure and evolutionary studies to find the sequence determinants of the different quaternary assemblies of this enzyme. The positions involved in icosahedral contacts suffer a larger increase in constraints than the rest. Eight sequence sites that would be the most important icosahedral sequence determinants are identified
additional information
lumazine synthase is found in different species in two different quaternary structures, pentameric and icosahedral, built from practically the same structural monomeric unit. The icosahedral structure is best described as a capsid of twelve pentamers. Despite this noticeable difference, the active sites are virtually identical in all structurally studied members. The main regions involved in the catalysis are located at the interface between adjacent subunits in the pentamer. Combined analysis that includes sequence-structure and evolutionary studies to find the sequence determinants of the different quaternary assemblies of this enzyme. The positions involved in icosahedral contacts suffer a larger increase in constraints than the rest. Eight sequence sites that would be the most important icosahedral sequence determinants are identified
additional information
lumazine synthase is found in different species in two different quaternary structures, pentameric and icosahedral, built from practically the same structural monomeric unit. The icosahedral structure is best described as a capsid of twelve pentamers. Despite this noticeable difference, the active sites are virtually identical in all structurally studied members. The main regions involved in the catalysis are located at the interface between adjacent subunits in the pentamer. Combined analysis that includes sequence-structure and evolutionary studies to find the sequence determinants of the different quaternary assemblies of this enzyme. The positions involved in icosahedral contacts suffer a larger increase in constraints than the rest. Eight sequence sites that would be the most important icosahedral sequence determinants are identified
additional information
lumazine synthase is found in different species in two different quaternary structures, pentameric and icosahedral, built from practically the same structural monomeric unit. The icosahedral structure is best described as a capsid of twelve pentamers. Despite this noticeable difference, the active sites are virtually identical in all structurally studied members. The main regions involved in the catalysis are located at the interface between adjacent subunits in the pentamer. Combined analysis that includes sequence-structure and evolutionary studies to find the sequence determinants of the different quaternary assemblies of this enzyme. The positions involved in icosahedral contacts suffer a larger increase in constraints than the rest. Eight sequence sites that would be the most important icosahedral sequence determinants are identified
additional information
lumazine synthase is found in different species in two different quaternary structures, pentameric and icosahedral, built from practically the same structural monomeric unit. The icosahedral structure is best described as a capsid of twelve pentamers. Despite this noticeable difference, the active sites are virtually identical in all structurally studied members. The main regions involved in the catalysis are located at the interface between adjacent subunits in the pentamer. Combined analysis that includes sequence-structure and evolutionary studies to find the sequence determinants of the different quaternary assemblies of this enzyme. The positions involved in icosahedral contacts suffer a larger increase in constraints than the rest. Eight sequence sites that would be the most important icosahedral sequence determinants are identified
additional information
lumazine synthase is found in different species in two different quaternary structures, pentameric and icosahedral, built from practically the same structural monomeric unit. The icosahedral structure is best described as a capsid of twelve pentamers. Despite this noticeable difference, the active sites are virtually identical in all structurally studied members. The main regions involved in the catalysis are located at the interface between adjacent subunits in the pentamer. Combined analysis that includes sequence-structure and evolutionary studies to find the sequence determinants of the different quaternary assemblies of this enzyme. The positions involved in icosahedral contacts suffer a larger increase in constraints than the rest. Eight sequence sites that would be the most important icosahedral sequence determinants are identified
additional information
lumazine synthase is found in different species in two different quaternary structures, pentameric and icosahedral, built from practically the same structural monomeric unit. The icosahedral structure is best described as a capsid of twelve pentamers. Despite this noticeable difference, the active sites are virtually identical in all structurally studied members. The main regions involved in the catalysis are located at the interface between adjacent subunits in the pentamer. Combined analysis that includes sequence-structure and evolutionary studies to find the sequence determinants of the different quaternary assemblies of this enzyme. The positions involved in icosahedral contacts suffer a larger increase in constraints than the rest. Eight sequence sites that would be the most important icosahedral sequence determinants are identified
additional information
lumazine synthase is found in different species in two different quaternary structures, pentameric and icosahedral, built from practically the same structural monomeric unit. The icosahedral structure is best described as a capsid of twelve pentamers. Despite this noticeable difference, the active sites are virtually identical in all structurally studied members. The main regions involved in the catalysis are located at the interface between adjacent subunits in the pentamer. Combined analysis that includes sequence-structure and evolutionary studies to find the sequence determinants of the different quaternary assemblies of this enzyme. The positions involved in icosahedral contacts suffer a larger increase in constraints than the rest. Eight sequence sites that would be the most important icosahedral sequence determinants are identified
additional information
lumazine synthase is found in different species in two different quaternary structures, pentameric and icosahedral, built from practically the same structural monomeric unit. The icosahedral structure is best described as a capsid of twelve pentamers. Despite this noticeable difference, the active sites are virtually identical in all structurally studied members. The main regions involved in the catalysis are located at the interface between adjacent subunits in the pentamer. Combined analysis that includes sequence-structure and evolutionary studies to find the sequence determinants of the different quaternary assemblies of this enzyme. The positions involved in icosahedral contacts suffer a larger increase in constraints than the rest. Eight sequence sites that would be the most important icosahedral sequence determinants are identified
additional information
lumazine synthase is found in different species in two different quaternary structures, pentameric and icosahedral, built from practically the same structural monomeric unit. The icosahedral structure is best described as a capsid of twelve pentamers. Despite this noticeable difference, the active sites are virtually identical in all structurally studied members. The main regions involved in the catalysis are located at the interface between adjacent subunits in the pentamer. Combined analysis that includes sequence-structure and evolutionary studies to find the sequence determinants of the different quaternary assemblies of this enzyme. The positions involved in icosahedral contacts suffer a larger increase in constraints than the rest. Eight sequence sites that would be the most important icosahedral sequence determinants are identified
additional information
lumazine synthase is found in different species in two different quaternary structures, pentameric and icosahedral, built from practically the same structural monomeric unit. The icosahedral structure is best described as a capsid of twelve pentamers. Despite this noticeable difference, the active sites are virtually identical in all structurally studied members. The main regions involved in the catalysis are located at the interface between adjacent subunits in the pentamer. Combined analysis that includes sequence-structure and evolutionary studies to find the sequence determinants of the different quaternary assemblies of this enzyme. The positions involved in icosahedral contacts suffer a larger increase in constraints than the rest. Eight sequence sites that would be the most important icosahedral sequence determinants are identified
additional information
