Information on EC 2.7.1.26 - riboflavin kinase

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

EC NUMBER
COMMENTARY hide
2.7.1.26
-
RECOMMENDED NAME
GeneOntology No.
riboflavin kinase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + riboflavin = ADP + FMN
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
5,6-dimethylbenzimidazole biosynthesis I (aerobic)
-
-
Biosynthesis of secondary metabolites
-
-
flavin biosynthesis
-
-
flavin biosynthesis I (bacteria and plants)
-
-
flavin biosynthesis III (fungi)
-
-
flavin biosynthesis IV (mammalian)
-
-
Metabolic pathways
-
-
Riboflavin metabolism
-
-
SYSTEMATIC NAME
IUBMB Comments
ATP:riboflavin 5'-phosphotransferase
The cofactors FMN and FAD participate in numerous processes in all organisms, including mitochondrial electron transport, photosynthesis, fatty-acid oxidation, and metabolism of vitamin B6, vitamin B12 and folates [5]. While monofunctional riboflavin kinase is found in eukaryotes, some bacteria have a bifunctional enzyme that exhibits both this activity and that of EC 2.7.7.2, FMN adenylyltransferase [5]. A divalent metal cation is required for activity (with different species preferring Mg2+, Mn2+ or Zn2+). In Bacillus subtilis, ATP can be replaced by other phosphate donors but with decreasing enzyme activity in the order ATP > dATP > CTP > UTP [6].
CAS REGISTRY NUMBER
COMMENTARY hide
9032-82-0
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
ecotype Columbia
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
cell wall lacking mutant
-
-
Manually annotated by BRENDA team
cv. Bright Yellow 2
-
-
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'-dATP + riboflavin
2'-dADP + riboflavin 5'-phosphate
show the reaction diagram
adenosine-5'-O-(3-thiotriphosphate) + riboflavin
?
show the reaction diagram
-
48% of the activity with ATP
-
-
?
ADP + riboflavin
AMP + FMN
show the reaction diagram
-
22% of the activity with ATP
-
-
?
ATP + 10-(D-allo)flavin
ADP + 10-(D-allo)flavin 5'-phosphate
show the reaction diagram
-
30% of the activity with riboflavin
-
-
?
ATP + 10-(L-arabo)flavin
ADP + 10-(L-arabo)flavin 5'-phosphate
show the reaction diagram
-
25% of the activity with riboflavin
-
-
?
ATP + 2'-deoxyriboflavin
ADP + 2'-deoxyriboflavin 5'-phosphate
show the reaction diagram
-
31% of the activity with riboflavin
-
-
?
ATP + 2-thioriboflavin
ADP + 2-thioriboflavin 5'-phosphate
show the reaction diagram
ATP + 3-deazariboflavin
ADP + 3-deazariboflavin 5'-phosphate
show the reaction diagram
-
-
-
-
?
ATP + 3-methylriboflavin
ADP + 3-methylriboflavin 5'-phosphate
show the reaction diagram
-
5% of the activity with riboflavin
-
-
?
ATP + 5-deazariboflavin
ADP + 5-deazariboflavin 5'-phosphate
show the reaction diagram
ATP + 5-methyl-5-deazariboflavin
ADP + 5-methyl-5-deazariboflavin 5'-phosphate
show the reaction diagram
-
-
-
-
?
ATP + 6,7-dichloro-9-(D-1'-ribityl)isoalloxazine
ADP + 6,7-dichloro-9-(D-1'-ribityl)isoalloxazine phosphate
show the reaction diagram
ATP + 6,7-dimethyl-9-(1'-D-ribityl)-2-iminoisoalloxazine
ADP + 6,7-dimethyl-9-(1'-D-ribityl)-2-iminoisoalloxazine 5'-phosphate
show the reaction diagram
-
18% of the activity with riboflavin
-
-
?
ATP + 6-methylriboflavin
ADP + 6-methylriboflavin 5'-phosphate
show the reaction diagram
-
-
-
-
?
ATP + 7-chlororiboflavin
ADP + 7-chlororiboflavin
show the reaction diagram
-
-
-
-
?
ATP + 8-bromo-8-demethylriboflavin
ADP + 8-bromo-8-demethylriboflavin 5-'phosphate
show the reaction diagram
-
384% of the activity with riboflavin
-
-
?
ATP + 8-chloro-8-demethylriboflavin
ADP + 8-chloro-8-demethylriboflavin 5'-phosphate
show the reaction diagram
-
122.2% of the activity with riboflavin
-
-
?
