Information on EC 2.5.1.78 - 6,7-dimethyl-8-ribityllumazine synthase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea

EC NUMBER
COMMENTARY
2.5.1.78
-
RECOMMENDED NAME
GeneOntology No.
6,7-dimethyl-8-ribityllumazine synthase
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
1-deoxy-L-glycero-tetrulose 4-phosphate + 5-amino-6-(D-ribitylamino)uracil = 6,7-dimethyl-8-(D-ribityl)lumazine + 2 H2O + phosphate
show the reaction diagram
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
flavin biosynthesis I (bacteria and plants)
-
flavin biosynthesis II (archaea)
-
flavin biosynthesis III (fungi)
-
Metabolic pathways
-
Riboflavin metabolism
-
SYSTEMATIC NAME
IUBMB Comments
5-amino-6-(D-ribitylamino)uracil butanedionetransferase
Involved in riboflavin biosynthesis.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6,7-dimethyl-8-ribityllumazine synthase
-
-
6,7-dimethyl-8-ribityllumazine synthase
-
-
6,7-dimethyl-8-ribityllumazine synthase
P50861
-
6,7-dimethyl-8-ribityllumazine synthase
-
-
6,7-dimethyl-8-ribityllumazine synthase 1
Q986N2
-
6,7-dimethyl-8-ribityllumazine synthase 1
Q92QU0
-
6,7-dimethyl-8-ribityllumazine synthase 2
Q983B0
-
6,7-dimethyl-8-ribityllumazine synthase 2
Q92NI1
-
lumazine synthase 1
Q9A9S4
-
lumazine synthase 1
Q92QU0
-
lumazine synthase 2
Q9A8J4
-
lumazine synthase 2
Q92NI1
-
lumazine synthase/riboflavin synthase complex
-
bifunctional enzyme complex
luminazine synthase
P61711
-
RIB4
P50861
gene name
ribE (gene name)
-
-
RibH
-
gene name
RibH
-
gene name
ribH1
Q57DY1
-
ribH1
-
gene name
ribH1
Q986N2
-
RibH1 protein
-
-
RibH2
P61711
-
RibH2
-
-
RibH2
Q983B0
-
type I lumazine synthase
-
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
strain C58, ATCC 33970
SwissProt
Manually annotated by BRENDA team
strain PCC 7120
SwissProt
Manually annotated by BRENDA team
lumazine synthase/riboflavin synthase complex
-
-
Manually annotated by BRENDA team
isoform RibH1
UniProt
Manually annotated by BRENDA team
isoform RibH2
SwissProt
Manually annotated by BRENDA team
isoform RibH1
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
subsp. Acyrthosiphon pisum
SwissProt
Manually annotated by BRENDA team
subsp. Schizaphis graminum
SwissProt
Manually annotated by BRENDA team
subsp. nucleatum
SwissProt
Manually annotated by BRENDA team
var. pombe
SwissProt
Manually annotated by BRENDA team
strain PCC 6803
SwissProt
Manually annotated by BRENDA team
pv. campestris
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
physiological function
P61711, Q57DY1
disruption mutants of either isform RibH1 or RibH2 obtained without any major difficulty, are not auxotrophic for riboflavin and grow at wild-type rates in both rich and minimal media. A double mutant lacking both RibH1 and RibH2 activity is not viable; disruption mutants of either isform RibH1 or RibH2 obtained without any major difficulty, are not auxotrophic for riboflavin and grow at wild-type rates in both rich and minimal media. A double mutant lacking both RibH1 and RibH2 activity is not viable. For virulence, at least one isoform must be present for Brucella abortus survival and RibH2 and not RibH1 is essential for intracellular survival due to its luminazine synthase activity in vivo.
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
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
show the reaction diagram
-
-
-
-
-
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
show the reaction diagram
-
-
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (3S)-3,4-dihydroxy-2-butanone
?
show the reaction diagram
-
-
-
-
?
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
-
-
-
?
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
show the reaction diagram
-
-
-
-
?
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
show the reaction diagram
-
-
-
-
?
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
show the reaction diagram
-
-
-
-
?
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
show the reaction diagram
-
-
-
-
?
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
show the reaction diagram
-
-
-
-
?
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
show the reaction diagram
-
-
-
-
?
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
show the reaction diagram
-
-
-
-
?
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
show the reaction diagram
-
-
-
-
?
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
show the reaction diagram
-
-
-
-
?
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
show the reaction diagram
-
-
-
-
?
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
show the reaction diagram
P61711
-
-
-
?
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
show the reaction diagram
-, Q57751
-
-
-
?
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
show the reaction diagram
P61711
-
-
-
?
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
show the reaction diagram
-
-
-
-
?
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
show the reaction diagram
P50861
-
-
-
?
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
show the reaction diagram
Q44681
-
-
-
?
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
show the reaction diagram
Q9KCL4
-
-
-
?
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
show the reaction diagram
Q983B0, Q986N2
-
-
-
?
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
show the reaction diagram
Q9UUB1, -
-
-
-
?
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
show the reaction diagram
Q9X2E5
-
-
-
?
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
show the reaction diagram
Q9KPU4
-
-
-
?
