Information on EC 2.5.1.9 - riboflavin synthase

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

EC NUMBER
COMMENTARY hide
2.5.1.9
-
RECOMMENDED NAME
GeneOntology No.
riboflavin synthase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2 6,7-dimethyl-8-(1-D-ribityl)lumazine = riboflavin + 4-(1-D-ribitylamino)-5-amino-2,6-dihydroxypyrimidine
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dismutation
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Biosynthesis of secondary metabolites
-
-
flavin biosynthesis
-
-
flavin biosynthesis I (bacteria and plants)
-
-
flavin biosynthesis II (archaea)
-
-
flavin biosynthesis III (fungi)
-
-
Metabolic pathways
-
-
Riboflavin metabolism
-
-
SYSTEMATIC NAME
IUBMB Comments
6,7-dimethyl-8-(1-D-ribityl)lumazine:6,7-dimethyl-8-(1-D-ribityl)lumazine 2,3-butanediyltransferase
A flavoprotein (riboflavin).
CAS REGISTRY NUMBER
COMMENTARY hide
9075-82-5
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
contains heavy and light form of the enzyme
-
-
Manually annotated by BRENDA team
contains heavy and light form of the enzyme
-
-
Manually annotated by BRENDA team
strain AG33
-
-
Manually annotated by BRENDA team
strain ATCC 8005
-
-
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
Methanothermobacter thermautotrophicum
Methanothermobacter thermautotrophicum Marburg
Marburg strain
SwissProt
Manually annotated by BRENDA team
bitter melon
UniProt
Manually annotated by BRENDA team
contains heavy and light form of the enzyme
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
no activity in Homo sapiens
-
-
-
Manually annotated by BRENDA team
contains heavy and light form of the enzyme
-
-
Manually annotated by BRENDA team
Pseudomonas iodinum
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
spinach
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2 6,7-dimethyl-8-ribityllumazine
riboflavin + 5-amino-6-ribitylamino-2,4(1H,3H)-pyrimidine-dione
show the reaction diagram
6,7-dimethyl-8-(1-D-ribityl)lumazine
riboflavin + 4-(1-D-ribitylamino)-5-amino-2,6-dihydroxypyrimidine
show the reaction diagram
6,7-dimethyl-8-(1-D-ribityl)lumazine
riboflavin + 5-amino-6-ribitylamino-2,4-(1H,3H)-pyrimidinedione
show the reaction diagram
6,7-dimethyl-8-ribityllumazine + 6,7-dimethyl-8-ribityllumazine
riboflavin + 4-(1'-D-ribitylamino)-5-amino-2,6-dihydroxypyrimidine
show the reaction diagram
6,7-dimethyl-8-ribityllumazine + 6,7-dimethyl-8-ribityllumazine
riboflavin + a compound related to 4-ribitylamino-2,5,6-trihydroxypyrimidine
show the reaction diagram
6,7-dimethyl-8-[1'-(5'-deoxy-D-ribityl)]lumazine + 6,7-dimethyl-8-[1'-(5'-deoxy-D-ribityl)]lumazine
5'-deoxyriboflavin + ?