lumazine synthase is found in different species in two different quaternary structures, pentameric and icosahedral, built from practically the same structural monomeric unit. The icosahedral structure is best described as a capsid of twelve pentamers. Despite this noticeable difference, the active sites are virtually identical in all structurally studied members. The main regions involved in the catalysis are located at the interface between adjacent subunits in the pentamer. Combined analysis that includes sequence-structure and evolutionary studies to find the sequence determinants of the different quaternary assemblies of this enzyme. The positions involved in icosahedral contacts suffer a larger increase in constraints than the rest. Eight sequence sites that would be the most important icosahedral sequence determinants are identified
additional information
lumazine synthase is found in different species in two different quaternary structures, pentameric and icosahedral, built from practically the same structural monomeric unit. The icosahedral structure is best described as a capsid of twelve pentamers. Despite this noticeable difference, the active sites are virtually identical in all structurally studied members. The main regions involved in the catalysis are located at the interface between adjacent subunits in the pentamer. Combined analysis that includes sequence-structure and evolutionary studies to find the sequence determinants of the different quaternary assemblies of this enzyme. The positions involved in icosahedral contacts suffer a larger increase in constraints than the rest. Eight sequence sites that would be the most important icosahedral sequence determinants are identified
additional information
lumazine synthase is found in different species in two different quaternary structures, pentameric and icosahedral, built from practically the same structural monomeric unit. The icosahedral structure is best described as a capsid of twelve pentamers. Despite this noticeable difference, the active sites are virtually identical in all structurally studied members. The main regions involved in the catalysis are located at the interface between adjacent subunits in the pentamer. Combined analysis that includes sequence-structure and evolutionary studies to find the sequence determinants of the different quaternary assemblies of this enzyme. The positions involved in icosahedral contacts suffer a larger increase in constraints than the rest. Eight sequence sites that would be the most important icosahedral sequence determinants are identified
additional information
Halalkalibacterium halodurans
lumazine synthase is found in different species in two different quaternary structures, pentameric and icosahedral, built from practically the same structural monomeric unit. The icosahedral structure is best described as a capsid of twelve pentamers. Despite this noticeable difference, the active sites are virtually identical in all structurally studied members. The main regions involved in the catalysis are located at the interface between adjacent subunits in the pentamer. Combined analysis that includes sequence-structure and evolutionary studies to find the sequence determinants of the different quaternary assemblies of this enzyme. The positions involved in icosahedral contacts suffer a larger increase in constraints than the rest. Eight sequence sites that would be the most important icosahedral sequence determinants are identified
additional information
lumazine synthase is found in different species in two different quaternary structures, pentameric and icosahedral, built from practically the same structural monomeric unit. The icosahedral structure is best described as a capsid of twelve pentamers. Despite this noticeable difference, the active sites are virtually identical in all structurally studied members. The main regions involved in the catalysis are located at the interface between adjacent subunits in the pentamer. Combined analysis that includes sequence-structure and evolutionary studies to find the sequence determinants of the different quaternary assemblies of this enzyme. The positions involved in icosahedral contacts suffer a larger increase in constraints than the rest. Eight sequence sites that would be the most important icosahedral sequence determinants are identified
additional information
lumazine synthase is found in different species in two different quaternary structures, pentameric and icosahedral, built from practically the same structural monomeric unit. The icosahedral structure is best described as a capsid of twelve pentamers. Despite this noticeable difference, the active sites are virtually identical in all structurally studied members. The main regions involved in the catalysis are located at the interface between adjacent subunits in the pentamer. Combined analysis that includes sequence-structure and evolutionary studies to find the sequence determinants of the different quaternary assemblies of this enzyme. The positions involved in icosahedral contacts suffer a larger increase in constraints than the rest. Eight sequence sites that would be the most important icosahedral sequence determinants are identified
additional information
lumazine synthase is found in different species in two different quaternary structures, pentameric and icosahedral, built from practically the same structural monomeric unit. The icosahedral structure is best described as a capsid of twelve pentamers. Despite this noticeable difference, the active sites are virtually identical in all structurally studied members. The main regions involved in the catalysis are located at the interface between adjacent subunits in the pentamer. Combined analysis that includes sequence-structure and evolutionary studies to find the sequence determinants of the different quaternary assemblies of this enzyme. The positions involved in icosahedral contacts suffer a larger increase in constraints than the rest. Eight sequence sites that would be the most important icosahedral sequence determinants are identified
additional information
lumazine synthase is found in different species in two different quaternary structures, pentameric and icosahedral, built from practically the same structural monomeric unit. The icosahedral structure is best described as a capsid of twelve pentamers. Despite this noticeable difference, the active sites are virtually identical in all structurally studied members. The main regions involved in the catalysis are located at the interface between adjacent subunits in the pentamer. Combined analysis that includes sequence-structure and evolutionary studies to find the sequence determinants of the different quaternary assemblies of this enzyme. The positions involved in icosahedral contacts suffer a larger increase in constraints than the rest. Eight sequence sites that would be the most important icosahedral sequence determinants are identified
additional information
lumazine synthase is found in different species in two different quaternary structures, pentameric and icosahedral, built from practically the same structural monomeric unit. The icosahedral structure is best described as a capsid of twelve pentamers. Despite this noticeable difference, the active sites are virtually identical in all structurally studied members. The main regions involved in the catalysis are located at the interface between adjacent subunits in the pentamer. Combined analysis that includes sequence-structure and evolutionary studies to find the sequence determinants of the different quaternary assemblies of this enzyme. The positions involved in icosahedral contacts suffer a larger increase in constraints than the rest. Eight sequence sites that would be the most important icosahedral sequence determinants are identified
additional information
lumazine synthase is found in different species in two different quaternary structures, pentameric and icosahedral, built from practically the same structural monomeric unit. The icosahedral structure is best described as a capsid of twelve pentamers. Despite this noticeable difference, the active sites are virtually identical in all structurally studied members. The main regions involved in the catalysis are located at the interface between adjacent subunits in the pentamer. Combined analysis that includes sequence-structure and evolutionary studies to find the sequence determinants of the different quaternary assemblies of this enzyme. The positions involved in icosahedral contacts suffer a larger increase in constraints than the rest. Eight sequence sites that would be the most important icosahedral sequence determinants are identified
additional information
lumazine synthase is found in different species in two different quaternary structures, pentameric and icosahedral, built from practically the same structural monomeric unit. The icosahedral structure is best described as a capsid of twelve pentamers. Despite this noticeable difference, the active sites are virtually identical in all structurally studied members. The main regions involved in the catalysis are located at the interface between adjacent subunits in the pentamer. Combined analysis that includes sequence-structure and evolutionary studies to find the sequence determinants of the different quaternary assemblies of this enzyme. The positions involved in icosahedral contacts suffer a larger increase in constraints than the rest. Eight sequence sites that would be the most important icosahedral sequence determinants are identified