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
Q01994, Q93E92
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
show the reaction diagram
-
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
show the reaction diagram
Q8PPD6
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
show the reaction diagram
Q8PCM7
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
show the reaction diagram
Q9PES4
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
show the reaction diagram
Q8ZC41
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
show the reaction diagram
-
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
show the reaction diagram
P50856
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
show the reaction diagram
Q8UG70
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
show the reaction diagram
-
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
show the reaction diagram
O66529
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
show the reaction diagram
O80575
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
show the reaction diagram
O28152
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
show the reaction diagram
Q9REF4
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
show the reaction diagram
Q8K9A6, Q9ZNM0
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
show the reaction diagram
Q9PIB9
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
show the reaction diagram
Q9A8J4, Q9A9S4
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
show the reaction diagram
Q9PLJ4
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
show the reaction diagram
O84737
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
show the reaction diagram
Q8KAW4
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
show the reaction diagram
Q97LG8
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
show the reaction diagram
Q8XMW9
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
show the reaction diagram
O24753
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
show the reaction diagram
Q8NQ53
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
show the reaction diagram
O68250
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
show the reaction diagram
Q9RXZ8
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
show the reaction diagram
Q8RIR4
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
show the reaction diagram
P45149
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
show the reaction diagram
Q9HRM5
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
show the reaction diagram
O24854
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
show the reaction diagram
Q9ZN56
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
show the reaction diagram
Q9CGU6
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
show the reaction diagram
Q9UVT8
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
show the reaction diagram
Q8TYL5
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
show the reaction diagram
Q8TPT7
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
show the reaction diagram
Q8Q093
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
show the reaction diagram
O27443
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
show the reaction diagram
Q9CCP3
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
show the reaction diagram
Q9UUB1
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
show the reaction diagram
Q9XH13
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
show the reaction diagram
Q8YQ43
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
show the reaction diagram
P57869
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
show the reaction diagram
P51963
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
show the reaction diagram
Q9HWX5
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
show the reaction diagram
Q8ZTE3
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
show the reaction diagram
Q8Y1H8
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
show the reaction diagram
Q53107
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
show the reaction diagram
Q92NI1, Q92QU0
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
show the reaction diagram
Q9EWJ9
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
show the reaction diagram
Q975M5
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
show the reaction diagram
P73527
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
show the reaction diagram
-
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
show the reaction diagram
Q57751
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
show the reaction diagram
P50861
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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 + 5-nitro-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
?
show the reaction diagram
-
-
-
-
?
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
show the reaction diagram
-
-
-
-
?
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
show the reaction diagram
-
-
-
-
-
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
show the reaction diagram
-
-
-
-
?
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
show the reaction diagram
Q983B0, Q986N2
-
-
-
?
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
show the reaction diagram
-
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 + 3,4-dihydroxy-2-butanone 4-phosphate
6,7-dimethyl-8-ribityllumazine + 2 H2O + phosphate
show the reaction diagram
P66038
-
-
-
?
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
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
show the reaction diagram
-
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
show the reaction diagram
-
-
-
-
?
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
show the reaction diagram
-
-
-
-
?
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
show the reaction diagram
-
-
-
-
?
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
show the reaction diagram
P61711
-
-
-
?
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
show the reaction diagram
-
-
-
-
?
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
show the reaction diagram
Q44681
-
-
-
?
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
show the reaction diagram
Q9KCL4
-
-
-
?
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
show the reaction diagram
Q9UUB1, -
-
-
-
?
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
show the reaction diagram
Q9X2E5
-
-
-
?
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
show the reaction diagram
Q9KPU4
-
-
-
?
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
Q8PPD6
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
show the reaction diagram
Q8PCM7
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
show the reaction diagram
Q9PES4
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
show the reaction diagram
Q8ZC41
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
show the reaction diagram
-
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
show the reaction diagram
P50856
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
show the reaction diagram
Q8UG70
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
show the reaction diagram
-
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
show the reaction diagram
O66529
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
show the reaction diagram
O80575
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
show the reaction diagram
O28152
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
show the reaction diagram
Q9REF4
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
show the reaction diagram
Q8K9A6, Q9ZNM0
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
show the reaction diagram
Q9PIB9
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
show the reaction diagram
Q9A8J4, Q9A9S4
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
show the reaction diagram
Q9PLJ4
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
show the reaction diagram
O84737
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
show the reaction diagram
Q8KAW4
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
show the reaction diagram
Q8XMW9
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
show the reaction diagram
O24753
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
show the reaction diagram
Q8NQ53
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
show the reaction diagram
O68250
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
show the reaction diagram
Q9RXZ8
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
show the reaction diagram
Q8RIR4
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
show the reaction diagram
P45149
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
show the reaction diagram
Q9HRM5
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
show the reaction diagram
Q9ZN56
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
show the reaction diagram
Q9CGU6
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
show the reaction diagram
Q9UVT8
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
show the reaction diagram
Q8TYL5
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
show the reaction diagram
Q8TPT7
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
show the reaction diagram
Q8Q093
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
show the reaction diagram
O27443
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
show the reaction diagram
Q9CCP3
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
show the reaction diagram
Q9UUB1
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
show the reaction diagram
Q9XH13
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
show the reaction diagram
Q8YQ43
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
show the reaction diagram
P57869
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
show the reaction diagram
Q01994, Q93E92
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
show the reaction diagram
P51963
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
show the reaction diagram
Q9HWX5
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
show the reaction diagram
Q8ZTE3
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
show the reaction diagram
Q8Y1H8
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
show the reaction diagram
Q53107
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
show the reaction diagram
Q92NI1, Q92QU0
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
show the reaction diagram
Q9EWJ9
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
show the reaction diagram
Q975M5
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
show the reaction diagram
P73527
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
show the reaction diagram
-
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
show the reaction diagram
Q57751
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
show the reaction diagram
P50861
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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-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
show the reaction diagram
-
-
-
-
?
