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Information on EC 2.5.1.78 - 6,7-dimethyl-8-ribityllumazine synthase and Organism(s) Bacillus subtilis and UniProt Accession P11998
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2.5.1.78 6,7-dimethyl-8-ribityllumazine synthaseIUBMB Comments
Involved in riboflavin biosynthesis.
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Word Map
- 2.5.1.78
- brucella
-
capsid
-
icosahedral
-
aquifex
- aeolicus
- brucellosis
- 4-phosphate
-
pentamer
- abortus
- 3,4-dihydroxy-2-butanone
-
5-amino-6-ribitylamino-2,41h,3h-pyrimidinedione
- medicine
-
guest
-
decameric
-
supercharged
-
homopentamer
-
nanocompartments
-
60-subunit
- biotechnology
- synthesis
- molecular biology
- analysis
- drug development
The taxonomic range for the selected organisms is: Bacillus subtilis
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
lumazine synthase, 6,7-dimethyl-8-ribityllumazine synthase, ribh2, ribh1, mj0303, ribh1 protein, dmrl synthase, 6,7-dimethyl-8-(d-ribityl)lumazine synthase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
lumazine synthase/riboflavin synthase complex
-
bifunctional enzyme complex
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
1-deoxy-L-glycero-tetrulose 4-phosphate + 5-amino-6-(D-ribitylamino)uracil = 6,7-dimethyl-8-(D-ribityl)lumazine + 2 H2O + phosphate
critical involvement of the active-site residues Phe22, His88 and Arg127 in substrate binding and catalysis
PATHWAY SOURCE
PATHWAYS
BRENDA
-
-, -, -
SYSTEMATIC NAME
IUBMB Comments
5-amino-6-(D-ribitylamino)uracil butanedionetransferase
Involved in riboflavin biosynthesis.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1-deoxy-L-glycero-tetrulose 4-phosphate + 5-amino-6-(D-ribitylamino)uracil
6,7-dimethyl-8-(D-ribityl)lumazine + 2 H2O + phosphate
-
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
-
-
-
?
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione + 3,4-dihydroxy-2-butanone 4-phosphate
6,7-dimethyl-8-ribityllumazine + 2 H2O + phosphate
-
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (3R)-3,4-dihydroxy-2-butanone 4-phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + 2 H2O + phosphate
-
-
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (3S)-3,4-dihydroxy-2-butanone
?
-
-
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + 5-nitro-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
?
-
-
-
-
?
additional information
?
-
critical involvement of the active-site residues Phe22, His88 and Arg127 in substrate binding and catalysis
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
-
-
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
-
penultimate step of riboflavin biosynthesis
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
-
lumazine synthase/riboflavin synthase complex, the beta subunit carries lumazine synthase activity. Product channeling for subsequent synthesis of riboflavin by riboflavin synthase present in the complex
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
-
the rate enhancement by the enzyme is predominantly achieved by establishing a favourable topological relation of the two substrates, whereas acid/base catalysis may play a secondary role
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1-deoxy-L-glycero-tetrulose 4-phosphate + 5-amino-6-(D-ribitylamino)uracil
6,7-dimethyl-8-(D-ribityl)lumazine + 2 H2O + phosphate
-
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
-
-
-
?
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione + 3,4-dihydroxy-2-butanone 4-phosphate
6,7-dimethyl-8-ribityllumazine + 2 H2O + phosphate
-
-
-
?