additional information
lumazine synthase is found in different species in two different quaternary structures, pentameric and icosahedral, built from practically the same structural monomeric unit. The icosahedral structure is best described as a capsid of twelve pentamers. Despite this noticeable difference, the active sites are virtually identical in all structurally studied members. The main regions involved in the catalysis are located at the interface between adjacent subunits in the pentamer. Combined analysis that includes sequence-structure and evolutionary studies to find the sequence determinants of the different quaternary assemblies of this enzyme. The positions involved in icosahedral contacts suffer a larger increase in constraints than the rest. Eight sequence sites that would be the most important icosahedral sequence determinants are identified
additional information
lumazine synthase is found in different species in two different quaternary structures, pentameric and icosahedral, built from practically the same structural monomeric unit. The icosahedral structure is best described as a capsid of twelve pentamers. Despite this noticeable difference, the active sites are virtually identical in all structurally studied members. The main regions involved in the catalysis are located at the interface between adjacent subunits in the pentamer. Combined analysis that includes sequence-structure and evolutionary studies to find the sequence determinants of the different quaternary assemblies of this enzyme. The positions involved in icosahedral contacts suffer a larger increase in constraints than the rest. Eight sequence sites that would be the most important icosahedral sequence determinants are identified
additional information
lumazine synthase is found in different species in two different quaternary structures, pentameric and icosahedral, built from practically the same structural monomeric unit. The icosahedral structure is best described as a capsid of twelve pentamers. Despite this noticeable difference, the active sites are virtually identical in all structurally studied members. The main regions involved in the catalysis are located at the interface between adjacent subunits in the pentamer. Combined analysis that includes sequence-structure and evolutionary studies to find the sequence determinants of the different quaternary assemblies of this enzyme. The positions involved in icosahedral contacts suffer a larger increase in constraints than the rest. Eight sequence sites that would be the most important icosahedral sequence determinants are identified
additional information
lumazine synthase is found in different species in two different quaternary structures, pentameric and icosahedral, built from practically the same structural monomeric unit. The icosahedral structure is best described as a capsid of twelve pentamers. Despite this noticeable difference, the active sites are virtually identical in all structurally studied members. The main regions involved in the catalysis are located at the interface between adjacent subunits in the pentamer. Combined analysis that includes sequence-structure and evolutionary studies to find the sequence determinants of the different quaternary assemblies of this enzyme. The positions involved in icosahedral contacts suffer a larger increase in constraints than the rest. Eight sequence sites that would be the most important icosahedral sequence determinants are identified
additional information
lumazine synthase is found in different species in two different quaternary structures, pentameric and icosahedral, built from practically the same structural monomeric unit. The icosahedral structure is best described as a capsid of twelve pentamers. Despite this noticeable difference, the active sites are virtually identical in all structurally studied members. The main regions involved in the catalysis are located at the interface between adjacent subunits in the pentamer. Combined analysis that includes sequence-structure and evolutionary studies to find the sequence determinants of the different quaternary assemblies of this enzyme. The positions involved in icosahedral contacts suffer a larger increase in constraints than the rest. Eight sequence sites that would be the most important icosahedral sequence determinants are identified
additional information
lumazine synthase is found in different species in two different quaternary structures, pentameric and icosahedral, built from practically the same structural monomeric unit. The icosahedral structure is best described as a capsid of twelve pentamers. Despite this noticeable difference, the active sites are virtually identical in all structurally studied members. The main regions involved in the catalysis are located at the interface between adjacent subunits in the pentamer. Combined analysis that includes sequence-structure and evolutionary studies to find the sequence determinants of the different quaternary assemblies of this enzyme. The positions involved in icosahedral contacts suffer a larger increase in constraints than the rest. Eight sequence sites that would be the most important icosahedral sequence determinants are identified
additional information
lumazine synthase is found in different species in two different quaternary structures, pentameric and icosahedral, built from practically the same structural monomeric unit. The icosahedral structure is best described as a capsid of twelve pentamers. Despite this noticeable difference, the active sites are virtually identical in all structurally studied members. The main regions involved in the catalysis are located at the interface between adjacent subunits in the pentamer. Combined analysis that includes sequence-structure and evolutionary studies to find the sequence determinants of the different quaternary assemblies of this enzyme. The positions involved in icosahedral contacts suffer a larger increase in constraints than the rest. Eight sequence sites that would be the most important icosahedral sequence determinants are identified
additional information
lumazine synthase is found in different species in two different quaternary structures, pentameric and icosahedral, built from practically the same structural monomeric unit. The icosahedral structure is best described as a capsid of twelve pentamers. Despite this noticeable difference, the active sites are virtually identical in all structurally studied members. The main regions involved in the catalysis are located at the interface between adjacent subunits in the pentamer. Combined analysis that includes sequence-structure and evolutionary studies to find the sequence determinants of the different quaternary assemblies of this enzyme. The positions involved in icosahedral contacts suffer a larger increase in constraints than the rest. Eight sequence sites that would be the most important icosahedral sequence determinants are identified
additional information
lumazine synthase is found in different species in two different quaternary structures, pentameric and icosahedral, built from practically the same structural monomeric unit. The icosahedral structure is best described as a capsid of twelve pentamers. Despite this noticeable difference, the active sites are virtually identical in all structurally studied members. The main regions involved in the catalysis are located at the interface between adjacent subunits in the pentamer. Combined analysis that includes sequence-structure and evolutionary studies to find the sequence determinants of the different quaternary assemblies of this enzyme. The positions involved in icosahedral contacts suffer a larger increase in constraints than the rest. Eight sequence sites that would be the most important icosahedral sequence determinants are identified
additional information
lumazine synthase is found in different species in two different quaternary structures, pentameric and icosahedral, built from practically the same structural monomeric unit. The icosahedral structure is best described as a capsid of twelve pentamers. Despite this noticeable difference, the active sites are virtually identical in all structurally studied members. The main regions involved in the catalysis are located at the interface between adjacent subunits in the pentamer. Combined analysis that includes sequence-structure and evolutionary studies to find the sequence determinants of the different quaternary assemblies of this enzyme. The positions involved in icosahedral contacts suffer a larger increase in constraints than the rest. Eight sequence sites that would be the most important icosahedral sequence determinants are identified
additional information