show the reaction diagram
-
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
6,7-dimethyl-8-(1-D-ribityl)lumazine
riboflavin + 4-(1-D-ribitylamino)-5-amino-2,6-dihydroxypyrimidine
show the reaction diagram
6,7-dimethyl-8-(1-D-ribityl)lumazine
riboflavin + 5-amino-6-ribitylamino-2,4-(1H,3H)-pyrimidinedione
show the reaction diagram
6,7-dimethyl-8-ribityllumazine + 6,7-dimethyl-8-ribityllumazine
riboflavin + 4-(1'-D-ribitylamino)-5-amino-2,6-dihydroxypyrimidine
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
no cofactor requirement
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mn2+
-
preferred cation; preferred cation
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1-deoxy-1-[2,6,8-trioxo-7-[4-(phosphonooxy)butyl]-1,2,3,6,7,8-hexahydro-9H-purin-9-yl]-D-ribitol
2,4-dioxo-6-[(3S,4S,5R)-3,4,5,6-tetrahydroxyhexyl]-1,2,3,4-tetrahydropyrimidin-5-aminium chloride
2,4-dioxo-6-[[(2R,3R,4R)-2,3,4,5-tetrahydroxypentyl]sulfanyl]-1,2,3,4-tetrahydropyrimidin-5-aminium chloride
2-Amino-4,6-dihydroxy-8-D-ribityl-7-pteridinone
-
-
2-chloro-N-(2,4-dioxo-6-((2S,3S,4R)-2,3,4,5-tetrahydroxypentylamino)-1,2,3,4-tetrahydropyrimidin-5-yl)acetamide
2-chloro-N-(2,4-dioxo-6-((2S,3S,4R)-2,3,4,5-tetrahydroxypentylamino)-1,2,3,4-tetrahydropyrimidin-5-yl)propanamide
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
-
comparison with inhibition of Bacillus subtilis lumazine 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
-
comparison with inhibition of Bacillus subtilis lumazine 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
-
competitive, comparison with inhibition of Bacillus subtilis lumazine synthase
5,5'-dithiobis(2-nitrobenzoate)
-
-
5,6,7,8-Tetrahydro-9-(1'-D-ribityl)isoalloxazine
-
-
5-(4-phosphonobutyryl)amino-6-D-ribitylaminouracil
-
comparison with inhibition of Bacillus subtilis luminazine synthase/riboflavin synthase
5-(4-phosphonopentyryl)amino-6-D-ribitylaminouracil
-
comparison with inhibition of Bacillus subtilis luminazine synthase/riboflavin synthase
5-(5-phosphonoxyvaleryl)amino-6-D-ribitylaminouracil
-
mixed inhibition, comparison with inhibition of Bacillus subtilis luminazine synthase/riboflavin synthase
5-(hexyl 6-dihydrogen phosphate)-6-([(2S,3S,4R)-2,3,4,5-tetrahydroxypentyl]amino)pyrimidine-2,4(1H,3H)-dione
5-(pentyl 6-dihydrogen phosphate)-6-([(2S,3S,4R)-2,3,4,5-tetrahydroxypentyl]amino)pyrimidine-2,4(1H,3H)-dione
-
comparison with inhibition of Bacillus subtilis lumazine synthase
5-amino-6-((2R,3R,4S)-2,3,4,5-tetrahydroxypentyloxy)-pyrimidine-2,4(1H,3H)-dione
5-amino-6-[[(2R,3R,4R)-2,3,4,5-tetrahydroxypentyl]sulfanyl]pyrimidine-2,4(1H,3H)-dione
5-nitro-6-[(3S,4S,5R)-3,4,5,6-tetrahydroxyhexyl]pyrimidine-2,4(1H,3H)-dione
5-nitro-6-[[(2R,3R,4R)-2,3,4,5 tetrahydroxypentyl]sulfanyl]pyrimidine-2,4(1H,3H)-dione
5-nitro-6-[[(2R,3R,4R)-2,3,4,5-tetrahydroxypentyl]sulfanyl]pyrimidine-2,4(1H,3H)-dione
5-nitro-6-[[(2S,3R,4R)-2,3,4,5-tetrahydroxypentyl]oxy]pyrimidine-2,4(1H,3H)-dione
5-nitro-6-[[(2S,3S,4R)-2,3,4,5-tetrahydroxypentyl]amino]pyrimidine-2,4(1H,3H)-dione
6,7-dihydroxy-8-ribityllumazine
-
-
6,7-dimethyl-8-(1'-D-xylityl)lumazine
-
-
6-Methyl-7-hydroxy-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
-
competitive, comparison with inhibition of Bacillus subtilis lumazine synthase
7-hydroxy-6-(2-carboxyethyl)-8-(1-D-ribityl)lumazine
-
-
7-hydroxy-6-(D-1,2-dihydroxyethyl)-8-(1-D-ribityl)lumazine
-
-
7-Hydroxy-6-(L-1,2-dihydroxyethyl)-8-(1-D-ribityl)lumazine
-
i.e. photolumazine A
7-hydroxy-6-(p-hydroxyphenyl)-8-(1-D-ribityl)lumazine
-
-
-