5-amino-6-(1-D-ribitylamino)pyrimidine-2,4(1H,3H)-dione + (S)-2-hydroxy-3-oxobutyl dihydrogen phosphate
6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O
-
penultimate step of riboflavin biosynthesis
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(1S)-1,2-dideoxy-1-fluoro-1-(5-nitro-2,6-dioxo-1,2,3,6-tetrahydropyrimidin-4-yl)-D-ribo-hexitol
-
-
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-dioxo-5-[[5-(phosphonooxy)pentanoyl]amino]-1,2,3,6-tetrahydropyrimidin-4-yl)amino]-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
3-(1,3,7,9-tetrahydro-9-D-ribityl-2,6,8-trioxopurin-7-yl)propane 1-phosphate
-
-
4-(1,3,7,9-tetrahydro-9-D-ribityl-2,6,8-trioxopurin-7-yl)butane 1-phosphate
-
-
4-(1,5,6,7-tetrahydro-6,7-dioxo-8-D-ribityllumazin-5-yl)butane 1-phosphate
-
-
4-[2,4,7-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
5-(1,3,7,9-tetrahydro-9-D-ribityl-2,6,8-trioxopurin-7-yl)-1,1-difluoropentane 1-phosphonate
-
-
5-(1,5,6,7-tetrahydro-6,7-dioxo-8-D-ribityllumazin-5-yl)pentane 1-phosphate
-
-
5-(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-(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-[[(2R,3R,4R)-2,3,4,5 tetrahydroxypentyl]sulfanyl]pyrimidine-2,4(1H,3H)-dione
-
inhibition of both lumazine synthase and riboflavin synthase
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
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)-dione-5-ylisobutyramide
-
partial inhibition, 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
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]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.005
5-nitro-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
native enzyme complex, pH 7.0, 37°C
0.0041
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
pH 7.0, 37°C, mutant enzyme T80V
0.0042
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
pH 7.0, 37°C, mutant enzyme A56S
0.00612
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
pH 7.0, 37°C, mutant enzyme F22W
0.00857
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
pH 7.0, 37°C, wild-type enzyme
0.01
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
pH 7.0, 37°C, mutant enzyme D138A
0.0107
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
pH 7.0, 37°C, mutant enzyme F22V
0.011
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
pH 7.0, 37°C, mutant enzyme S142L
0.0115
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
pH 7.0, 37°C, mutant enzyme K135A
0.0119
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
pH 7.0, 37°C, mutant enzyme N23S
0.0138
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
pH 7.0, 37°C, mutant enzyme K131R
0.0345
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
pH 7.0, 37°C, mutant enzyme F57S
0.0355
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
pH 7.0, 37°C, mutant enzyme K131N
0.056
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
pH 7.0, 37°C, mutant enzyme H88K
0.0849
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
pH 7.0, 37°C, mutant enzyme R127H
0.14
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
pH 7.0, 37°C, mutant enzyme F22S
0.147
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
pH 7.0, 37°C, mutant enzyme H88A
0.173
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
pH 7.0, 37°C, mutant enzyme E58Q
0.278
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
pH 7.0, 37°C, mutant enzyme F113S
0.72
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
pH 7.0, 37°C, mutant enzyme F22D
0.042
L-3,4-dihydroxybutan-2-one 4-phosphate
-
pH 7.0, 37°C, mutant enzyme H88K
0.042
L-3,4-dihydroxybutan-2-one 4-phosphate
-
pH 7.0, 37°C, mutant enzyme T80V
0.05
L-3,4-dihydroxybutan-2-one 4-phosphate
-
pH 7.0, 37°C, mutant enzyme K131R
0.05
L-3,4-dihydroxybutan-2-one 4-phosphate
-
pH 7.0, 37°C, phosphate buffer
0.0546
L-3,4-dihydroxybutan-2-one 4-phosphate
-
pH 7.0, 37°C, wild-type enzyme
0.0581
L-3,4-dihydroxybutan-2-one 4-phosphate
-
pH 7.0, 37°C, mutant enzyme N23S
0.0598
L-3,4-dihydroxybutan-2-one 4-phosphate