lumazine synthase is found in different species in two different quaternary structures, pentameric and icosahedral, built from practically the same structural monomeric unit. The icosahedral structure is best described as a capsid of twelve pentamers. Despite this noticeable difference, the active sites are virtually identical in all structurally studied members. The main regions involved in the catalysis are located at the interface between adjacent subunits in the pentamer. Combined analysis that includes sequence-structure and evolutionary studies to find the sequence determinants of the different quaternary assemblies of this enzyme. The positions involved in icosahedral contacts suffer a larger increase in constraints than the rest. Eight sequence sites that would be the most important icosahedral sequence determinants are identified
additional information
lumazine synthase is found in different species in two different quaternary structures, pentameric and icosahedral, built from practically the same structural monomeric unit. The icosahedral structure is best described as a capsid of twelve pentamers. Despite this noticeable difference, the active sites are virtually identical in all structurally studied members. The main regions involved in the catalysis are located at the interface between adjacent subunits in the pentamer. Combined analysis that includes sequence-structure and evolutionary studies to find the sequence determinants of the different quaternary assemblies of this enzyme. The positions involved in icosahedral contacts suffer a larger increase in constraints than the rest. Eight sequence sites that would be the most important icosahedral sequence determinants are identified
additional information
lumazine synthase is found in different species in two different quaternary structures, pentameric and icosahedral, built from practically the same structural monomeric unit. The icosahedral structure is best described as a capsid of twelve pentamers. Despite this noticeable difference, the active sites are virtually identical in all structurally studied members. The main regions involved in the catalysis are located at the interface between adjacent subunits in the pentamer. Combined analysis that includes sequence-structure and evolutionary studies to find the sequence determinants of the different quaternary assemblies of this enzyme. The positions involved in icosahedral contacts suffer a larger increase in constraints than the rest. Eight sequence sites that would be the most important icosahedral sequence determinants are identified
additional information
lumazine synthase is found in different species in two different quaternary structures, pentameric and icosahedral, built from practically the same structural monomeric unit. The icosahedral structure is best described as a capsid of twelve pentamers. Despite this noticeable difference, the active sites are virtually identical in all structurally studied members. The main regions involved in the catalysis are located at the interface between adjacent subunits in the pentamer. Combined analysis that includes sequence-structure and evolutionary studies to find the sequence determinants of the different quaternary assemblies of this enzyme. The positions involved in icosahedral contacts suffer a larger increase in constraints than the rest. Eight sequence sites that would be the most important icosahedral sequence determinants are identified
additional information
lumazine synthase is found in different species in two different quaternary structures, pentameric and icosahedral, built from practically the same structural monomeric unit. The icosahedral structure is best described as a capsid of twelve pentamers. Despite this noticeable difference, the active sites are virtually identical in all structurally studied members. The main regions involved in the catalysis are located at the interface between adjacent subunits in the pentamer. Combined analysis that includes sequence-structure and evolutionary studies to find the sequence determinants of the different quaternary assemblies of this enzyme. The positions involved in icosahedral contacts suffer a larger increase in constraints than the rest. Eight sequence sites that would be the most important icosahedral sequence determinants are identified
additional information
lumazine synthase is found in different species in two different quaternary structures, pentameric and icosahedral, built from practically the same structural monomeric unit. The icosahedral structure is best described as a capsid of twelve pentamers. Despite this noticeable difference, the active sites are virtually identical in all structurally studied members. The main regions involved in the catalysis are located at the interface between adjacent subunits in the pentamer. Combined analysis that includes sequence-structure and evolutionary studies to find the sequence determinants of the different quaternary assemblies of this enzyme. The positions involved in icosahedral contacts suffer a larger increase in constraints than the rest. Eight sequence sites that would be the most important icosahedral sequence determinants are identified
additional information
structure analysis and comparisons, overview
additional information
lumazine synthase is found in different species in two different quaternary structures, pentameric and icosahedral, built from practically the same structural monomeric unit. The icosahedral structure is best described as a capsid of twelve pentamers. Despite this noticeable difference, the active sites are virtually identical in all structurally studied members. The main regions involved in the catalysis are located at the interface between adjacent subunits in the pentamer. Combined analysis that includes sequence-structure and evolutionary studies to find the sequence determinants of the different quaternary assemblies of this enzyme. The positions involved in icosahedral contacts suffer a larger increase in constraints than the rest. Eight sequence sites that would be the most important icosahedral sequence determinants are identified
additional information
lumazine synthase is found in different species in two different quaternary structures, pentameric and icosahedral, built from practically the same structural monomeric unit. The icosahedral structure is best described as a capsid of twelve pentamers. Despite this noticeable difference, the active sites are virtually identical in all structurally studied members. The main regions involved in the catalysis are located at the interface between adjacent subunits in the pentamer. Combined analysis that includes sequence-structure and evolutionary studies to find the sequence determinants of the different quaternary assemblies of this enzyme. The positions involved in icosahedral contacts suffer a larger increase in constraints than the rest. Eight sequence sites that would be the most important icosahedral sequence determinants are identified
additional information
lumazine synthase is found in different species in two different quaternary structures, pentameric and icosahedral, built from practically the same structural monomeric unit. The icosahedral structure is best described as a capsid of twelve pentamers. Despite this noticeable difference, the active sites are virtually identical in all structurally studied members. The main regions involved in the catalysis are located at the interface between adjacent subunits in the pentamer. Combined analysis that includes sequence-structure and evolutionary studies to find the sequence determinants of the different quaternary assemblies of this enzyme. The positions involved in icosahedral contacts suffer a larger increase in constraints than the rest. Eight sequence sites that would be the most important icosahedral sequence determinants are identified
additional information
-
lumazine synthase is found in different species in two different quaternary structures, pentameric and icosahedral, built from practically the same structural monomeric unit. The icosahedral structure is best described as a capsid of twelve pentamers. Despite this noticeable difference, the active sites are virtually identical in all structurally studied members. The main regions involved in the catalysis are located at the interface between adjacent subunits in the pentamer. Combined analysis that includes sequence-structure and evolutionary studies to find the sequence determinants of the different quaternary assemblies of this enzyme. The positions involved in icosahedral contacts suffer a larger increase in constraints than the rest. Eight sequence sites that would be the most important icosahedral sequence determinants are identified
additional information