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
(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
-
competitive
(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
-
association constants and thermodynamic parameters of binding
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-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
-
inhibition of both lumazine synthase and riboflavin synthase
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
-
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)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
-
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
3-[4,6-dioxo-4,5,6,7-tetrahydro-1-D-ribityl-1H-pyrazolo[3,4-d]pyrimidin-3-yl]propyl 1-phosphate
-
competitive
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
-
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-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-tetrahydropyrimidine-5-yl)-6-keton-hexyl 1-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-(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; crystallization data
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
-
inhibition of both lumazine synthase and riboflavin synthase
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
-
competitive
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
-
competitive
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
-
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
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
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
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
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.13
-
(3S)-3,4-dihydroxy-2-butanone
-
native enzyme complex, pH 7.0, 37C
0.0025
-
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
isoform RibH1, pH 7.0, 37C
0.003
-
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
Q9UUB1
pH 7.0, 37C, mutant enzyme W27F; pH 7.0, 37C, mutant enzyme W27Y
0.004
-
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
pH 7.0, 37C
0.004
-
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
-
0.0041
-
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
pH 7.0, 37C, 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, 37C, mutant enzyme A56S
0.005
-
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
Q9UUB1
pH 7.0, 37C, wild-type enzyme
0.00612
-
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
pH 7.0, 37C, mutant enzyme F22W
0.00857
-
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
pH 7.0, 37C, wild-type enzyme
0.01
-
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
37C, pH 7.0
0.01
-
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
pH 7.0, 37C, mutant enzyme D138A
0.0107
-
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
pH 7.0, 37C, mutant enzyme F22V
0.011
-
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
pH 7.0, 37C, mutant enzyme S142L
0.0115
-
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
pH 7.0, 37C, mutant enzyme K135A
0.0119
-
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
pH 7.0, 37C, mutant enzyme N23S
0.0125
-
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
37C, pH 7.0
0.0138
-
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
pH 7.0, 37C, mutant enzyme K131R
0.02
-
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
isoform RibH2, pH 7.0, 37C
0.02
-
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
-
0.0345
-
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
pH 7.0, 37C, mutant enzyme F57S
0.0355
-
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
pH 7.0, 37C, mutant enzyme K131N
0.056
-
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
pH 7.0, 37C, mutant enzyme H88K
0.0849
-
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
pH 7.0, 37C, 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, 37C, mutant enzyme F22S
0.147
-
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
pH 7.0, 37C, mutant enzyme H88A
0.173
-
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
pH 7.0, 37C, mutant enzyme E58Q
0.23
-
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
Q9UUB1
pH 7.0, 37C, mutant enzyme W27I
0.278
-
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
pH 7.0, 37C, mutant enzyme F113S
0.4
-
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
Q9UUB1
pH 7.0, 37C, mutant enzyme W27H
0.43
-
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
Q9UUB1
pH 7.0, 37C, mutant enzyme W27G
0.46
-
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
Q9UUB1
pH 7.0, 37C, mutant enzyme W27S
0.72
-
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
pH 7.0, 37C, mutant enzyme F22D
0.005
-
5-nitro-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
native enzyme complex, pH 7.0, 37C
0.0052
-
L-3,4-dihydroxybutan-2-one 4-phosphate
-
pH 7.0, 37C, Tris buffer
0.0067
-
L-3,4-dihydroxybutan-2-one 4-phosphate
-
pH 7.0, 37C, MOPS buffer
0.015
-
L-3,4-dihydroxybutan-2-one 4-phosphate
-
isoform RibH1, pH 7.0, 37C
0.026
-
L-3,4-dihydroxybutan-2-one 4-phosphate
-
37C, pH 7.0
0.026
-
L-3,4-dihydroxybutan-2-one 4-phosphate
-
-
0.042
-
L-3,4-dihydroxybutan-2-one 4-phosphate
-
pH 7.0, 37C, mutant enzyme H88K; pH 7.0, 37C, mutant enzyme T80V
0.05
-
L-3,4-dihydroxybutan-2-one 4-phosphate
-
pH 7.0, 37C, mutant enzyme K131R
0.05
-
L-3,4-dihydroxybutan-2-one 4-phosphate
-
pH 7.0, 37C, phosphate buffer
0.052
-
L-3,4-dihydroxybutan-2-one 4-phosphate
-
37C, pH 7.0
0.0546
-
L-3,4-dihydroxybutan-2-one 4-phosphate
-
pH 7.0, 37C, wild-type enzyme
0.0581
-
L-3,4-dihydroxybutan-2-one 4-phosphate
-
pH 7.0, 37C, mutant enzyme N23S
0.0598
-
L-3,4-dihydroxybutan-2-one 4-phosphate
-
pH 7.0, 37C, mutant enzyme F22W
0.06
-
L-3,4-dihydroxybutan-2-one 4-phosphate
-
pH 7.0, 37C, 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, 37C, mutant enzyme D138A
0.065
-
L-3,4-dihydroxybutan-2-one 4-phosphate
Q9UUB1
pH 7.0, 37C, mutant enzyme W27F
0.0665
-
L-3,4-dihydroxybutan-2-one 4-phosphate
-
pH 7.0, 37C, mutant enzyme F113S
0.067
-
L-3,4-dihydroxybutan-2-one 4-phosphate
Q9UUB1
pH 7.0, 37C, wild-type enzyme
0.0702
-
L-3,4-dihydroxybutan-2-one 4-phosphate
-
pH 7.0, 37C, mutant enzyme A56S
0.08
-
L-3,4-dihydroxybutan-2-one 4-phosphate
-
pH 7.0, 37C, mutant enzyme F57S
0.086
-
L-3,4-dihydroxybutan-2-one 4-phosphate
Q9UUB1
pH 7.0, 37C, 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, 37C, mutant enzyme S142L
0.124
-