7-Hydroxy-6-hydroxymethyl-8-(1-D-ribityl)lumazine
-
photolumazine B
7-hydroxy-7-methyl-8-((2S,3S,4R)-2,3,4,5-tetrahydroxypentyl)-7,8-dihydropteridin-2,4,6(1H,3H,5H)-trione
7-Hydroxy-8-(1-D-ribityl)lumazine
-
i.e. photolumazine
8-[(2S,3S,4R)-2,3,4,5-tetrahydroxypentyl]-5,8-dihydropteridine-2,4,6,7(1H,3H)-tetrone
9-[(2S,3S,4R)-2,3,4,5-tetrahydroxypentyl]-7,9-dihydro-1H-purine-2,6,8(3H)-trione
Avidin
-
moderately, no prevention by biotin
-
ethyl 2-(2,4-dioxo-6-((2S,3R,4R)-2,3,4,5-tetrahydroxypentyloxy)-1,2,3,4-tetrahydropyrimidin-5-ylamino)-2-oxoacetate
ethyl [(2,4-dioxo-6-[[(2S,3S,4R)-2,3,4,5-tetrahydroxypentyl]amino]-1,2,3,4-tetrahydropyrimidin-5-yl)amino](oxo)acetate
ethyl [(6-chloro-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)amino](oxo)acetate
methyl 2-(2,4-dioxo-6-((2S,3R,4R)-2,3,4,5-tetrahydroxypentyloxy)-1,2,3,4-tetrahydropyrimidin-5-ylamino)-2-oxoacetate
N-(2,4-dioxo-6-((2R,3R,4R)-2,3,4,5-tetrahydroxypentylthio)-1,2,3,4-tetrahydropyrimidin-5-yl)methacrylamide
N-(2,4-dioxo-6-((2R,3R,4R)-2,3,4,5-tetrahydroxypentylthio)-1,2,3,4-tetrahydropyrimidin-5-yl)propionamide
N-(2,4-dioxo-6-((2S,3R,4R)-2,3,4,5-tetrahydroxypentyloxy)-1,2,3,4-tetrahydropyrimidin-5-yl)isobutyramide
N-(2,4-dioxo-6-((2S,3R,4R)-2,3,4,5-tetrahydroxypentyloxy)-1,2,3,4-tetrahydropyrimidin-5-yl)methacrylamide
N-(2,4-dioxo-6-((2S,3R,4R)-2,3,4,5-tetrahydroxypentyloxy)-1,2,3,4-tetrahydropyrimidin-5-yl)propionamide
N-(2,4-dioxo-6-((2S,3S,4R)-2,3,4,5-tetrahydroxypentylamino)-1,2,3,4-tetrahydropyrimidin-5-yl)-3,3,3-trifluoropropanamide
N-(2,4-dioxo-6-[[(2S,3S,4R)-2,3,4,5-tetrahydroxypentyl]amino]-1,2,3,4-tetrahydropyrimidin-5-yl)-2-methylpropanamide
N-(2,4-dioxo-6-[[(2S,3S,4R)-2,3,4,5-tetrahydroxypentyl]amino]-1,2,3,4-tetrahydropyrimidin-5-yl)propanamide
N-(6-chloro-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)-methacrylamide
N-(6-chloro-2,4-dioxo-1,2,3,4-tetrahydropyrimidin-5-yl)propanamide
N-6-(ribitylamino)pyrimidine-2,4(1H,3H)-dion-5-ylpropionamide
-
uncompetitive
N-6-(ribitylamino)pyrimidine-2,4(1H,3H)-dione-5-ylisobutyramide
-
uncompetitive
N-[2,4-dioxo-6-((2S,3S,4R)-2,3,4,5-tetrahydroxypentylamino]-1,2,3,4-tetrahydropyrimidin-5-yl)methacrylamide
N-[2,4-dioxo-6-(ribitylamino)-1,2,3,4-tetrahydropyrimidin-5-yl]oxalamic acid ethyl ester
-
mixed type inhibition
p-chloromercuribenzenesulfonate
-
reversible by cysteine or 2-mercaptoethanol
p-chloromercuribenzoate
riboflavin
[3-(4-chlorophenyl)-5-hydroxy-5-(trifluoromethyl)-4,5-dihydro-1H-pyrazol-1-yl](m-tolyl)methanone
[3-(4-chlorophenyl)-5-hydroxy-5-(trifluoromethyl)-4,5-dihydro-1H-pyrazol-1-yl](o-tolyl)methanone
[3-(4-chlorophenyl)-5-hydroxy-5-(trifluoromethyl)-4,5-dihydro-1H-pyrazol-1-yl](p-tolyl)methanone
[5-(4-chlorophenyl)-5-hydroxy-3-(trifluoromethyl)-4,5-dihydro-1H-pyrazol-1-yl](m-tolyl)methanone
[5-(4-chlorophenyl)-5-hydroxy-3-(trifluoromethyl)-4,5-dihydro-1H-pyrazol-1-yl](o-tolyl)methanone
[5-(4-chlorophenyl)-5-hydroxy-3-(trifluoromethyl)-4,5-dihydro-1H-pyrazol-1-yl](p-tolyl)methanone
additional information
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2,3-dimercapto-1-propanol
2-mercaptoethanol
diacetyl
-
activates
N-acetylcysteine
additional information
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.01 - 0.13
6,7-dimethyl-8-(1'-D-ribityl)lumazine
0.0057
6,7-dimethyl-8-(1-D-ribityl)lumazine
pH 7.2, 37C, recombinant enzyme
additional information
additional information
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.2 - 2
6,7-dimethyl-8-(1'-D-ribityl)lumazine
0.001 - 0.267
6,7-dimethyl-8-(1-D-ribityl)lumazine
0.00833 - 0.019