lumazine synthase is found in different species in two different quaternary structures, pentameric and icosahedral, built from practically the same structural monomeric unit. The icosahedral structure is best described as a capsid of twelve pentamers. Despite this noticeable difference, the active sites are virtually identical in all structurally studied members. The main regions involved in the catalysis are located at the interface between adjacent subunits in the pentamer. Combined analysis that includes sequence-structure and evolutionary studies to find the sequence determinants of the different quaternary assemblies of this enzyme. The positions involved in icosahedral contacts suffer a larger increase in constraints than the rest. Eight sequence sites that would be the most important icosahedral sequence determinants are identified
additional information
lumazine synthase is found in different species in two different quaternary structures, pentameric and icosahedral, built from practically the same structural monomeric unit. The icosahedral structure is best described as a capsid of twelve pentamers. Despite this noticeable difference, the active sites are virtually identical in all structurally studied members. The main regions involved in the catalysis are located at the interface between adjacent subunits in the pentamer. Combined analysis that includes sequence-structure and evolutionary studies to find the sequence determinants of the different quaternary assemblies of this enzyme. The positions involved in icosahedral contacts suffer a larger increase in constraints than the rest. Eight sequence sites that would be the most important icosahedral sequence determinants are identified
additional information
lumazine synthase is found in different species in two different quaternary structures, pentameric and icosahedral, built from practically the same structural monomeric unit. The icosahedral structure is best described as a capsid of twelve pentamers. Despite this noticeable difference, the active sites are virtually identical in all structurally studied members. The main regions involved in the catalysis are located at the interface between adjacent subunits in the pentamer. Combined analysis that includes sequence-structure and evolutionary studies to find the sequence determinants of the different quaternary assemblies of this enzyme. The positions involved in icosahedral contacts suffer a larger increase in constraints than the rest. Eight sequence sites that would be the most important icosahedral sequence determinants are identified
additional information
lumazine synthase is found in different species in two different quaternary structures, pentameric and icosahedral, built from practically the same structural monomeric unit. The icosahedral structure is best described as a capsid of twelve pentamers. Despite this noticeable difference, the active sites are virtually identical in all structurally studied members. The main regions involved in the catalysis are located at the interface between adjacent subunits in the pentamer. Combined analysis that includes sequence-structure and evolutionary studies to find the sequence determinants of the different quaternary assemblies of this enzyme. The positions involved in icosahedral contacts suffer a larger increase in constraints than the rest. Eight sequence sites that would be the most important icosahedral sequence determinants are identified
additional information
lumazine synthase is found in different species in two different quaternary structures, pentameric and icosahedral, built from practically the same structural monomeric unit. The icosahedral structure is best described as a capsid of twelve pentamers. Despite this noticeable difference, the active sites are virtually identical in all structurally studied members. The main regions involved in the catalysis are located at the interface between adjacent subunits in the pentamer. Combined analysis that includes sequence-structure and evolutionary studies to find the sequence determinants of the different quaternary assemblies of this enzyme. The positions involved in icosahedral contacts suffer a larger increase in constraints than the rest. Eight sequence sites that would be the most important icosahedral sequence determinants are identified
additional information
lumazine synthase is found in different species in two different quaternary structures, pentameric and icosahedral, built from practically the same structural monomeric unit. The icosahedral structure is best described as a capsid of twelve pentamers. Despite this noticeable difference, the active sites are virtually identical in all structurally studied members. The main regions involved in the catalysis are located at the interface between adjacent subunits in the pentamer. Combined analysis that includes sequence-structure and evolutionary studies to find the sequence determinants of the different quaternary assemblies of this enzyme. The positions involved in icosahedral contacts suffer a larger increase in constraints than the rest. Eight sequence sites that would be the most important icosahedral sequence determinants are identified
additional information
lumazine synthase is found in different species in two different quaternary structures, pentameric and icosahedral, built from practically the same structural monomeric unit. The icosahedral structure is best described as a capsid of twelve pentamers. Despite this noticeable difference, the active sites are virtually identical in all structurally studied members. The main regions involved in the catalysis are located at the interface between adjacent subunits in the pentamer. Combined analysis that includes sequence-structure and evolutionary studies to find the sequence determinants of the different quaternary assemblies of this enzyme. The positions involved in icosahedral contacts suffer a larger increase in constraints than the rest. Eight sequence sites that would be the most important icosahedral sequence determinants are identified
additional information
lumazine synthase is found in different species in two different quaternary structures, pentameric and icosahedral, built from practically the same structural monomeric unit. The icosahedral structure is best described as a capsid of twelve pentamers. Despite this noticeable difference, the active sites are virtually identical in all structurally studied members. The main regions involved in the catalysis are located at the interface between adjacent subunits in the pentamer. Combined analysis that includes sequence-structure and evolutionary studies to find the sequence determinants of the different quaternary assemblies of this enzyme. The positions involved in icosahedral contacts suffer a larger increase in constraints than the rest. Eight sequence sites that would be the most important icosahedral sequence determinants are identified
additional information
lumazine synthase is found in different species in two different quaternary structures, pentameric and icosahedral, built from practically the same structural monomeric unit. The icosahedral structure is best described as a capsid of twelve pentamers. Despite this noticeable difference, the active sites are virtually identical in all structurally studied members. The main regions involved in the catalysis are located at the interface between adjacent subunits in the pentamer. Combined analysis that includes sequence-structure and evolutionary studies to find the sequence determinants of the different quaternary assemblies of this enzyme. The positions involved in icosahedral contacts suffer a larger increase in constraints than the rest. Eight sequence sites that would be the most important icosahedral sequence determinants are identified
additional information
lumazine synthase is found in different species in two different quaternary structures, pentameric and icosahedral, built from practically the same structural monomeric unit. The icosahedral structure is best described as a capsid of twelve pentamers. Despite this noticeable difference, the active sites are virtually identical in all structurally studied members. The main regions involved in the catalysis are located at the interface between adjacent subunits in the pentamer. Combined analysis that includes sequence-structure and evolutionary studies to find the sequence determinants of the different quaternary assemblies of this enzyme. The positions involved in icosahedral contacts suffer a larger increase in constraints than the rest. Eight sequence sites that would be the most important icosahedral sequence determinants are identified
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crystallized at room temperature by sitting-drop vapor-diffusion method, the protein is crystallized in the cubic space group I23 with the cell dimensions a = b = c = 180.8 A, diffraction data are collected to 1.6 A resolution