L-3,4-dihydroxybutan-2-one 4-phosphate
-
pH 7.0, 37C, mutant enzyme F22V
0.125
-
L-3,4-dihydroxybutan-2-one 4-phosphate
-
-
0.137
-
L-3,4-dihydroxybutan-2-one 4-phosphate
Q9UUB1
pH 7.0, 37C, mutant enzyme W27I
0.137
-
L-3,4-dihydroxybutan-2-one 4-phosphate
-
pH 7.0, 37C, mutant enzyme F22S
0.145
-
L-3,4-dihydroxybutan-2-one 4-phosphate
Q9UUB1
pH 7.0, 37C, mutant enzyme W27H
0.146
-
L-3,4-dihydroxybutan-2-one 4-phosphate
-
pH 7.0, 37C, mutant enzyme E58Q
0.167
-
L-3,4-dihydroxybutan-2-one 4-phosphate
-
pH 7.0, 37C, mutant enzyme K135A
0.168
-
L-3,4-dihydroxybutan-2-one 4-phosphate
Q9UUB1
pH 7.0, 37C, mutant enzyme W27G
0.187
-
L-3,4-dihydroxybutan-2-one 4-phosphate
Q9UUB1
pH 7.0, 37C, mutant enzyme W27S
0.225
-
L-3,4-dihydroxybutan-2-one 4-phosphate
-
pH 7.0, 37C
0.283
-
L-3,4-dihydroxybutan-2-one 4-phosphate
-
pH 7.0, 37C, mutant enzyme K131N
0.45
-
L-3,4-dihydroxybutan-2-one 4-phosphate
-
isoform RibH2, pH 7.0, 37C
0.675
-
L-3,4-dihydroxybutan-2-one 4-phosphate
-
pH 7.0, 37C, mutant enzyme F22D
3.14
-
L-3,4-dihydroxybutan-2-one 4-phosphate
-
pH 7.0, 37C, mutant enzyme R127H
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0003
-
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
isoform RibH2, pH 7.0, 37C
0.0022
-
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
pH 7.0, 37C, mutant enzyme H88K
0.003
-
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
pH 7.0, 37C
0.0038
-
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
pH 7.0, 37C, mutant enzyme F113S
0.0054
-
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
pH 7.0, 37C, mutant enzyme K131N
0.0067
-
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
pH 7.0, 37C, mutant enzyme H88A
0.0081
-
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
pH 7.0, 37C, mutant enzyme F22D
0.0122
-
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
pH 7.0, 37C, mutant enzyme K135A; pH 7.0, 37C, mutant enzyme N23S
0.0147
-
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
pH 7.0, 37C, mutant enzyme F22V
0.0166
-
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
pH 7.0, 37C, mutant enzyme K131R
0.0244
-
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
pH 7.0, 37C, mutant enzyme F22W; pH 7.0, 37C, mutant enzyme F57S
0.0263
-
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
pH 7.0, 37C, mutant enzyme F22S
0.0307
-
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
pH 7.0, 37C, mutant enzyme T80V
0.0347
-
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
pH 7.0, 37C, mutant enzyme S142L
0.0389
-
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
pH 7.0, 37C, mutant enzyme R127H
0.0391
-
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
pH 7.0, 37C, mutant enzyme E58Q
0.04
-
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
isoform RibH1, pH 7.0, 37C
0.0453
-
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
pH 7.0, 37C, mutant enzyme A56S
0.051
-
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
pH 7.0, 37C, mutant enzyme D138A
0.0557
-
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
pH 7.0, 37C, wild-type enzyme
0.056
-
5-nitro-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
native enzyme complex, pH 7.0, 37C
0.076
-
5-nitro-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
hollow beta60 capsid, pH 7.0, 37C
0.0022
-
L-3,4-dihydroxybutan-2-one 4-phosphate
-
pH 7.0, 37C, mutant enzyme H88K
0.0038
-
L-3,4-dihydroxybutan-2-one 4-phosphate
-
pH 7.0, 37C, mutant enzyme F113S
0.0054
-
L-3,4-dihydroxybutan-2-one 4-phosphate
-
pH 7.0, 37C, mutant enzyme K131N
0.0067
-
L-3,4-dihydroxybutan-2-one 4-phosphate
-
pH 7.0, 37C, mutant enzyme H88A
0.0081
-
L-3,4-dihydroxybutan-2-one 4-phosphate
-
pH 7.0, 37C, mutant enzyme F22D
0.0122
-
L-3,4-dihydroxybutan-2-one 4-phosphate
-
pH 7.0, 37C, mutant enzyme K135A; pH 7.0, 37C, mutant enzyme N23S
0.0147
-
L-3,4-dihydroxybutan-2-one 4-phosphate
-
pH 7.0, 37C, mutant enzyme F22V
0.0166
-
L-3,4-dihydroxybutan-2-one 4-phosphate
-
pH 7.0, 37C, mutant enzyme K131R
0.0244
-
L-3,4-dihydroxybutan-2-one 4-phosphate
-
pH 7.0, 37C, mutant enzyme F22W; pH 7.0, 37C, mutant enzyme F57S
0.0263
-
L-3,4-dihydroxybutan-2-one 4-phosphate
-
pH 7.0, 37C, mutant enzyme F22S
0.0307
-
L-3,4-dihydroxybutan-2-one 4-phosphate
-
pH 7.0, 37C, mutant enzyme T80V
0.0347
-
L-3,4-dihydroxybutan-2-one 4-phosphate
-
pH 7.0, 37C, mutant enzyme S142L
0.0389
-
L-3,4-dihydroxybutan-2-one 4-phosphate
-
pH 7.0, 37C, mutant enzyme R127H
0.0391
-
L-3,4-dihydroxybutan-2-one 4-phosphate
-
pH 7.0, 37C, mutant enzyme E58Q
0.0453
-
L-3,4-dihydroxybutan-2-one 4-phosphate
-
pH 7.0, 37C, mutant enzyme A56S
0.051
-
L-3,4-dihydroxybutan-2-one 4-phosphate
-
pH 7.0, 37C, mutant enzyme D138A
0.0557
-
L-3,4-dihydroxybutan-2-one 4-phosphate
-
pH 7.0, 37C, wild-type enzyme
0.056
-
L-3,4-dihydroxybutan-2-one 4-phosphate
-
native enzyme complex, pH 7.0, 37C
0.076
-
L-3,4-dihydroxybutan-2-one 4-phosphate
-
hollow beta60 capsid, pH 7.0, 37C
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
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, 37C, variable concentration of 5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
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, 37C, 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, 37C, 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, 27C
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, 27C
0.041
-
(E)-4-(2-(5-nitro-2,6-dioxo-1,2,3,6-tetrahydropyrimidine-4-yl)vinyl)benzoate
-
pH 7.0, 27C
0.035
-
(E)-4-(2-(5-nitro-2,6-dioxo-1,2,3,6-tetrahydropyrimidine-4-yl)vinyl)benzoic acid
-
pH 7.0, 27C
0.095
-
(E)-5-nitro-6-(2-hydroxystyryl)pyrimidine-2,4(1H,3H)-dione
-
pH 7.0, 27C
0.21
-
(E)-5-nitro-6-(2-hydroxystyryl)pyrimidine-2,4(1H,3H)-dione
-
pH 7.0, 27C
0.026
-
(E)-5-nitro-6-(3-(pyridin-3-yl)vinyl)pyrimidine-2,4(1H,3H)-dione
-
pH 7.0, 27C
0.011
-
(E)-5-nitro-6-(3-nitrostyryl)pyrimidine-2,4(1H,3H)-dione
-
pH 7.0, 27C
0.042
-
(E)-5-nitro-6-(3-nitrostyryl)pyrimidine-2,4(1H,3H)-dione
-
pH 7.0, 27C
0.026
-
(E)-5-nitro-6-(4-bromostyryl)pyrimidine-2,4(1H,3H)-dione
-
pH 7.0, 27C
0.0037
-
(E)-5-nitro-6-(4-nitrostyryl)pyrimidine-2,4(1H,3H)-dione
-
pH 7.0, 27C
0.013
-
(E)-5-nitro-6-(4-nitrostyryl)pyrimidine-2,4(1H,3H)-dione
-
pH 7.0, 27C
0.013
-
(E)-5-nitro-6-[2-(1H-pyrrol-2-yl)vinyl]pyrimidine-2,4(1H,3H)-dione
-
pH 7.0, 27C
0.03
-
(E)-5-nitro-6-[2-(1H-pyrrol-2-yl)vinyl]pyrimidine-2,4(1H,3H)-dione
-
pH 7.0, 27C
0.048