-
pH 7.0, 37°C, mutant enzyme F22W
0.06
L-3,4-dihydroxybutan-2-one 4-phosphate
-
pH 7.0, 37°C, mutant enzyme H88A
0.0636
L-3,4-dihydroxybutan-2-one 4-phosphate
-
pH 7.0, 37°C, mutant enzyme D138A
0.0665
L-3,4-dihydroxybutan-2-one 4-phosphate
-
pH 7.0, 37°C, mutant enzyme F113S
0.0702
L-3,4-dihydroxybutan-2-one 4-phosphate
-
pH 7.0, 37°C, mutant enzyme A56S
0.08
L-3,4-dihydroxybutan-2-one 4-phosphate
-
pH 7.0, 37°C, mutant enzyme F57S
0.0905
L-3,4-dihydroxybutan-2-one 4-phosphate
-
pH 7.0, 37°C, mutant enzyme S142L
0.124
L-3,4-dihydroxybutan-2-one 4-phosphate
-
pH 7.0, 37°C, mutant enzyme F22V
0.137
L-3,4-dihydroxybutan-2-one 4-phosphate
-
pH 7.0, 37°C, mutant enzyme F22S
0.146
L-3,4-dihydroxybutan-2-one 4-phosphate
-
pH 7.0, 37°C, mutant enzyme E58Q
0.167
L-3,4-dihydroxybutan-2-one 4-phosphate
-
pH 7.0, 37°C, mutant enzyme K135A
0.283
L-3,4-dihydroxybutan-2-one 4-phosphate
-
pH 7.0, 37°C, mutant enzyme K131N
0.675
L-3,4-dihydroxybutan-2-one 4-phosphate
-
pH 7.0, 37°C, mutant enzyme F22D
3.14
L-3,4-dihydroxybutan-2-one 4-phosphate
-
pH 7.0, 37°C, mutant enzyme R127H
additional information
additional information
steady-state kinetics, and kinetic modelling of the interaction of the single enzymes and identification of rate-limiting steps in the biosynthetic pathway, detailed overview
-
additional information
additional information
-
steady-state kinetics, and kinetic modelling of the interaction of the single enzymes and identification of rate-limiting steps in the biosynthetic pathway, detailed overview
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0022
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
pH 7.0, 37°C, mutant enzyme H88K
0.0038
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
pH 7.0, 37°C, mutant enzyme F113S
0.0054
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
pH 7.0, 37°C, mutant enzyme K131N
0.0067
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
pH 7.0, 37°C, mutant enzyme H88A
0.0081
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
pH 7.0, 37°C, mutant enzyme F22D
0.0122
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
pH 7.0, 37°C, mutant enzyme K135A
0.0122
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
pH 7.0, 37°C, mutant enzyme N23S
0.0147
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
pH 7.0, 37°C, mutant enzyme F22V
0.0166
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
pH 7.0, 37°C, mutant enzyme K131R
0.0244
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
pH 7.0, 37°C, mutant enzyme F22W
0.0244
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
pH 7.0, 37°C, mutant enzyme F57S
0.0263
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
pH 7.0, 37°C, mutant enzyme F22S
0.0307
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
pH 7.0, 37°C, mutant enzyme T80V
0.0347
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
pH 7.0, 37°C, mutant enzyme S142L
0.0389
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
pH 7.0, 37°C, mutant enzyme R127H
0.0391
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
pH 7.0, 37°C, mutant enzyme E58Q
0.0453
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
pH 7.0, 37°C, mutant enzyme A56S
0.051
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
pH 7.0, 37°C, mutant enzyme D138A
0.0557
5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
pH 7.0, 37°C, wild-type enzyme
0.056
5-nitro-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
native enzyme complex, pH 7.0, 37°C
0.076
5-nitro-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
-
hollow beta60 capsid, pH 7.0, 37°C
0.0022
L-3,4-dihydroxybutan-2-one 4-phosphate
-
pH 7.0, 37°C, mutant enzyme H88K
0.0038
L-3,4-dihydroxybutan-2-one 4-phosphate
-
pH 7.0, 37°C, mutant enzyme F113S
0.0054
L-3,4-dihydroxybutan-2-one 4-phosphate
-
pH 7.0, 37°C, mutant enzyme K131N
0.0067
L-3,4-dihydroxybutan-2-one 4-phosphate
-
pH 7.0, 37°C, mutant enzyme H88A
0.0081
L-3,4-dihydroxybutan-2-one 4-phosphate
-
pH 7.0, 37°C, mutant enzyme F22D