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sitting-drop vapor diffusion method, crystal structures of the enzyme from the hyperthermophilic bacterium Aquifex aeolicus in complex with different inhibitor compounds. The structures are refined at resolutions of 1.72 A (enzyme-7-dioxo-5H-8-ribitylaminolumazine complex), 1.85 A (enzyme-3-(7-hydroxy-8-ribityllumazine-6-yl)propionic acid complex), 2.05 A (enzyme-5-nitroso-6-ribityl-amino-2,4(1H,3H)pyrimidinedione complex) and 2.2 A (enzyme-5-(6-D-ribitylamino-2,4(1H,3H)pyrimidinedione-5-yl)-1-pentyl-phosphonic acid complex), respectively. Structural comparisons of the native enzyme and the inhibitor complexes as well as the kinetic data of single site mutants of lumazine synthase from Bacillus subtilis show that several highly conserved residues at the active site, namely Phe22, His88, Arg127, Lys135 and Glu138 are most likely involved in catalysis. A structural model of the catalytic process, which illustrates binding of substrates, enantiomer specificity, proton abstraction/donation, phosphate elimination, formation of the Schiff base and cyclization is proposed
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substrate binding site structure analysis of Aquifex aeolicus lumazine synthase in complex with the inhibitor 3-(7-hydroxy-8-ribityllumazine-6-yl)propionic acid
to 3.5 A resolution. Structure reveals the icosahedral symmetry of the enzyme. Structure-based modeling of inhibitors 4-(6-chloro-2,4-dioxo-1,2,3,4-tetrahydropyrimidine-5-yl)-n-butyl 1-phosphate, 5-(6-chloro-2,4-dioxo-1,2,3,4-tetrahydropyrimidine-5-yl)-n-pentyl 1-phosphonate, 5-(6-chloro-2,4-dioxo-1,2,3,4-tetrahydropyrimidine-5-yl)-6-keton-hexyl 1-phosphate in the active site
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crystal structure analysis of reconstituted, icosahedral beta-subunit capsids with bound substrate analogue inhibitor (5-nitro-6-(D-ribitylamino)-2,4(1H,3H)-pyrimidinedione) at 2.4 A resolution
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molecular modeling of enzyme with inhibitor 5-nitro-6-[[(2R,3R,4R)-2,3,4,5 tetrahydroxypentyl]sulfanyl]pyrimidine-2,4(1H,3H)-dione
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molecular modeling of inhibitors to the active site
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native protein, 2.4 A resolution, space group P6322 or C2. Mutant D44G/C93S/C139S/T118A crystallizes in space group R3 and diffracts to 1.6 A resolution
isoform RibH1, unliganded, to 2.2 A resolution, and bound to the substrate analogue inhibitor 5-nitro-6-ribitylamino-2,4(1H,3H)-pyrimidinedione. Comparison with structure of isoform RibH2
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three-dimensional X-ray crystal structure of the enzyme solved and refined at 2.7 A resolution to a final R-value of 0.18. Structures of the enzyme from Bacillus subtilis and Bruvella abortus are compared
isoform RibH1, bound to the substrate analogue inhibitor 5-nitro-6-ribitylamino-2,4(1H,3H)-pyrimidinedione. Comparison with structure of isoform RibH2
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crystals are obtained by means of the hanging-drop, vapor-diffusion method at room temperature
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crystallized in sitting drops by vapor diffusion. The crystal structure of lumazine synthase from Candida albicans is solved by molecular replacement and refined at 2.5 A resolution. The results of crystallographic investigations and sedimentation equilibrium experiments clearly indicate the presence of pentameric assemblies of the enzyme either in crystals or in solution
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molecular modeling of enzyme in complex with inhibitor 3-(1,3,7-trihydro-9-D-ribityl-2,6,8-purinetrione-7-yl)pentane 1-phosphate. The pyrazolopyrimidinedione ring of the ligand is stacked with the indole ring of Trp27. The phosphate of the ligand is extensively hydrogen bonded with the one water molecule, the side chain nitrogens of Arg128, as well as the backbone nitrogens of Gln86 and Thr87 and the side-chain hydroxyl of Thr87. The ribityl hydroxyl groups are hydrogen bonded to the backbone nitrogen and oxygen of Asn114, the side-chain oxygens of Glu61, and the backbone nitrogen of Ile60. The pyrazolopyrimidinedione ring of the ligand is hydrogen bonded to the backbone nitrogen of Ala59, the backbone nitrogen of Ile83, backbone oxygen of Val81, and the side-chain nitrogen of Lys138
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isoform RibH2, bound to the substrate analogue inhibitor 5-nitro-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
crystallized in the presence of two inhibitor compounds 3-(1,3,7-trihydro-9-D-ribityl-2,6,8-purinetrione-7-yl)propane 1-phosphate and 3-(1,3,7-trihydro-9-D-ribityl-2,6,8-purinetrion-7-yl)butane 1-phosphate. The crystals are obtained in sitting drops by the vapor diffusion technique with the following macroseeding procedure
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crystals are obtained in sitting drops by the vapour diffusion technique with the macroseeding procedure
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in complex with inhibitor N-6-(ribitylamino)pyrimidine-2,4(1H,3H)-dion-5-ylpropionamide and phosphate, to 2.3 A resolution. The aromatic ring of the inhibitor is packed in the hydrophobic environment in the active site formed by Trp27, Ile60, Val81 and Val82, Ile83, Phe90, and Val93 residues of one subunit. The pyrimidine ring is in stacking interaction with the indole ring of Trp27 at a distance of 4 A
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molecular modeling of binding of inhibitor 4-(6-chloro-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)butyl dihydrogen phosphate to luminazine synthase. The main forces stabilizing the complex with the enzyme involve pi-pi stacking interactions with Trp27 and hydrogen bonding of the phosphates with Arg128, the backbone nitrogens of Gly85 and Gln86, and the side chain hydroxyl of Thr87
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molecular modeling of enzyme in complex with inhibitor 3-(1,3,7-trihydro-9-D-ribityl-2,6,8-purinetrione-7-yl)pentane 1-phosphate. The pyrazolopyrimidinedione ring of the ligand is stacked with the indole ring of Trp27. The phosphate of the ligand is extensively hydrogen bonded with the one water molecule, the side chain nitrogens of Arg128, as well as the backbone nitrogens of Gln86 and Thr87 and the side-chain hydroxyl of Thr87. The ribityl hydroxyl groups are hydrogen bonded to the backbone nitrogen and oxygen of Asn114, the side-chain oxygens of Glu61, and the backbone nitrogen of Ile60. The pyrazolopyrimidinedione ring of the ligand is hydrogen bonded to the backbone nitrogen of Ala59, the backbone nitrogen of Ile83, backbone oxygen of Val81, and the side-chain nitrogen of Lys138
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sitting-drop vapour-diffusion method. Crystals of the recombinant enzyme with a size of up to 1.6 mm are obtained. The space group is P4(1)2(1)2 with lattice dimensions 82.9 A x 82.9 A x 300.2 A. X-ray diffraction data collected under cryogenic conditions are complete to 1.85 A resolution. The structure of the enzyme in complex with the intermediate analogue, 5-(6-D-ribitylamino-2,4-dihydroxypyrimidine-5-yl)-1-pentyl-phosphonic acid is solved via molecular replacement using the structure of the Bacillus subtilis enzyme as search model and is refined to a final R-factor of 19.8%
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at 3.57 A resolution. Crystals belong to monoclinic space group P21, with 60 subunits per asymmetric unit, packed as an icosahedron. Enzyme contains an N-terminal proline residue
crystals are grown at 18°C by the sitting drop vapor diffusion method. The W27Y mutant protein in complex with riboflavin, the substrate analogue 5-nitroso-6-ribitylamino-2,4(1H,3H)-pyrimidinedione, and the product analogue 6-carboxyethyl-7-oxo-8-ribityllumazine, are determined by X-ray crystallography at resolutions of 2.72.8 A
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sitting drop vapour diffusion method, the enzyme is crystallised either in complex with bound riboflavin (RIBO) or in complex with the substrate analogue 5-nitro-6-(D-ribitylamino)-2,4(1H,3H)-pyrimidinedione (NRAP) or the product analogue 6-carboxyethyl-7-oxo-8-ribityllumazine (CEOL). The mutant proteins W27G, W63Y and W63Y/L119F, which do not bind riboflavin, and the mutant L119F, which only weakly binds to riboflavin, are also analysed. Diffraction data are collected to resolutions of 2.4 A (RIBO), 2.4 A (NRAP), 2.6 A (CEOL), 2.0 A (W27G), 3.1 A (W63Y and L119F) and 2.7 A (W63Y/L119F), respectively. All crystals belong to space group C222(1) with one pentamer in the asymmetric unit corresponding to the solution state of the protein
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sitting-drop vapour diffusion method, crystallizes in space group C222(1). The crystals diffract to a resolution of 2.4 A
purified recombinant enzyme, hanging drop vapour diffusion method, mixing of 200 nl 8.4 mg/ml protein in 100 mM potassium phosphate, pH 7.5, and 150 mM NaCl, with 200 nl of reservoir solution containing 1.6 M ammonium sulfate, 100 mM sodium acetate pH 5.5, 100 mM sodium chloride, and equilibration against 0.1 ml reservoir solution, X-ray diffraction structure determination and analysis at 2.24 A resolution
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Zhang, Y.; Illarionov, B.; Bacher, A.; Fischer, M.; Georg, G.I.; Ye, Q.Z.; Vander Velde, D.; Fanwick, P.E.; Song, Y.; Cushman, M.