-
(E)-6-(2,3,4-trimethoxystyryl)-5-nitropyrimidine-2,4(1H,3H)-dione
-
pH 7.0, 27C
0.0049
-
(E)-6-(2,3-dihydroxystyryl)-5-nitropyrimidine-2,4(1H,3H)-dione
-
pH 7.0, 27C
0.012
-
(E)-6-(2,3-dihydroxystyryl)-5-nitropyrimidine-2,4(1H,3H)-dione
-
pH 7.0, 27C
0.0096
-
(E)-6-(2,3-dimethoxystyryl)-5-nitropyrimidine-2,4(1H,3H)-dione
-
pH 7.0, 27C
0.243
-
(E)-6-(2,3-dimethoxystyryl)-5-nitropyrimidine-2,4(1H,3H)-dione
-
pH 7.0, 27C
0.07
-
(E)-6-(2-(3H-indol-3-yl)vinyl)-5-nitropyrimidine-2,4(1H,3H)-dione
-
pH 7.0, 27C
0.141
-
(E)-6-(2-(3H-indol-3-yl)vinyl)-5-nitropyrimidine-2,4(1H,3H)-dione
-
pH 7.0, 27C
0.011
-
(E)-6-(2-(naphthalen-2-yl)vinyl)-5-nitropyrimidine-2,4(1H,3H)-dione
-
pH 7.0, 27C
0.094
-
(E)-6-(2-(naphthalen-2-yl)vinyl)-5-nitropyrimidine-2,4(1H,3H)-dione
-
pH 7.0, 27C
0.024
-
(E)-6-(2-fluoro-3-methoxystyryl)-5-nitropyrimidine-2,4(1H,3H)-dione
-
pH 7.0, 27C
0.151
-
(E)-6-(2-fluoro-3-methoxystyryl)-5-nitropyrimidine-2,4(1H,3H)-dione
-
pH 7.0, 27C
0.0078
-
(E)-6-(2-fluorostyryl)-5-nitropyrimidine-2,4(1H,3H)-dione
-
pH 7.0, 27C
0.042
-
(E)-6-(2-hydroxy-3-nitrostyryl)-3-nitropyrimidine-2,4(1H,3H)-dione
-
pH 7.0, 27C
0.031
-
(E)-6-(2-hydroxy-5-nitrostyryl)-5-nitropyrimidine-2,4(1H,3H)-dione
-
pH 7.0, 27C
0.023
-
(E)-6-(2-methoxy-5-nitrostyryl)-5-nitropyrimidine-2,4(1H,3H)-dione
-
pH 7.0, 27C
0.085
-
(E)-6-(2-methoxy-5-nitrostyryl)-5-nitropyrimidine-2,4(1H,3H)-dione
-
pH 7.0, 27C
0.028
-
(E)-6-(2-methoxystyryl)-5-nitropyrimidine-2,4(1H,3H)-dione
-
pH 7.0, 27C
0.205
-
(E)-6-(2-methoxystyryl)-5-nitropyrimidine-2,4(1H,3H)-dione
-
pH 7.0, 27C
0.016
-
(E)-6-(2-nitrostyryl)-5-nitropyrimidine-2,4(1H,3H)-dione
-
pH 7.0, 27C
0.017
-
(E)-6-(3,4,5-trimethoxystyryl)-5-nitropyrimidine-2,4(1H,3H)-dione
-
pH 7.0, 27C
0.032
-
(E)-6-(3,4-dimethoxystyryl)-5-nitropyrimidine-2,4(1H,3H)-dione
-
pH 7.0, 27C
0.052
-
(E)-6-(3-hydroxy-4-methoxystyryl)-5-nitropyrimidine-2,4(1H,3H)-dione
-
pH 7.0, 27C
0.012
-
(E)-6-(3-hydroxy-4-nitrostyryl)-5-nitropyrimidine-2,4(1H,3H)-dione
-
pH 7.0, 27C
0.094
-
(E)-6-(3-hydroxy-4-nitrostyryl)-5-nitropyrimidine-2,4(1H,3H)-dione
-
pH 7.0, 27C
0.0071
-
(E)-6-(3-hydroxystyryl)-5-nitropyrimidine-2,4(1H,3H)-dione
-
pH 7.0, 27C
0.045
-
(E)-6-(4-chlorostyryl)-5-nitropyrimidine-2,4(1H,3H)-dione
-
pH 7.0, 27C
0.086
-
(E)-6-(4-fluorostyryl)-5-nitropyrimidine-2,4(1H,3H)-dione
-
pH 7.0, 27C
0.087
-
(E)-6-(4-hydroxy-3-nitrostyryl)-5-nitropyrimidine-2,4(1H,3H)-dione
-
pH 7.0, 27C
0.012
-
(E)-6-(4-hydroxystyryl)-5-nitropyrimidine-2,4(1H,3H)-dione
-
pH 7.0, 27C
0.35
-
1,3,6,8-tetrahydroxynaphthyridine
-
pH 7.0, 37C
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, 37C
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, 37C
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, 37C, 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, 37C, variable concentration of L-3,4-dihydroxybutan-2-one 4-phosphate
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, 37C, 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, 37C
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, 37C
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, 37C
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, 37C
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, 37C
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, 37C, 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, 37C
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, 37C, 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, 37C, 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, 37C, 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, 37C, 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, 37C, variable concentration of L-3,4-dihydroxybutan-2-one 4-phosphate
0.44
-
1-deoxy-1-[[2,6-dioxo-5-(4-phosphonobutyl)-1,2,3,6-tetrahydropyrimidin-4-yl]amino]-D-ribitol
-
pH 7.0, 37C, 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, 37C, 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, 37C, 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, 37C, 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, 37C, 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, 37C, 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, 27C
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, 27C
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, 27C
0.022
-
2,5,8,11-tetraaza-5,11-dihydro-4,10-dihydroxyperylene-1,3,6,7,9,12-hexaone
-
pH 7.0, 37C, 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, 37C, Tris buffer
0.07
-
2-(2-oxo-1,2-dihydrobenzo[cd]indole-6-sulfonamido)acetic acid
-
pH 7.0, 27C
0.0026
-
3-(1,3,7,9-tetrahydro-9-D-ribityl-2,6,8-trioxopurin-7-yl)-1-propanol
-
pH 7.0, 37C, variable concentration of 5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
0.0045
-
3-(1,3,7,9-tetrahydro-9-D-ribityl-2,6,8-trioxopurin-7-yl)propane 1-phosphate
-
pH 7.0, 37C, 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, 37C, 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, 27C
0.000014
-
3-(1,3,7-trihydro-9-D-ribityl-2,6,8-purinetrione-7-yl)butane 1-phosphate
-
pH 7.0, 27C
0.000015
-
3-(1,3,7-trihydro-9-D-ribityl-2,6,8-purinetrione-7-yl)butane 1-phosphate
-
pH 7.0, 27C
0.0000008
-
3-(1,3,7-trihydro-9-D-ribityl-2,6,8-purinetrione-7-yl)pentane 1-phosphate
-
pH 7.0, 27C
0.0000009
-
3-(1,3,7-trihydro-9-D-ribityl-2,6,8-purinetrione-7-yl)pentane 1-phosphate
-
pH 7.0, 27C
0.00003
-
3-(1,3,7-trihydro-9-D-ribityl-2,6,8-purinetrione-7-yl)pentane 1-phosphate
-
pH 7.0, 27C
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, 27C
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, 27C
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, 27C
0.0041
-
4-(1,3,7,9-tetrahydro-9-D-ribityl-2,6,8-trioxopurin-7-yl)butane 1-phosphate
-
pH 7.0, 37C, 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, 37C, 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, 37C
0.15
-
4-(1,5,6,7-tetrahydro-6,7-dioxo-8-D-ribityllumazin-5-yl)butane 1-phosphate
-
pH 7.0, 37C
0.038
-
4-(2-oxo-1,2-dihydrobenzo[cd]indole-6-sulfonamido)butyl dihydrogen phosphate
-
pH 7.0, 27C
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, 37C, 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, 37C, 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, 37C, recombinant beta60 capsid
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, 27C
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, 27C