0.0122
L-3,4-dihydroxybutan-2-one 4-phosphate
-
pH 7.0, 37°C, mutant enzyme K135A
0.0122
L-3,4-dihydroxybutan-2-one 4-phosphate
-
pH 7.0, 37°C, mutant enzyme N23S
0.0147
L-3,4-dihydroxybutan-2-one 4-phosphate
-
pH 7.0, 37°C, mutant enzyme F22V
0.0166
L-3,4-dihydroxybutan-2-one 4-phosphate
-
pH 7.0, 37°C, mutant enzyme K131R
0.0244
L-3,4-dihydroxybutan-2-one 4-phosphate
-
pH 7.0, 37°C, mutant enzyme F22W
0.0244
L-3,4-dihydroxybutan-2-one 4-phosphate
-
pH 7.0, 37°C, mutant enzyme F57S
0.0263
L-3,4-dihydroxybutan-2-one 4-phosphate
-
pH 7.0, 37°C, mutant enzyme F22S
0.0307
L-3,4-dihydroxybutan-2-one 4-phosphate
-
pH 7.0, 37°C, mutant enzyme T80V
0.0347
L-3,4-dihydroxybutan-2-one 4-phosphate
-
pH 7.0, 37°C, mutant enzyme S142L
0.0389
L-3,4-dihydroxybutan-2-one 4-phosphate
-
pH 7.0, 37°C, mutant enzyme R127H
0.0391
L-3,4-dihydroxybutan-2-one 4-phosphate
-
pH 7.0, 37°C, mutant enzyme E58Q
0.0453
L-3,4-dihydroxybutan-2-one 4-phosphate
-
pH 7.0, 37°C, mutant enzyme A56S
0.051
L-3,4-dihydroxybutan-2-one 4-phosphate
-
pH 7.0, 37°C, mutant enzyme D138A
0.0557
L-3,4-dihydroxybutan-2-one 4-phosphate
-
pH 7.0, 37°C, wild-type enzyme
0.056
L-3,4-dihydroxybutan-2-one 4-phosphate
-
native enzyme complex, pH 7.0, 37°C
0.076
L-3,4-dihydroxybutan-2-one 4-phosphate
-
hollow beta60 capsid, pH 7.0, 37°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.221
(1S)-1,2-dideoxy-1-fluoro-1-(5-nitro-2,6-dioxo-1,2,3,6-tetrahydropyrimidin-4-yl)-D-ribo-hexitol
-
pH 7.0, 37°C, variable concentration of 5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
0.0078
1-deoxy-1-(2,4,6,7-tetraoxo-1,3,4,5,6,7-hexahydropteridin-8(2H)-yl)-D-ribitol
-
pH 7.0, 37°C
0.046
1-deoxy-1-(2,6,8-trioxo-1,2,3,6,7,8-hexahydro-9H-purin-9-yl)-D-ribitol
-
pH 7.0, 37°C, variable concentration of L-3,4-dihydroxybutan-2-one 4-phosphate
0.83
1-deoxy-1-[(2,6-dioxo-5-[[5-(phosphonooxy)pentanoyl]amino]-1,2,3,6-tetrahydropyrimidin-4-yl)amino]-D-ribitol
-
pH 7.0, 37°C, variable concentration of L-3,4-dihydroxybutan-2-one 4-phosphate
0.17
1-deoxy-1-[2,6,8-trioxo-7-[4-(phosphonooxy)butyl]-1,2,3,6,7,8-hexahydro-9H-purin-9-yl]-D-ribitol
-
pH 7.0, 37°C
0.27 - 0.852
1-deoxy-1-[2,6,8-trioxo-7-[5-(phosphonooxy)pentyl]-1,2,3,6,7,8-hexahydro-9H-purin-9-yl]-D-ribitol
0.0783 - 0.175
1-deoxy-1-[2,6,8-trioxo-7-[6-(phosphonooxy)hexyl]-1,2,3,6,7,8-hexahydro-9H-purin-9-yl]-D-ribitol
0.44
1-deoxy-1-[[2,6-dioxo-5-(4-phosphonobutyl)-1,2,3,6-tetrahydropyrimidin-4-yl]amino]-D-ribitol
-
pH 7.0, 37°C, variable concentration of L-3,4-dihydroxybutan-2-one 4-phosphate
0.18
1-deoxy-1-[[2,6-dioxo-5-(5-phosphonopentyl)-1,2,3,6-tetrahydropyrimidin-4-yl]amino]-D-ribitol
-
pH 7.0, 37°C, variable concentration of L-3,4-dihydroxybutan-2-one 4-phosphate
0.13
1-deoxy-1-[[2,6-dioxo-5-(6-phosphonohexyl)-1,2,3,6-tetrahydropyrimidin-4-yl]amino]-D-ribitol
-
pH 7.0, 37°C, variable concentration of L-3,4-dihydroxybutan-2-one 4-phosphate
0.18 - 0.492
1-[(5-amino-2,6-dioxo-1,2,3,6-tetrahydropyrimidin-4-yl)(methyl)amino]-1-deoxy-D-ribitol hydrochloride
0.0026
2,4-dioxo-6-[[(2R,3R,4R)-2,3,4,5-tetrahydroxypentyl]sulfanyl]-1,2,3,4-tetrahydropyrimidin-5-aminium chloride
-
pH 7.0, 27°C
0.0414
3-(1,3,7,9-tetrahydro-9-D-ribityl-2,6,8-trioxopurin-7-yl)propane 1-phosphate
-
pH 7.0, 37°C, variable concentration of 5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
0.168
4-(1,3,7,9-tetrahydro-9-D-ribityl-2,6,8-trioxopurin-7-yl)butane 1-phosphate
-
pH 7.0, 37°C, variable concentration of 5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
0.15
4-(1,5,6,7-tetrahydro-6,7-dioxo-8-D-ribityllumazin-5-yl)butane 1-phosphate
-
pH 7.0, 37°C
0.084
4-[2,4,7-trioxo-8-[(2S,3S,4R)-2,3,4,5-tetrahydroxypentyl]-1,2,3,4,7,8-hexahydropteridin-6-yl]butanoic acid
-
pH 7.5, 37°C, recombinant beta60 capsid
0.16
4-[2,4,7-trioxo-8-[(2S,3S,4R)-2,3,4,5-tetrahydroxypentyl]-1,2,3,4,7,8-hexahydropteridin-6-yl]butyl dihydrogen phosphate
-
pH 7.5, 37°C, recombinant beta60 capsid
0.12
4-[2,4,7-trioxo-8-[(2S,3S,4R)-2,3,4,5-tetrahydroxypentyl]-1,2,3,4,7,8-hexahydropteridin-6-yl]propyl dihydrogen phosphate