ATP + 8-demethylriboflavin
ADP + 8-demethylriboflavin 5'-phosphate
show the reaction diagram
ATP + 8-dimethylamino-8-demethylriboflavin
ADP + 8-dimethylamino-8-demethylriboflavin 5'-phosphate
show the reaction diagram
ATP + 8-ethoxy-8-demethylriboflavin
ADP + 8-ethoxy-8-demethylriboflavin 5'-phosphate
show the reaction diagram
-
210% of the activity with riboflavin
-
-
?
ATP + 8-fluoro-8-demethylriboflavin
ADP + 8-fluoro-8-demethylriboflavin 5'-phosphate
show the reaction diagram
-
132.2% of the activity with riboflavin
-
-
?
ATP + 8-iodo-8-demethylriboflavin
ATP + 8-iodo-8-demethylriboflavin 5'-phosphate
show the reaction diagram
-
334.7% of the activity with riboflavin
-
-
?
ATP + 8-methoxy-8-demethylriboflavin
ADP + 8-methoxy-8-demethylriboflavin 5'-phosphate
show the reaction diagram
-
114.5% of the activity with riboflavin
-
-
?
ATP + 8-methylamino-8-demethylriboflavin
ATP + 8-methylamino-8-demethylriboflavin 5'-phosphate
show the reaction diagram
-
237.3% of the activity with riboflavin
-
-
?
ATP + 9-azariboflavin
ADP + 9-azariboflavin 5'-phosphate
show the reaction diagram
-
-
-
-
?
ATP + alloflavin
ADP + alloflavin 5'-phosphate
show the reaction diagram
-
-
-
-
?
ATP + arabitylflavin
ADP + arabitylflavin phosphate
show the reaction diagram
ATP + D-erythroflavin
ADP + D-erythroflavin 5'-phosphate
show the reaction diagram
ATP + riboflavin
ADP + FMN
show the reaction diagram
ATP + roseoflavin
ADP + roseoflavin 5'-phosphate
show the reaction diagram
CTP + riboflavin
CTP + riboflavin 5'-phosphate
show the reaction diagram
dATP + riboflavin
dADP + FMN
show the reaction diagram
GTP + riboflavin
GTP + riboflavin 5'-phosphate
show the reaction diagram
riboflavin + ATP
FMN + ADP
show the reaction diagram
-
-
-
-
?
UTP + riboflavin
UDP + FMN
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
ATP + riboflavin
ADP + FMN
show the reaction diagram
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Cd2+
-
38% of the activation with Zn2+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1'-DL-glyceryl-6,7-dimethylisoalloxazine
-
competitive
1-Deazariboflavin
-
-
10-(2'-Hydroxyethyl)-isoalloxazine
-
0.01 mM, 34% inhibition
10-(4'-Carboxybutyl)-isoalloxazine
-
0.001 mM, 16% inhibition
10-(5'-Hydroxypentyl)-isoalloxazine
-
0.01 mM, 38% inhibition
10-(5'-Hydroxypentyl)flavin
-
-
10-(Hydroxyethyl)flavin
-
-
2'-Thioriboflavin
-
0.01 mM, 59% inhibition
3'-hydroxypropyl-6,7-dimethylisoalloxazine
-
competitive
3-Deazariboflavin
-
-
3-methylriboflavin
-
0.01 mM, 5% inhibition
4'-hydroxybutyl-6,7-dimethylisoalloxazine
-
competitive
5'-hydroxypentyl-6,7-dimethylisoalloxazine
-
competitive
5-Deazariboflavin
-
-
7,8-dimethyl-10-(2'-hydroxyethyl)-isoalloxazine
-
0.5 mM, 10% inhibition
7,8-dimethyl-10-(O-methylacetoxime)-isoaloxazine
-
0.5 mM, 34% inhibition
7alpha-Methylriboflavin
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0.01 mM, 95% inhibition
8-Aminoriboflavin
-
-
8-Diethylaminoriboflavin
-
-
8-Ethoxyriboflavin
-
-
8-Ethylaminoriboflavin
-
-
8-hydroxyriboflavin
-
-
8-Methoxyriboflavin
-
-
8-Methylaminoriboflavin
-
-
8-Methylethylaminoriboflavin
-
-
9-(6'-hydroxyhexyl)-6,7-dimethylisoalloxazine
-
competitive
FMN
-
product inhibition
lumichrome
-
-
Lumiflavin
riboflavin
substrate inhibition
riboflavin 5'-phosphate
-
-
roseoflavin
-
0.4 mM, 8% inhibition
ZnADP-
-
product inhibition
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Carbonate
-
50 mM, activates
NO3-
-
50 mM, activates
phosphate
-
50 mM, activates
SO42-
-
50 mM, activates
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.025
adenosine-5'-O-(3-thiotriphosphate)
-
-
0.0002 - 4.55
ATP
0.0015
D-alloflavin
-
-
0.0011
D-erythroflavin
-
-
0.0012
D-riboflavin
-
-
0.000021 - 0.005
MgATP2-
0.0000103 - 0.18
riboflavin
0.03
roseoflavin
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.042 - 1.33
ATP
0.1
MgATP2-
Neurospora crassa
-
pH 8.5, 30C
0.045 - 7.12
riboflavin
0.4 - 0.5
roseoflavin
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.83 - 101.7