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, 37C, 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, 37C, 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, 37C
0.027
-
5-(1,5,6,7-tetrahydro-6,7-dioxo-8-D-ribityllumazin-5-yl)pentane 1-phosphate
-
pH 7.0, 37C
0.86
-
5-(4-phosphonobutyryl)amino-6-D-ribitylaminouracil
-
pH 7.5, 37C, recombinant beta60 capsid
1
-
5-(5-phosphonopentyl)amino-6-D-ribitylaminouracil
-
pH 7.5, 37C, recombinant beta60 capsid
0.83
-
5-(5-phosphonoxyvaleryl)amino-6-D-ribitylaminouracil
-
pH 7.5, 37C, recombinant beta60 capsid
0.00014
-
5-(6-chloro-2,4-dioxo-1,2,3,4-tetrahydropyrimidine-5-yl)-6-keton-hexyl 1-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, 37C, 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, 37C, recombinant beta60 capsid
0.015
-
5-nitro-6-styryluracil
-
pH 7.0, 27C
0.143
-
5-nitro-6-styryluracil
-
pH 7.0, 27C
0.264
-
5-nitro-6-[(D-ribityl)methyl]pyrimidine-2,4-dione
-
pH 7.0, 37C, variable concentration of 5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
0.002
-
5-nitro-6-[[(2R,3R,4R)-2,3,4,5 tetrahydroxypentyl]sulfanyl]pyrimidine-2,4(1H,3H)-dione
-
pH 7.0, 27C
0.011
-
5-nitro-6-[[(2R,3R,4R)-2,3,4,5 tetrahydroxypentyl]sulfanyl]pyrimidine-2,4(1H,3H)-dione
-
pH 7.0, 27C
0.026
-
5-nitro-6-[[(2R,3R,4R)-2,3,4,5 tetrahydroxypentyl]sulfanyl]pyrimidine-2,4(1H,3H)-dione
-
pH 7.0, 27C
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, 27C
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, 27C
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, 37C, recombinant beta60 capsid
0.0014
-
8-[[(2S,3S,4R)-2,3,4,5-tetrahydroxypentyl]amino]tetrahydropteridine-2,4,6,7(1H,3H)-tetrone
-
pH 7.0, 27C
0.0078
-
8-[[(2S,3S,4R)-2,3,4,5-tetrahydroxypentyl]amino]tetrahydropteridine-2,4,6,7(1H,3H)-tetrone
-
pH 7.0, 27C
0.046
-
9-[(2S,3S,4R)-2,3,4,5-tetrahydroxypentyl]-7,9-dihydro-1H-purine-2,6,8(3H)-trione
-
pH 7.5, 37C, recombinant beta60 capsid
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, 27C
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, 27C
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, 27C
0.017
-
riboflavin
Q9UUB1
pH 7.0, 37C, wild-type enzyme
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.011
-
N-6-(ribitylamino)pyrimidine-2,4(1H,3H)-dion-5-ylpropionamide
-
pH 7.0, 27C
0.02
-
N-6-(ribitylamino)pyrimidine-2,4(1H,3H)-dion-5-ylpropionamide
-
pH 7.0, 27C
0.11
-
N-6-(ribitylamino)pyrimidine-2,4(1H,3H)-dion-5-ylpropionamide
-
pH 7.0, 27C
0.0079
-
N-6-(ribitylamino)pyrimidine-2,4(1H,3H)-dione-5-ylisobutyramide
-
pH 7.0, 27C
0.042
-
N-6-(ribitylamino)pyrimidine-2,4(1H,3H)-dione-5-ylisobutyramide
-
pH 7.0, 27C
0.095
-
N-6-(ribitylamino)pyrimidine-2,4(1H,3H)-dione-5-ylisobutyramide
-
pH 7.0, 27C
0.00101
-
N-[2,4-dioxo-6-(ribitylamino)-1,2,3,4-tetrahydropyrimidin-5-yl]oxalamic acid ethyl ester
-
pH 7.0, 27C
0.004
-
N-[2,4-dioxo-6-(ribitylamino)-1,2,3,4-tetrahydropyrimidin-5-yl]oxalamic acid ethyl ester
-
pH 7.0, 27C
0.607
-
N-[2,4-dioxo-6-(ribitylamino)-1,2,3,4-tetrahydropyrimidin-5-yl]oxalamic acid ethyl ester
-
pH 7.0, 27C
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.011
-
-
37C, pH 7.0
0.018
-
-
-
0.031
-
-
37C, pH 7.0
0.166
-
-
-
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
37
-
-
assay at
37
-
-
assay at
37
-
-
assay at
37
-
Q9UUB1
assay at
37
-
P61711
assay at
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.6
-
-
calculated from sequence
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
L0C9N6, -
high expression
Manually annotated by BRENDA team
L0C9N6, -
high expression in young leaf
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
constitutes less than 0.02% of the total chloroplast protein. The enzyme is exclusivelylocated in the chloroplast stroma
Manually annotated by BRENDA team
L0C9N6, -
sequence contains an N-terminal extension representing a plastid-targeting sequence
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Aquifex aeolicus (strain VF5)
Aquifex aeolicus (strain VF5)
Aquifex aeolicus (strain VF5)
Aquifex aeolicus (strain VF5)
Aquifex aeolicus (strain VF5)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Brucella abortus biovar 1 (strain 9-941)
Brucella abortus biovar 1 (strain 9-941)
Brucella abortus biovar 1 (strain 9-941)
Brucella abortus biovar 1 (strain 9-941)
Brucella abortus biovar 1 (strain 9-941)
Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094)
Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65)
Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958)
Mycobacterium leprae (strain Br4923)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Schizosaccharomyces pombe (strain 972 / ATCC 24843)
Schizosaccharomyces pombe (strain 972 / ATCC 24843)
Schizosaccharomyces pombe (strain 972 / ATCC 24843)
Schizosaccharomyces pombe (strain 972 / ATCC 24843)
Schizosaccharomyces pombe (strain 972 / ATCC 24843)
Schizosaccharomyces pombe (strain 972 / ATCC 24843)
Schizosaccharomyces pombe (strain 972 / ATCC 24843)
Schizosaccharomyces pombe (strain 972 / ATCC 24843)
Schizosaccharomyces pombe (strain 972 / ATCC 24843)
Schizosaccharomyces pombe (strain 972 / ATCC 24843)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
75300
-
-
isoform RibH1, light scattering experiments
80100
-
-
light scattering experiments, isoform RibH1
85500
-
-
isoform RibH1, light scattering experiments
87000
-
Q9UUB1
sedimentation equilibrium centrifugation
88000
-
-
sedimentation equilibrium experiments
90000
-
-
sedimentation equilibrium analysis
90000
-
P61711
gel filtration
158500
-
-
isoform RinH2, light scattering experiments
850000
-
-
gel filtration
973000
991000
-
sedimentaion equilibrium studies
977000
-
-
sedimentation equilibrium analysis
additional information
-
-
the protein is an icosahedral capsid of 60 subunits with a mass of about 1 MDa as shown by hydrodynamic studies and by electron microscopy. The lumazine synthase of Escherichia coli is not physically associated with another enzyme of the riboflavin pathway, and the core of the icosahedral capsid is empty
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
60-mer
-
60 * 15645, the enzyme can form capsids with icosahedral 532 symmetry consisting of 60 subunits, electrospray mass spectrometry; 60 * 16000, the enzyme can form capsids with icosahedral 532 symmetry consisting of 60 subunits, SDS-PAGE
60-mer
-
60 * 16156, calculated from sequence
60-mer
-