-
pH 7.5, 37°C, recombinant beta60 capsid
0.132
5-(1,3,7,9-tetrahydro-9-D-ribityl-2,6,8-trioxopurin-7-yl)-1,1-difluoropentane 1-phosphonate
-
pH 7.0, 37°C, variable concentration of 5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
0.027
5-(1,5,6,7-tetrahydro-6,7-dioxo-8-D-ribityllumazin-5-yl)pentane 1-phosphate
-
pH 7.0, 37°C
0.86
5-(4-phosphonobutyryl)amino-6-D-ribitylaminouracil
-
pH 7.5, 37°C, recombinant beta60 capsid
1
5-(5-phosphonopentyl)amino-6-D-ribitylaminouracil
-
pH 7.5, 37°C, recombinant beta60 capsid
0.83
5-(5-phosphonoxyvaleryl)amino-6-D-ribitylaminouracil
-
pH 7.5, 37°C, recombinant beta60 capsid
0.13
5-(hexyl 6-dihydrogen phosphate)-6-([(2S,3S,4R)-2,3,4,5-tetrahydroxypentyl]amino)pyrimidine-2,4(1H,3H)-dione
-
pH 7.5, 37°C, recombinant beta60 capsid
0.18
5-(pentyl 6-dihydrogen phosphate)-6-([(2S,3S,4R)-2,3,4,5-tetrahydroxypentyl]amino)pyrimidine-2,4(1H,3H)-dione
-
pH 7.5, 37°C, recombinant beta60 capsid
0.264
5-nitro-6-[(D-ribityl)methyl]pyrimidine-2,4-dione
-
pH 7.0, 37°C, variable concentration of 5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
0.026
5-nitro-6-[[(2R,3R,4R)-2,3,4,5 tetrahydroxypentyl]sulfanyl]pyrimidine-2,4(1H,3H)-dione
-
pH 7.0, 27°C
0.094
6-methyl-7-methylidene-8-[(2S,3S,4R)-2,3,4,5-tetrahydroxypentyl]-7,8-dihydropyrido[2,3-d]pyrimidine-2,4(1H,3H)-dione
-
pH 7.5, 37°C, recombinant beta60 capsid
0.0078
8-[[(2S,3S,4R)-2,3,4,5-tetrahydroxypentyl]amino]tetrahydropteridine-2,4,6,7(1H,3H)-tetrone
-
pH 7.0, 27°C
0.046
9-[(2S,3S,4R)-2,3,4,5-tetrahydroxypentyl]-7,9-dihydro-1H-purine-2,6,8(3H)-trione
-
pH 7.5, 37°C, recombinant beta60 capsid
0.607
ethyl [(2,4-dioxo-6-[[(2S,3S,4R)-2,3,4,5-tetrahydroxypentyl]amino]-1,2,3,4-tetrahydropyrimidin-5-yl)amino](oxo)acetate
-
pH 7.0, 27°C
0.27
1-deoxy-1-[2,6,8-trioxo-7-[5-(phosphonooxy)pentyl]-1,2,3,6,7,8-hexahydro-9H-purin-9-yl]-D-ribitol
-
pH 7.0, 37°C
0.271
1-deoxy-1-[2,6,8-trioxo-7-[5-(phosphonooxy)pentyl]-1,2,3,6,7,8-hexahydro-9H-purin-9-yl]-D-ribitol
-
pH 7.0, 37°C, variable concentration of 5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
0.852
1-deoxy-1-[2,6,8-trioxo-7-[5-(phosphonooxy)pentyl]-1,2,3,6,7,8-hexahydro-9H-purin-9-yl]-D-ribitol
-
pH 7.0, 37°C, variable concentration of L-3,4-dihydroxybutan-2-one 4-phosphate
0.0783
1-deoxy-1-[2,6,8-trioxo-7-[6-(phosphonooxy)hexyl]-1,2,3,6,7,8-hexahydro-9H-purin-9-yl]-D-ribitol
-
pH 7.0, 37°C, variable concentration of 5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
0.175
1-deoxy-1-[2,6,8-trioxo-7-[6-(phosphonooxy)hexyl]-1,2,3,6,7,8-hexahydro-9H-purin-9-yl]-D-ribitol
-
pH 7.0, 37°C, variable concentration of L-3,4-dihydroxybutan-2-one 4-phosphate
0.18
1-[(5-amino-2,6-dioxo-1,2,3,6-tetrahydropyrimidin-4-yl)(methyl)amino]-1-deoxy-D-ribitol hydrochloride
-
pH 7.0, 37°C, variable concentration of 5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione
0.492
1-[(5-amino-2,6-dioxo-1,2,3,6-tetrahydropyrimidin-4-yl)(methyl)amino]-1-deoxy-D-ribitol hydrochloride
-
pH 7.0, 37°C, variable concentration of L-3,4-dihydroxybutan-2-one 4-phosphate
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.02
N-6-(ribitylamino)pyrimidine-2,4(1H,3H)-dion-5-ylpropionamide
Bacillus subtilis
-
pH 7.0, 27°C
0.095
N-6-(ribitylamino)pyrimidine-2,4(1H,3H)-dione-5-ylisobutyramide
Bacillus subtilis
-
pH 7.0, 27°C
0.607
N-[2,4-dioxo-6-(ribitylamino)-1,2,3,4-tetrahydropyrimidin-5-yl]oxalamic acid ethyl ester
Bacillus subtilis
-
pH 7.0, 27°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
in Bacillaceae, lumazine synthase and riboflavin synthase form a structurally unique complex comprising an icosahedral shell of 60 lumazine synthase subunits and a core of three riboflavin synthase subunits, whereas many other bacteria have empty lumazine synthase capsids, fungi, Archaea and some eubacteria have pentameric lumazine synthases, and the riboflavin synthases of Archaea are paralogues of lumazine synthase. The quaternary structure of the icosahedral beta subunit capsids undergoes drastic changes, resulting in formation of large, quasi-spherical capsids