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Paracoccidioides brasiliensis
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Rosas, G.; Fragoso, G.; Ainciart, N.; Esquivel-Guadarrama, F.; Santana, A.; Bobes, R.J.; Ramirez-Pliego, O.; Toledo, A.; Cruz-Revilla, C.; Meneses, G.M.; Berguer, P.; Goldbaum, F.A.; Sciutto, E.
Brucella spp. lumazine synthase: a novel adjuvant and antigen delivery system to effectively induce oral immunity
Microbes Infect.
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2006
Brucella sp.
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Fornasari, M.S.; Laplagne, D.A.; Frankel, N.; Cauerhff, A.A.; Goldbaum, F.A.; Echave, J.
Sequence determinants of quaternary structure in lumazine synthase
Mol. Biol. Evol.
21
97-107
2003
Spinacia oleracea, Corynebacterium ammoniagenes (O24753), Helicobacter pylori (O24854), Methanothermobacter thermautotrophicus (O27443), Archaeoglobus fulgidus (O28152), Aquifex aeolicus (O66529), Sulfurospirillum multivorans (O68250), Arabidopsis thaliana (O80575), Chlamydia trachomatis (O84737), Bacillus subtilis (P11998), Haemophilus influenzae (P45149), Actinobacillus pleuropneumoniae (P50856), Saccharomyces cerevisiae (P50861), Photobacterium phosphoreum (P51963), Pasteurella multocida (P57869), Brucella abortus (P61711), Synechocystis sp. (P73527), Photobacterium leiognathi (Q01994), Photobacterium leiognathi (Q93E92), Bacillus amyloliquefaciens (Q44681), Rhodococcus erythropolis (Q53107), Methanocaldococcus jannaschii (Q57751), Buchnera aphidicola (Q8K9A6), Buchnera aphidicola (Q9ZNM0), Chlorobaculum tepidum (Q8KAW4), Corynebacterium glutamicum (Q8NQ53), Xanthomonas campestris (Q8PCM7), Xanthomonas citri (Q8PPD6), Methanosarcina mazei (Q8Q093), Fusobacterium nucleatum (Q8RIR4), Methanosarcina acetivorans (Q8TPT7), Methanopyrus kandleri (Q8TYL5), Agrobacterium tumefaciens (Q8UG70), Clostridium perfringens (Q8XMW9), Ralstonia solanacearum (Q8Y1H8), Anabaena sp. (Q8YQ43), Yersinia pestis (Q8ZC41), Pyrobaculum aerophilum (Q8ZTE3), Sinorhizobium meliloti (Q92NI1), Sinorhizobium meliloti (Q92QU0), Sulfurisphaera tokodaii (Q975M5), Clostridium acetobutylicum (Q97LG8), Mesorhizobium loti (Q983B0), Mesorhizobium loti (Q986N2), Caulobacter vibrioides (Q9A8J4), Caulobacter vibrioides (Q9A9S4), Mycobacterium leprae (Q9CCP3), Lactococcus lactis subsp. lactis (Q9CGU6), Streptomyces coelicolor (Q9EWJ9), Halobacterium salinarum (Q9HRM5), Pseudomonas aeruginosa (Q9HWX5), Halalkalibacterium halodurans (Q9KCL4), Vibrio cholerae (Q9KPU4), Xylella fastidiosa (Q9PES4), Campylobacter jejuni (Q9PIB9), Chlamydia muridarum (Q9PLJ4), Bartonella henselae (Q9REF4), Deinococcus radiodurans (Q9RXZ8), Schizosaccharomyces pombe (Q9UUB1), Pyricularia grisea (Q9UVT8), Thermotoga maritima (Q9X2E5), Nicotiana tabacum (Q9XH13), Chlamydia pneumoniae (Q9Z733), Helicobacter pylori J99 (Q9ZN56), Agrobacterium tumefaciens C58 / ATCC 33970 (Q8UG70)
brenda
Sciutto, E.; Toledo, A.; Cruz, C.; Rosas, G.; Meneses, G.; Laplagne, D.; Ainciart, N.; Cervantes, J.; Fragoso, G.; Goldbaum, F.A.
Brucella spp. lumazine synthase: a novel antigen delivery system
Vaccine
23
2784-2790
2005
Brucella sp.
brenda
Bellido, D.; Craig, P.O.; Mozgovoj, M.V.; Gonzalez, D.D.; Wigdorovitz, A.; Goldbaum, F.A.; Dus Santos, M.J.
Brucella spp. lumazine synthase as a bovine rotavirus antigen delivery system
Vaccine
27
136-145
2009
Brucella sp.
brenda
Morgunova, E.; Illarionov, B.; Saller, S.; Popov, A.; Sambaiah, T.; Bacher, A.; Cushman, M.; Fischer, M.; Ladenstein, R.
Structural study and thermodynamic characterization of inhibitor binding to lumazine synthase from Bacillus anthracis
Acta Crystallogr. Sect. D
66
1001-1011
2010
Bacillus anthracis
brenda
Kumar, P.; Singh, M.; Karthikeyan, S.
Crystal structure analysis of icosahedral lumazine synthase from Salmonella typhimurium, an antibacterial drug target
Acta Crystallogr. Sect. D
67
131-139
2011
Salmonella enterica subsp. enterica serovar Typhimurium (P66038), Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Talukdar, A.; Morgunova, E.; Duan, J.; Meining, W.; Foloppe, N.; Nilsson, L.; Bacher, A.; Illarionov, B.; Fischer, M.; Ladenstein, R.; Cushman, M.
Virtual screening, selection and development of a benzindolone structural scaffold for inhibition of lumazine synthase
Bioorg. Med. Chem.
18
3518-3534
2010
Mycobacterium tuberculosis
brenda
Tuan, P.A.; Kim, J.K.; Lee, S.; Chae, S.C.; Park, S.U.
Riboflavin accumulation and characterization of cDNAs encoding lumazine synthase and riboflavin synthase in bitter melon (Momordica charantia)
J. Agric. Food Chem.
60
11980-11986
2012
Momordica charantia (L0C9N6), Momordica charantia
brenda
Talukdar, A.; Zhao, Y.; Lv, W.; Bacher, A.; Illarionov, B.; Fischer, M.; Cushman, M.
O-Nucleoside, S-nucleoside, and N-nucleoside probes of lumazine synthase and riboflavin synthase
J. Org. Chem.
77
6239-6261
2012
Bacillus subtilis, Mycobacterium tuberculosis, Schizosaccharomyces pombe (Q9UUB1)
brenda
Bonomi, H.; Marchesini, M.; Klinke, S.; Ugalde, J.; Zylberman, V.; Ugalde, R.; Comerci, D.; Goldbaum, F.
An atypical riboflavin pathway is essential for Brucella abortus virulence
PLoS ONE
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e9435
2010
Brucella abortus (P61711), Brucella abortus (Q57DY1), Brucella abortus
brenda
Shankar, M.; Wilbanks, S.M.; Nakatani, Y.; Monk, B.C.; Tyndall, J.D.