60 * 15500, subunit of mature enzyme, SDS-PAGE; 60 * 16534, subunit of mature enzyme, calculated from sequence; 60 * 16536, subunit of mature enzyme, electrospray ionization mass spectrometry
60-mer
-
the spherical protein consists of 60 identical subunits with strict icosahedral 532 symmetry
60-mer
O66529
sequence determinants responsible for the icosahedral quaternary structure
60-mer
-
sequence determinants responsible for the icosahedral quaternary structure
?
P61711
x * 18000, SDS-PAGE
?
-
x * 19000, calculated from sequence
?
P66038
x * 16008, calculated, x * 17000-18000, SDS-PAGE, x * 18100, MALDI-TOF
?
L0C9N6, -
x * 23230, calculated
decamer
-
10 * 17300, calculated, isoform RibH2
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
pentamer
-
5 * 16800, calculated, isoform RibH1
pentamer
-
5 * 17200, calculated, isoform RibH1
pentamer
Q9UUB1
5 * 17188, calculated from sequence; 5 * 17189, electrospray MS
pentamer
-
5 * 17599, calculated from sequence
pentamer
-
5 * 18600, calculated from sequence
pentamer
-
5 * 18598, calculated from sequence
pentamer
P61711
-
pentamer
Q9UVT8
-
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
additional information
P61711
Brucella spp. lumazine synthase arranges in icosahedric capsids similar to those formed by the lumazine synthases of other bacteria
additional information
-
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
P50856
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
Q8UG70
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
Q8YQ43
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
O66529
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
O80575
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
O28152
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
Q44681
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
Q9KCL4
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
Q9REF4
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
Q8K9A6, Q9ZNM0
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; 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
Q9PIB9
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
Q9A8J4, Q9A9S4
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; 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
Q9Z733
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
O84737
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
Q8KAW4
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
Q97LG8
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
Q8XMW9
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
O24753
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
Q8NQ53
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
Q9RXZ8
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
Q8RIR4
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
P45149
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
Q9HRM5
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
Q9ZN56
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
O24854
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
Q9CGU6
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
Q9UVT8
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; 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
Q8TYL5
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
Q8TPT7
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
Q8Q093
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
O27443
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
Q9CCP3
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
Q9XH13
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
P57869
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
Q01994, Q93E92
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; 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
P51963
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
Q9HWX5
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
Q8ZTE3
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
Q8Y1H8
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
Q53107
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
Q92NI1, Q92QU0
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; 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
Q9EWJ9
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
Q975M5
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
O68250
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
P73527
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
Q9X2E5
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
Q9KPU4
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
Q8PCM7
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
Q8PPD6
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
Q9PES4
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
Q8ZC41
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
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
proteolytic modification
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plant lumazine synthase is synthesized in the cytosol as a larger molecular weight precursor protein, which is post-translationally imported into chloroplasts where it is proteolytically cleaved to its mature size
proteolytic modification
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plant lumazine synthase is synthesized in the cytosol as a larger molecular weight precursor protein, which is post-translationally imported into chloroplasts where it is proteolytically cleaved to its mature size
additional information
Q9PLJ4
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
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
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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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
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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
-
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
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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%
-
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
P66038
crystals are grown at 18C 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
-
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
-
sitting-drop vapour diffusion method, crystallizes in space group C222(1). The crystals diffract to a resolution of 2.4 A
Q9UUB1
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