metabolism
physiological function
the enzyme is involved in the riboflavin biosynthesis pathway. Riboflavin or vitamin B2 is the precursor of the flavin cofactors flavin mononucleotide (FMN) and flavin adenine dinucleotide (FAD), and is used commercially as an animal feed supplement and as a food colorant (E101)
additional information
modelling of the lumazine synthase/riboflavin synthase complex
metabolism
the enzyme is involved in the riboflavin biosynthesis pathway. The RibA protein is rate limiting in the pathway, reductase activity of RibG and lumazine synthase (RibH) might be the next most limiting steps. Computational minimization of the enzyme concentrations of the pathway suggests the need for a greater RibH enzyme concentration (0.251 mM) compared with the other enzymes (RibG 0.188 mM, RibB 0.023 mM). Kinetic modelling of the interaction of the single enzymes and identification of rate-limiting steps in the biosynthetic pathway. The potential order of enzyme limitation under increasing RibA concentration is as follows: the reductase activity of RibG and the lumazine synthase (RibH) are rather more limiting than riboflavin synthase (RibB) and the deaminase activity of RibG
metabolism
the xylene ring of riboflavin (vitamin B2) is assembled from two molecules of 3,4-dihydroxy-2-butanone 4-phosphate by a mechanistically complex process that is jointly catalyzed by lumazine synthase and riboflavin synthase as part of the riboflavin pathway, overview
PDB
SCOP
CATH
UNIPROT
ORGANISM
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
60-mer
sequence determinants responsible for the icosahedral quaternary structure
pentamer
the lumazine protein folds into two closely similar domains
additional information
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
-
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
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
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
-
molecular modeling of enzyme with inhibitor 5-nitro-6-[[(2R,3R,4R)-2,3,4,5 tetrahydroxypentyl]sulfanyl]pyrimidine-2,4(1H,3H)-dione
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
additional information
-
the C-terminal tail of ribiflavin synthase can act as an encapsulation tag capable of targeting other proteins to the lumazine synthase capsid interior. Fusion of to either the last 11 or the last 32 amino acids of riboflavin synthase, yields variant GFP11 or GFP32, respectively. After purification, lumazine synthase capsids that have been coproduced in bacteria with GFP11 and GFP32 are 15- and 6fold more fluorescent, respectively. GFP11 is localized within the lumazine synthase capsid. Fusing the last 11 amino acids of riboflavin synthase to the C-terminus of the Abrin A chain also leads to its encapsulation by lumazine synthase at a level similar to that of GFP11. Mild changes in pH and buffer identity trigger dissociation of the GFP11 guest
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
Bacillus subtilis is used for riboflavin production, also involving the enzyme RibH
biotechnology
-
the C-terminal tail of ribiflavin synthase can act as an encapsulation tag capable of targeting other proteins to the lumazine synthase capsid interior. Fusion of to either the last 11 or the last 32 amino acids of riboflavin synthase, yields variant GFP11 or GFP32, respectively. After purification, lumazine synthase capsids that have been coproduced in bacteria with GFP11 and GFP32 are 15- and 6fold more fluorescent, respectively. GFP11 is localized within the lumazine synthase capsid. Fusing the last 11 amino acids of riboflavin synthase to the C-terminus of the Abrin A chain also leads to its encapsulation by lumazine synthase at a level similar to that of GFP11. Mild changes in pH and buffer identity trigger dissociation of the GFP11 guest
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kis, K.; Bacher, A.