6,7-dimethyl-8-ribityllumazine
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.332
1-deoxy-1-[2,6,8-trioxo-7-[4-(phosphonooxy)butyl]-1,2,3,6,7,8-hexahydro-9H-purin-9-yl]-D-ribitol
-
in 100 mM Tris-HCl, pH 7.0, 100 mM NaCl, 2% (v/v) DMSO, 5 mM dithiothreitol, at 27C
0.0025 - 0.047
2,4-dioxo-6-[[(2R,3R,4R)-2,3,4,5-tetrahydroxypentyl]sulfanyl]-1,2,3,4-tetrahydropyrimidin-5-aminium chloride
0.314
2-chloro-N-(2,4-dioxo-6-((2S,3S,4R)-2,3,4,5-tetrahydroxypentylamino)-1,2,3,4-tetrahydropyrimidin-5-yl)propanamide
-
in 100 mM Tris-HCl, pH 7.0, 100 mM NaCl, 2% (v/v) DMSO, 5 mM dithiothreitol, at 27C
0.02
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
0.15
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
1.6
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
0.16
5-(4-phosphonobutyryl)amino-6-D-ribitylaminouracil
-
pH 7.5, 37C
0.0068
5-(4-phosphonopentyryl)amino-6-D-ribitylaminouracil
-
pH 7.5, 37C
0.19
5-(5-phosphonoxyvaleryl)amino-6-D-ribitylaminouracil
-
pH 7.5, 37C
1
5-(hexyl 6-dihydrogen phosphate)-6-([(2S,3S,4R)-2,3,4,5-tetrahydroxypentyl]amino)pyrimidine-2,4(1H,3H)-dione
0.0025 - 0.047
5-amino-6-[[(2R,3R,4R)-2,3,4,5-tetrahydroxypentyl]sulfanyl]pyrimidine-2,4(1H,3H)-dione
0.0084 - 0.037
5-nitro-6-[(3S,4S,5R)-3,4,5,6-tetrahydroxyhexyl]pyrimidine-2,4(1H,3H)-dione
0.00056 - 0.0027
5-nitro-6-[[(2R,3R,4R)-2,3,4,5 tetrahydroxypentyl]sulfanyl]pyrimidine-2,4(1H,3H)-dione
0.0027
5-nitro-6-[[(2R,3R,4R)-2,3,4,5-tetrahydroxypentyl]sulfanyl]pyrimidine-2,4(1H,3H)-dione
-
in 100 mM Tris-HCl, pH 7.0, 100 mM NaCl, 2% (v/v) DMSO, 5 mM dithiothreitol, at 27C
0.036 - 0.038
5-nitro-6-[[(2S,3R,4R)-2,3,4,5-tetrahydroxypentyl]oxy]pyrimidine-2,4(1H,3H)-dione
0.0042 - 0.008
5-nitro-6-[[(2S,3S,4R)-2,3,4,5-tetrahydroxypentyl]amino]pyrimidine-2,4(1H,3H)-dione
0.0029 - 0.18
6-Methyl-7-hydroxy-8-ribityllumazine
0.65
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
0.027
7-hydroxy-6-(2-carboxyethyl)-8-(1-D-ribityl)lumazine
-
-
0.017
7-hydroxy-6-(D-1,2-dihydroxyethyl)-8-(1-D-ribityl)lumazine
0.028
7-hydroxy-6-(p-hydroxyphenyl)-8-(1-D-ribityl)lumazine
-
-
-
0.003
7-Hydroxy-6-hydroxymethyl-8-(1-D-ribityl)lumazine
-
-
0.00074
7-hydroxy-7-methyl-8-((2S,3S,4R)-2,3,4,5-tetrahydroxypentyl)-7,8-dihydropteridin-2,4,6(1H,3H,5H)-trione
-
in 100 mM Tris-HCl, pH 7.0, 100 mM NaCl, 2% (v/v) DMSO, 5 mM dithiothreitol, at 27C
0.011
7-Hydroxy-8-(1-D-ribityl)lumazine
-
-
0.0000062
8-[(2S,3S,4R)-2,3,4,5-tetrahydroxypentyl]-5,8-dihydropteridine-2,4,6,7(1H,3H)-tetrone
-
in 100 mM Tris-HCl, pH 7.0, 100 mM NaCl, 2% (v/v) DMSO, 5 mM dithiothreitol, at 27C
0.00061
9-[(2S,3S,4R)-2,3,4,5-tetrahydroxypentyl]-7,9-dihydro-1H-purine-2,6,8(3H)-trione
0.0000013
ethyl [(2,4-dioxo-6-[[(2S,3S,4R)-2,3,4,5-tetrahydroxypentyl]amino]-1,2,3,4-tetrahydropyrimidin-5-yl)amino](oxo)acetate
-
in 100 mM Tris-HCl, pH 7.0, 100 mM NaCl, 2% (v/v) DMSO, 5 mM dithiothreitol, at 27C
0.052
N-[2,4-dioxo-6-((2S,3S,4R)-2,3,4,5-tetrahydroxypentylamino]-1,2,3,4-tetrahydropyrimidin-5-yl)methacrylamide
-
in 100 mM Tris-HCl, pH 7.0, 100 mM NaCl, 2% (v/v) DMSO, 5 mM dithiothreitol, at 27C
0.014 - 0.106
[3-(4-chlorophenyl)-5-hydroxy-5-(trifluoromethyl)-4,5-dihydro-1H-pyrazol-1-yl](m-tolyl)methanone
0.0087 - 0.036
[3-(4-chlorophenyl)-5-hydroxy-5-(trifluoromethyl)-4,5-dihydro-1H-pyrazol-1-yl](o-tolyl)methanone
0.01 - 0.135
[3-(4-chlorophenyl)-5-hydroxy-5-(trifluoromethyl)-4,5-dihydro-1H-pyrazol-1-yl](p-tolyl)methanone
0.02 - 0.05
[5-(4-chlorophenyl)-5-hydroxy-3-(trifluoromethyl)-4,5-dihydro-1H-pyrazol-1-yl](m-tolyl)methanone
0.0067 - 0.312