20
-
-
the higher molecular order of the decameric enzyme increases its stability at 20C compared with pentameric lumazine synthases
88
-
-
melting temperature. The loss of secondary structure is not recovered after slow cooling of the samples, indicating that an irreversible unfolding takes place under these conditions
120
-
-
melting temperature: 119.9C
ORGANIC SOLVENT
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
guanidine-HCl
-
produces a cooperative and reversible change in the tertiary structure reflected by a decrease in tryptophan fluorescence emission. In addition, guanidine-HCl incubation produces a complete loss of secondary structure of BLS as monitored by CD spectra
urea
-
8 M, the absence of structural changes indicates that the quaternary arrangement of the enzyme is very stable
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
recombinant
-
recombinant enzyme
-
overexpression of the RIB4 coding sequence in yeast cells under the control of the strong TEF1 promoter allowed ready purification of 6,7-dimethyl-8-ribityllumazine synthase to apparent homogeneity by a simple procedure
-
recombinant enzyme
Q9UUB1
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expression in Escherichia coli
-
expression in Escherichia coli
-
expression in Escherichia coli
-
expression of beta60 capsid
-
expression of beta60 capsid carying lumazine synthase activity
-
expression in Escherichia coli
-
expression in Escherichia coli
-
expression in Escherichia coli. The recombinant protein is soluble only under reducing conditions, but alkylation with iodoacetamide renders it soluble in non-reducing media
P61711
expression in Escherichia coli
-
expression in Escherichia coli; expression in Escherichia coli
-
expression in Escherichia coli
-
expression in Escherichia coli
-
expression in Escherichia coli
Q9UUB1
expression in Escherichia coli
-
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
enzyme is constitutively expressed, with the strongest expression levels observed during the last stage of fruit ripening and correlating with the highest level of riboflavin content
L0C9N6, -
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
A56S
-
kcat is 81.3% of wild-type value
D138A
-
kcat is 91.5% of wild-type value
D44G/C93S/C139S/T118A
-
mutant constructed to improve the overexpression and purification of the molecule as well as to obtain new crystal forms. Two cysteines are replaced to bypass misfolding problems and a charged surface residue is replaced to force different molecular packings. Mutant crystallizes in space group R3 and diffracts to 1.6 A resolution
E58Q
-
kcat is 70.2% of wild-type value
F113S
-
kcat is 6.8% of wild-type value
F22D
-
kcat is 14.5% of wild-type value
F22S
-
kcat is 47.2% of wild-type value
F22V
-
kcat is 26.4% of wild-type value
F22W
-
kcat is 43.8% of wild-type value
F57S
-
kcat is 43.8% of wild-type value
H88A
-
kcat is 12% of wild-type value
H88K
-
kcat is 39.5% of wild-type value
K131N
-
kcat is 9.7% of wild-type value
K131R
-
kcat is 29.8% of wild-type value
K135A
-
kcat is 21.9% of wild-type value
N23S
-
kcat is 21.9% of wild-type value
R127H
-
kcat is 69.7% of wild-type value
S142L
-
kcat is 62.3% of wild-type value
T80V
-
kcat is 55.1% of wild-type value
W22A
P61711, Q57DY1
single amino acid mutation located in the active site of the endogenous RibH2. Mutant lacks enzymatic activity but its stability and structure are unaltered
L119F
-
weakly binds to riboflavin
W27F
Q9UUB1
the replacement of tryptophan 27 by aliphatic amino acids substantially reduces the affinity of the enzyme for riboflavin and for the substrate, 5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
W27G
Q9UUB1
the replacement of tryptophan 27 by aliphatic amino acids substantially reduces the affinity of the enzyme for riboflavin and for the substrate, 5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
W27G
-
does not bind riboflavin
W27H
Q9UUB1
the replacement of tryptophan 27 by aliphatic amino acids substantially reduces the affinity of the enzyme for riboflavin and for the substrate, 5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
W27I
Q9UUB1
the replacement of tryptophan 27 by aliphatic amino acids substantially reduces the affinity of the enzyme for riboflavin and for the substrate, 5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
W27S
Q9UUB1
the replacement of tryptophan 27 by aliphatic amino acids substantially reduces the affinity of the enzyme for riboflavin and for the substrate, 5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
W27Y
Q9UUB1
the replacement of tryptophan 27 by aliphatic amino acids substantially reduces the affinity of the enzyme for riboflavin and for the substrate, 5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
W27Y
-
whereas the indole system of W27 forms a coplanar pi-complex with riboflavin, the corresponding phenyl ring in the W27Y mutant establishes only peripheral contact with the heterocyclic ring system of the bound riboflavin
W63Y
-
does not bind riboflavin
W63Y/L119F
-
does not bind riboflavin
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
medicine
-
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
medicine
P61711
this protein constitutes an interesting candidate for serological diagnosis and for the design of specific chemotherapeutic agents, and its polymeric characteristics could provide the basis for the development of an acellular vaccine
medicine
-
Brucella lumazine synthase can be used as both an antigen-carrier and as an adjuvant in the design of new oral subunit vaccines
medicine
-
lumazine synthase is a potent delivery system for the improvement of subunit vaccines
medicine
-
feasibility of using Brucella spp. lumazine synthase as a novel and effective delivery system to induce a protective immune response against rotavirus disease. In particular, previous results showing the plasticity of the Brucella spp. lumazine synthase scaffold for the production of polyvalent chimeras suggest that VP8 from different strains can be coupled to Brucella spp. lumazine synthase in order to elicit wide-protecting neutralizing antibodies against different field strains of rotavirus
medicine
-
the fact that the enzymes of the riboflavin biosynthesis pathway are not present in the human or animal host makes them potential targets for anti-infective agents