Substrate channeling in the lumazine synthase/riboflavin synthase complex of Bacillus subtilis
J. Biol. Chem.
270
16788-16795
1995
Bacillus subtilis
Cushman, M.; Yang, D.; Gerhardt, S.; Huber, R.; Fischer, M.; Kis, K.; Bacher, A.
Design, synthesis, and evaluation of 6-carboxyalkyl and 6-phosphonoxyalkyl derivatives of 7-oxo-8-ribitylaminolumazines as inhibitors of riboflavin synthase and lumazine synthase
J. Org. Chem.
67
5807-5816
2002
Bacillus subtilis
Cushman, M.; Yang, D.; Mihalic, J.T.; Chen, J.; Gerhardt, S.; Huber, R.; Fischer, M.; Kis, K.; Bacher, A.
Incorporation of an amide into 5-phosphonoalkyl-6-D-ribitylaminopyrimidinedione lumazine synthase inhibitors results in an unexpected reversal of selectivity for riboflavin synthase vs lumazine synthase
J. Org. Chem.
67
6871-6877
2002
Bacillus subtilis
Rodriguez-Fernandez, L.; Lopez-Jaramillo, F.J.; Bacher, A.; Fischer, M.; Weinkauf, S.
Improvement of the quality of lumazine synthase crystals by protein engineering
Acta Crystallogr. Sect. F
64
625-628
2008
Bacillus subtilis (P11998), Bacillus subtilis
Talukdar, A.; Illarionov, B.; Bacher, A.; Fischer, M.; Cushman, M.
Synthesis and enzyme inhibitory activity of the s-nucleoside analogue of the ribitylaminopyrimidine substrate of lumazine synthase and product of riboflavin synthase
J. Org. Chem.
72
7167-7175
2007
Bacillus subtilis, Mycobacterium tuberculosis, Schizosaccharomyces pombe
Zhang, Y.; Illarionov, B.; Morgunova, E.; Jin, G.; Bacher, A.; Fischer, M.; Ladenstein, R.; Cushman, M.
A new series of N-[2,4-dioxo-6-d-ribitylamino-1,2,3,4-tetrahydropyrimidin-5-yl]oxalamic acid derivatives as inhibitors of lumazine synthase and riboflavin synthase: design, synthesis, biochemical evaluation, crystallography, and mechanistic implications
J. Org. Chem.
73
2715-2724
2008
Bacillus subtilis, Mycobacterium tuberculosis, Schizosaccharomyces pombe
Ritsert, K.; Huber, R.; Turk, D.; Ladenstein, R.; Schmidt-Bse, K.; Bacher, A.
Studies on the lumazine synthase/riboflavin synthase complex of Bacillus subtilis: crystal structure analysis of reconstituted, icosahedral beta-subunit capsids with bound substrate analogue inhibitor at 2.4 A resolution
J. Mol. Biol.
253
151-167
1995
Bacillus subtilis
Fischer, M.; Haase, I.; Kis, K.; Meining, W.; Ladenstein, R.; Cushman, M.; Schramek, N.; Huber, R.; Bacher, A.
Enzyme catalysis via control of activation entropy: site-directed mutagenesis of 6,7-dimethyl-8-ribityllumazine synthase
J. Mol. Biol.
326
783-793
2003
Bacillus subtilis
Cushman, M.; Sambaiah, T.; Jin, G.; Illarionov, B.; Fischer, M.; Bacher, A.
Design, synthesis, and evaluation of 9-D-ribitylamino-1,3,7,9-tetrahydro-2,6,8-purinetriones bearing alkyl phosphate and alpha,alpha-difluorophosphonate substituents as inhibitors of riboflavin synthase and lumazine synthase
J. Org. Chem.
69
601-612
2004
Bacillus subtilis, Mycobacterium tuberculosis
Chen, J.; Sambaiah, T.; Illarionov, B.; Fischer, M.; Bacher, A.; Cushman, M.
Design, synthesis, and evaluation of acyclic C-nucleoside and N-methylated derivatives of the ribitylaminopyrimidine substrate of lumazine synthase as potential enzyme inhibitors and mechanistic probes
J. Org. Chem.
69
6996-7003
2004
Bacillus subtilis, Mycobacterium tuberculosis
Cushman, M.; Jin, G.; Sambaiah, T.; Illarionov, B.; Fischer, M.; Ladenstein, R.; Bacher, A.