[5-(4-chlorophenyl)-5-hydroxy-3-(trifluoromethyl)-4,5-dihydro-1H-pyrazol-1-yl](o-tolyl)methanone
0.01 - 0.104
[5-(4-chlorophenyl)-5-hydroxy-3-(trifluoromethyl)-4,5-dihydro-1H-pyrazol-1-yl](p-tolyl)methanone
additional information
additional information
-
inhibition kinetics, recombinant enzyme
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0000013
N-[2,4-dioxo-6-(ribitylamino)-1,2,3,4-tetrahydropyrimidin-5-yl]oxalamic acid ethyl ester
Escherichia coli
-
pH 7.0, 27C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00025
-
partially purified enzyme
0.0014
-
partially purified enzyme
0.002
-
purified recombinant enzyme, in absence of divalent cations; purified recombinant enzyme, in absence of divalent cations
0.021
-
with substrate compound Q, a dimer of the pentameric reaction intermediate
0.024
-
purified recombinant enzyme, in presence of divalent cations; purified recombinant enzyme, in presence of divalent cations
0.032
Methanothermobacter thermautotrophicum
65C; purified recombinant enzyme
0.033
-
heavy enzyme
0.045
Methanothermobacter thermautotrophicum
65C; purified enzyme
0.052
-
purified enzyme
0.16
-
purified enzyme
0.266
-
purified enzyme
0.5
-
light enzyme
0.833
-
light enzyme
1.2 - 2.8
-
partially purified enzyme
27
purified recombinant mutant C48S
158
purified recombinant wild-type enzyme
179
purified recombinant mutant S146C
183
purified recombinant mutant S146A
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.3
-
assay at
7.4
-
light enzyme, the pH-optimum of the heavy enzyme is similar, detailed measurement is not possible because of instability at elevated pH
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.4 - 8.8
-
about 50% of activity maximum at pH 5.4 and 8.8
5.8 - 8.4
-
about 50% of activity maximum at pH 5.8 and 8.4
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50 - 95
-
50C: about 10% of activity maximum, 80C: about 30% of activity maximum, 95C: activity maximum
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
high expression
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Schizosaccharomyces pombe (strain 972 / ATCC 24843)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
67500
-
recombinant enzyme expressed from synthetic gene, sedimentation equilibrium centrifugation and gel filtration
70000 - 80000
-
analytical ultracentrifugation
88300
-
sedimentation equilibrium centrifugation, recombinant enzyme; sedimentation equilibrium centrifugation, recombinant enzyme
100000
345000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pentamer
polymer
additional information
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
detailed structure determination and analysis of enzyme complexed with heavy atoms, three-dimensional structure model
-
from 1.3 M sodium/potassium phosphate, pH 8.7, 0.35 mM 5-nitroso-6-(1'-D-ribitylamino)-2,4(1H,3H)-pyrimidinedione, X-ray structure determination and analysis
-
large crystals by vapour diffusion method, initial solution: 0.7 M sodium/potassium phosphate, pH 8.7, 0.3 mM 5-nitroso-6-ribitylamino-2,4(1H,3H)-pyrimidinedione, protein 2 mg/ml, reservoir solution: 1.3 M sodium/potassium phosphate, pH 8.7, X-ray structure determination and analysis
-
modeling for the binding of two molecules of inhibitor 5-(4-phosphonobutyryl)amino-6-D-ribitylaminouracil in the active site
-
molecular modeling of inhibitors to the active site
-
purified recombinant homodimeric N-terminal enzyme domain in complex with riboflavin, 7 mg/ml protein in 70 mM sodium potassium phosphate, pH 7.0, and 100 mM sodium chloride, X-ray diffraction structure determination and analysis at 2.6 A resolution, molecular modeling