Catalysis product captured in lumazine synthase from the fungal pathogen Candida glabrata
Acta Crystallogr. Sect. D
69
1580-1586
2013
[Candida] glabrata (Q6FXA8), [Candida] glabrata
brenda
Du, Z.; Li, X.; Wang, J.
Immunogenicity analysis of a novel subunit vaccine candidate molecule - recombinant L7/L12 ribosomal protein of Brucella suis
Appl. Biochem. Biotechnol.
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2016
Brucella suis (P61711), Brucella suis
brenda
Birkenmeier, M.; Neumann, S.; Roeder, T.
Kinetic modeling of riboflavin biosynthesis in Bacillus subtilis under production conditions
Biotechnol. Lett.
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919-928
2014
Bacillus subtilis (P11998), Bacillus subtilis
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Ladenstein, R.; Fischer, M.; Bacher, A.
The lumazine synthase/riboflavin synthase complex: shapes and functions of a highly variable enzyme system
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Aquifex aeolicus (O66529), Bacillus subtilis (P11998), Brucella abortus (Q2YKV1), Brucella abortus (Q2YNC6), Saccharomyces cerevisiae (P50861)
brenda
Alfano, E.; Lentz, E.; Bellido, D.; Dus Santos, M.; Goldbaum, F.; Wigdorovitz, A.; Bravo-Almonacid, F.
Expression of the multimeric and highly immunogenic Brucella spp. lumazine synthase fused to bovine rotavirus VP8D as a scaffold for antigen production in tobacco chloroplasts
Front. Plant Sci.
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1170
2015
Brucella sp. (P61711), Brucella sp. 9-941 (P61711)
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Du, Z.Q.; Wang, J.Y.
A novel lumazine synthase molecule from Brucella significantly promotes the immune-stimulation effects of antigenic protein
Genet. Mol. Res.
14
13084-13095
2015
Brucella suis (P61711), Brucella suis
brenda
Mejias, M.P.; Cabrera, G.; Fernandez-Brando, R.J.; Baschkier, A.; Ghersi, G.; Abrey-Recalde, M.J.; Miliwebsky, E.; Meiss, R.; Goldbaum, F.; Zylberman, V.; Rivas, M.; Palermo, M.S.
Protection of mice against Shiga toxin 2 (Stx2)-associated damage by maternal immunization with a Brucella lumazine synthase-Stx2 B subunit chimera
Infect. Immun.
82
1491-1499
2014
Brucella sp.
brenda
Mejias, M.P.; Ghersi, G.; Craig, P.O.; Panek, C.A.; Bentancor, L.V.; Baschkier, A.; Goldbaum, F.A.; Zylberman, V.; Palermo, M.S.
Immunization with a chimera consisting of the B subunit of Shiga toxin type 2 and Brucella lumazine synthase confers total protection against Shiga toxins in mice
J. Immunol.
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2013
Brucella sp.
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Tuan, P.; Zhao, S.; Kim, J.; Kim, Y.; Yang, J.; Li, C.; Kim, S.; Arasu, M.; Al-Dhabi, N.; Park, S.
Riboflavin accumulation and molecular characterization of cDNAs encoding bifunctional GTP cyclohydrolase II/3,4-dihydroxy-2-butanone 4-phosphate synthase, lumazine synthase, and riboflavin synthase in different organs of Lycium chinense plant
Molecules
19
17141-17153
2014
Lycium chinense (W0FEU6), Lycium chinense (W0FJR2)
brenda
Rossi, A.H.; Farias, A.; Fernandez, J.E.; Bonomi, H.R.; Goldbaum, F.A.; Berguer, P.M.
Brucella spp. lumazine synthase induces a TLR4-mediated protective response against B16 melanoma in mice
PLoS ONE
10
e0126827
2015
Brucella sp. (P61711)
brenda
Min, J.; Kim, S.; Lee, J.; Kang, S.
Lumazine synthase protein cage nanoparticles as modular delivery platforms for targeted drug delivery
RSC Adv.
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48596-48600
2014
Aquifex aeolicus
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brenda
Song, Y.; Kang, Y.J.; Jung, H.; Kim, H.; Kang, S.; Cho, H.
Lumazine synthase protein nanoparticle-Gd(III)-DOTA conjugate as a T1 contrast agent for high-field MRI
Sci. Rep.
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15656
2015
Aquifex aeolicus (O66529), Aquifex aeolicus
brenda
Akbari, R.; Sekhavati, M.H.; Bahrami, A.; Majidzadeh Heravi, R.; Yousefi, S.
Production of Brucella lumazine synthase recombinant protein to pesign a subunit vaccine against undulant fever
Arch. Razi Inst.
74
1-6
2019
Brucella melitensis (X5DV28)
brenda
Han, X.; Woycechowsky, K.J.
Encapsulation and controlled release of protein guests by the Bacillus subtilis lumazine synthase capsid
Biochemistry
56
6211-6220
2017
Bacillus subtilis
brenda
Azuma, Y.; Herger, M.; Hilvert, D.
Diversification of protein cage structure using circularly permuted subunits
J. Am. Chem. Soc.
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558-561
2018
Aquifex aeolicus (O66529), Aquifex aeolicus
brenda
Azuma, Y.; Zschoche, R.; Hilvert, D.
The C-terminal peptide of Aquifex aeolicus riboflavin synthase directs encapsulation of native and foreign guests by a cage-forming lumazine synthase
J. Biol. Chem.
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10321-10327
2017
Aquifex aeolicus, Aquifex aeolicus (O66529)
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Wei, Y.; Wahome, N.; Kumar, P.; Whitaker, N.; Picking, W.L.; Middaugh, C.R.
Effect of phosphate ion on the structure of lumazine synthase, an antigen presentation system from Bacillus anthracis
J. Pharm. Sci.
107
814-823
2018
Bacillus anthracis
brenda
Hiriart, Y.; Rossi, A.H.; Biedma, M.E.; Errea, A.J.; Moreno, G.; Cayet, D.; Rinaldi, J.; Blanca, B.; Sirard, J.C.; Goldbaum, F.; Berguer, P.; Rumbo, M.
Characterization of structural and immunological properties of a fusion protein between flagellin from Salmonella and lumazine synthase from Brucella
Protein Sci.
26
1049-1059
2017
Brucella abortus (Q2YKV1), Brucella abortus 2308 (Q2YKV1)
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Wei, Y.; Wahome, N.; VanSlyke, G.; Whitaker, N.; Kumar, P.; Barta, M.L.; Picking, W.L.; Volkin, D.B.; Mantis, N.J.; Middaugh, C.R.
Evaluation of lumazine synthase from Bacillus anthracis as a presentation platform for polyvalent antigen display
Protein Sci.
26
2059-2072
2017
Bacillus anthracis
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Lin, G.Z.; Yang, J.T.; Wei, S.C.; Chen, S.E.; Huo, S.D.; Ma, Z.R.
Immunogenicity of adenovirus and DNA vaccines co-expressing P39 and lumazine synthase proteins of Brucella abortus in BALB/c mice
Trop. Anim. Health Prod.
50
957-963
2018
Brucella abortus
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