Design, synthesis, and biochemical evaluation of 1,5,6,7-tetrahydro-6,7-dioxo-9-D-ribitylaminolumazines bearing alkyl phosphate substituents as inhibitors of lumazine synthase and riboflavin synthase
J. Org. Chem.
70
8162-8170
2005
Bacillus subtilis, Mycobacterium tuberculosis
Fornasari, M.S.; Laplagne, D.A.; Frankel, N.; Cauerhff, A.A.; Goldbaum, F.A.; Echave, J.
Sequence determinants of quaternary structure in lumazine synthase
Mol. Biol. Evol.
21
97-107
2003
Spinacia oleracea, Corynebacterium ammoniagenes (O24753), Helicobacter pylori (O24854), Methanothermobacter thermautotrophicus (O27443), Archaeoglobus fulgidus (O28152), Aquifex aeolicus (O66529), Sulfurospirillum multivorans (O68250), Arabidopsis thaliana (O80575), Chlamydia trachomatis (O84737), Bacillus subtilis (P11998), Haemophilus influenzae (P45149), Actinobacillus pleuropneumoniae (P50856), Saccharomyces cerevisiae (P50861), Photobacterium phosphoreum (P51963), Pasteurella multocida (P57869), Brucella abortus (P61711), Synechocystis sp. (P73527), Photobacterium leiognathi (Q01994), Photobacterium leiognathi (Q93E92), Bacillus amyloliquefaciens (Q44681), Rhodococcus erythropolis (Q53107), Methanocaldococcus jannaschii (Q57751), Buchnera aphidicola (Q8K9A6), Buchnera aphidicola (Q9ZNM0), Chlorobaculum tepidum (Q8KAW4), Corynebacterium glutamicum (Q8NQ53), Xanthomonas campestris (Q8PCM7), Xanthomonas citri (Q8PPD6), Methanosarcina mazei (Q8Q093), Fusobacterium nucleatum (Q8RIR4), Methanosarcina acetivorans (Q8TPT7), Methanopyrus kandleri (Q8TYL5), Agrobacterium tumefaciens (Q8UG70), Clostridium perfringens (Q8XMW9), Ralstonia solanacearum (Q8Y1H8), Anabaena sp. (Q8YQ43), Yersinia pestis (Q8ZC41), Pyrobaculum aerophilum (Q8ZTE3), Sinorhizobium meliloti (Q92NI1), Sinorhizobium meliloti (Q92QU0), Sulfurisphaera tokodaii (Q975M5), Clostridium acetobutylicum (Q97LG8), Mesorhizobium loti (Q983B0), Mesorhizobium loti (Q986N2), Caulobacter vibrioides (Q9A8J4), Caulobacter vibrioides (Q9A9S4), Mycobacterium leprae (Q9CCP3), Lactococcus lactis subsp. lactis (Q9CGU6), Streptomyces coelicolor (Q9EWJ9), Halobacterium salinarum (Q9HRM5), Pseudomonas aeruginosa (Q9HWX5), Halalkalibacterium halodurans (Q9KCL4), Vibrio cholerae (Q9KPU4), Xylella fastidiosa (Q9PES4), Campylobacter jejuni (Q9PIB9), Chlamydia muridarum (Q9PLJ4), Bartonella henselae (Q9REF4), Deinococcus radiodurans (Q9RXZ8), Schizosaccharomyces pombe (Q9UUB1), Pyricularia grisea (Q9UVT8), Thermotoga maritima (Q9X2E5), Nicotiana tabacum (Q9XH13), Chlamydia pneumoniae (Q9Z733), Helicobacter pylori J99 (Q9ZN56), Agrobacterium tumefaciens C58 / ATCC 33970 (Q8UG70)
Talukdar, A.; Zhao, Y.; Lv, W.; Bacher, A.; Illarionov, B.; Fischer, M.; Cushman, M.
O-Nucleoside, S-nucleoside, and N-nucleoside probes of lumazine synthase and riboflavin synthase
J. Org. Chem.
77
6239-6261
2012
Bacillus subtilis, Mycobacterium tuberculosis, Schizosaccharomyces pombe (Q9UUB1)
Birkenmeier, M.; Neumann, S.; Roeder, T.
Kinetic modeling of riboflavin biosynthesis in Bacillus subtilis under production conditions
Biotechnol. Lett.
36
919-928
2014
Bacillus subtilis (P11998), Bacillus subtilis
Ladenstein, R.; Fischer, M.; Bacher, A.
The lumazine synthase/riboflavin synthase complex: shapes and functions of a highly variable enzyme system
FEBS J.
280
2537-2563
2013
Aquifex aeolicus (O66529), Bacillus subtilis (P11998), Saccharomyces cerevisiae (P50861), Brucella abortus (Q2YKV1), Brucella abortus (Q2YNC6)
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