-
structure determination by multiwavelength anomalous diffraction method, modeling
-
crystals of wild-type enzyme are grown at 18C using the sitting drop vapor diffusion method by mixing equal amounts of protein (6 mg/ml) in 100 mM potassium phosphate, pH 7.0, containing 30 mM Tris and 2 mM dithiothreitol with a reservoir solution containing 0.1 M HEPES, pH 7.0, and 40% 2-methyl-2,4-pentanediol. Crystal structures of the enzyme and its complex with the substrate analog inhibitor, 6,7-dioxo-8-ribityllumazine
-
crystallization of enzyme complexed with 6-carboxyethyl-7-oxo-8-ribityllumazine, sitting drop vapour diffusion method against equal amounts of reservoir solution containing 0.1 M bicine, pH 9.0, 65% v/v 2-mehyl-2,4-pentanediol, enzyme solution: 9 mg/ml, 20 mM TrisHCl, pH 7.0, 0.1 M KCl, 10 molar excess of solid 8, X-ray structure determination and analysis, structure model building and refinement, overview
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 8
-
0C, stable for several h in presence of a suitable reducing agent
637561
6 - 10
-
26C, 18 h, stable
637575
6.3 - 7.6
-
55C, 18 h, stable
637575
additional information
-
heavy enzyme is instable at elevated pH
637570
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0 - 2
-
cold lability, inclusion of 0.01 M sodium sulfite in the solution used in purification prevents inactivation
60
-
24 h, no loss of activity, without substrate
85
-
10 min, complete loss of activity
92
-
1 min, complete loss of activity
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
freezing, completely inactivates spinach enzyme
-
high ionic strength protects yeast enzyme against inactivation
-
reducing agents, e.g. cysteine, ascorbate or Na2SO4 stabilize yeast and spinach enzyme
stable at 26C in 4 M urea for 18 h, 4 M urea completely inactivates at 55C
-
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
lability in presence of O2
-
637563
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, completely purified enzyme, stable for several months
-
-20C, slow decomposition by formation of large beta-subunit aggregates devoid of alpha-subunits
-
-90C or in liquid N2, stable for several months
-
0-4C, stable for 1 week in presence of saturated ammonium sulfate
-
4C, 6 months, no loss of activity
-
frozen, mycelium, several months without loss of activity
-
frozen, partially purified in dissolved ammonium sulfate precipitation pellet, stable several weeks
-
solution in 0.1 M phosphate, pH 7.0, 10 mM EDTA and 10 mM sodium sulfite, stable for several months
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
1500fold
Methanothermobacter thermautotrophicum
heavy enzyme
-
heavy enzyme; light enzyme
-
light enzyme
-
partially
recombinant enzyme from Escherichia coli
-
recombinant enzyme from Escherichia coli to homogeneity; recombinant enzyme from Escherichia coli to homogeneity
-
recombinant wild-type and mutant enzymes from Escherichia coli by ion exchange chromatography, ultrafiltration, gel filtration, and hydrophobic interaction chromatography
wild-type enzyme and mutants
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cloning of sequence segments of residues 1-97 and 101-213, and expression in Escherichia coli
-
DNA and amino acid sequence determination and analysis, functional expression in riboflavin-deficient Escherichia coli mutant BSV23
Methanothermobacter thermautotrophicum
DNA and amino acid sequence determination and analysis, subcloning and expression in Escherichia coli strains M15 and XL1-Blue, wild-type and mutant enzymes
expression in Escherichia coli
expression of beta60 capsid
-
expression of wild-type and mutant enzymes in strain BL21(DE3)
-
optimization of expression in Escherichia coli by construction of a synthetic gene; optimization of expression in Escherichia coli by construction of a synthetic gene, phylogenetic analysis
-
phylogenetic analysis, highly effective expression in Escherichia coli by construction of a synthetic gene optimized for heterologous expression by exchange of 59 codons
-
recombinant N-terminal domain of riboflavin synthase is prepared
-
ribC hyperexpression strain, DNA sequence determination of mutants
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
gene expression is up-regulated 5.7fold under iron deficiency
strongest expression levels are observed during the last stage of fruit ripening
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A43L
-
decrease in affinity for substrate 6,7-dimethyl-8-ribityllumazine. A43L replacement causes substantial perturbation of the overall binding site topology
C48S
-
mutation in the activity cavity, causes significant 19F NMR chemical shift modulation of trifluoromethyl derivatives of 6,7-dimethyl-8-ribityllumazine in complex with the protein. Replacement of C48 changes the electron density topology in the N-terminal substrate binding site in the vicinity of C-6 and C-7 atoms of bound ligand
D143G
-
site-directed mutagenesis, soluble protein, too unstable to be purified
D143N
-
site-directed mutagenesis, soluble protein, too unstable to be purified
D185L
-
site-directed mutagenesis, low remaining activity
E183G
-
site-directed mutagenesis, reduced activity
E66G
-
site-directed mutagenesis, low remaining activity
E85G
-
site-directed mutagenesis, reduced activity
F2Y
-
site-directed mutagenesis, very low remaining activity
H97Q
-
site-directed mutagenesis, low remaining activity
K137A
-
site-directed mutagenesis, low remaining activity
N181G
-
site-directed mutagenesis, soluble protein, too unstable to be purified
N45G
-
site-directed mutagenesis, slightly reduced activity
N83G
-
site-directed mutagenesis, reduced activity
S146G
-
site-directed mutagenesis, low remaining activity
T3R
-
site-directed mutagenesis, slightly reduced activity, low expression rate
T50A
-
production by site-directed mutagenesis, replacement of threonine residue with alanine decreases the acidity of protein-bound by 1-2 orders of magnitude
T67A
-
production by site-directed mutagenesis, replacement of threonine residue with alanine decreases the acidity of protein-bound by 1-2 orders of magnitude
T71A
-
site-directed mutagenesis, slightly reduced activity
Y133A
-
site-directed mutagenesis, soluble protein, too unstable to be purified
C48A
site-directed mutagenesis, nearly inactive mutant
C48M
site-directed mutagenesis, nearly inactive mutant
C48S
site-directed mutagenesis, highly decreased activity compared to the wild-type enzyme
S146A
site-directed mutagenesis, slightly increased activity compared to the wild-type enzyme
S146C
site-directed mutagenesis, slightly increased activity compared to the wild-type enzyme
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
drug development
medicine
-
enzyme is an attractive target for antimicrobial agents, since it is nonexistent in humans
pharmacology
the enzyme is a target for development of antiinfective drugs
additional information
Show AA Sequence (4219 entries)
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