ATP
10.83 - 1083
riboflavin
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0065
1'-DL-glyceryl-6,7-dimethylisoalloxazine
-
competitive
0.021
1-Deazariboflavin
-
pH 8, 37C
0.008
10-(5'-Hydroxypentyl)flavin
-
pH 8, 37C
0.007
10-(Hydroxyethyl)flavin
-
pH 8, 37C
0.0071
3'-hydroxypropyl-6,7-dimethylisoalloxazine
-
competitive
0.41
3-Deazariboflavin
-
pH 8, 37C
0.0076
4'-hydroxybutyl-6,7-dimethylisoalloxazine
-
competitive
0.0078
5'-hydroxypentyl-6,7-dimethylisoalloxazine
-
competitive
0.275
5-Deazariboflavin
-
pH 8, 37C
0.25
8-Aminoriboflavin
-
pH 8, 37C
0.02
8-Diethylaminoriboflavin
-
pH 8, 37C
0.016
8-Ethoxyriboflavin
-
pH 8, 37C
0.175
8-Ethylaminoriboflavin
-
pH 8, 37C
0.5
8-hydroxyriboflavin
-
pH 8, 37C
0.015
8-Methoxyriboflavin
-
pH 8, 37C
0.47
8-Methylaminoriboflavin
-
pH 8, 37C
0.03
8-Methylethylaminoriboflavin
-
pH 8, 37C
0.0079
9-(6'-hydroxyhexyl)-6,7-dimethylisoalloxazine
-
competitive
0.006
FMN
-
pH 8.0, 37C, against riboflavin
0.01
lumichrome
-
pH 8, 37C
0.007
Lumiflavin
-
pH 8, 37C
0.0018 - 0.0063
riboflavin
0.018
riboflavin 5'-phosphate
-
pH 8, 37C
0.023 - 0.12
ZnADP-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0083
0.716
-
enzyme from brain
additional information
-
bioluminescent assay
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.5 - 9
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 9
-
pH 5.0: about 30% of maximal activity, pH 9.0: about 65% of maximal activity
5 - 8.5
-
enzyme is active between pH 5 and 8.5
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
15 - 45
-
15C: about 60% of maximal activity, 45C: about 75% of maximal activity
20 - 45
-
the relative activities at pH 7.2 and 20C, 25C, 37C and 45C are 0.22, 0.46, 1, and 1.35, respectively
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Schizosaccharomyces pombe (strain 972 / ATCC 24843)
Schizosaccharomyces pombe (strain 972 / ATCC 24843)
Schizosaccharomyces pombe (strain 972 / ATCC 24843)
Schizosaccharomyces pombe (strain 972 / ATCC 24843)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
13500
-
gel filtration
27000
-
gel filtration
27250
-
gel filtration
34200
gel filtration
35000
-
gel filtration
35500
-
gel filtration
40000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purified recombinant enzyme with bound products FMN and MgADP, hanging drop vapour diffusion method, 34 mg/ml protein in 50 mM Tris, pH 7.4, 0.3 M NaCl, 1 mM DTT, 20C, mixing with equal volume of reservoir solution containing 0.1 M sodium acetate, pH 4.7, 30% PEG monomethyl ether 5000, and 0.2 M ammonium sulfate, followed by microseeding in reservoir solution containing 0.1 M sodium acetate, pH 4.4, 22.5% PEG monomethyl ether 5000, and 0.2 M ammonium sulfate, cryoprotection in 30% glycerol in reservoir solution, storage in liquid propane, X-ray diffraction structure determination and analysis at 2.4 A resolution
-
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
-
enzyme immobilized by amide linkage to omega aminoalkyl-agarose-beads has a half-life of three weeks
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
50% of the activity is lost on freezing, but the stability of the enzyme is not greatly affected by the period of freezing
-
enzyme immobilized by amide linkage to omega aminoalkyl-agarose-beads has a half-life of three weeks at 25C
-
enzyme is inactivated by freezing and thawing unless both riboflavin and 20% glycerol are added
-
loss of activity during repeated freezing and thawing
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
3C, MOPS buffer, activity decreases to approximately 35, 30 and 13% of the initial level after 24, 48, and 96 h, respectively
-
4C, 50% loss of activity after 2 d when the enzyme is stored in buffer alone, complete protection by 0.01 mM riboflavin
-
purified enzyme is unstable in dilute solution and can not be stored at -20C
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
affinity chromatography
-
enzyme from brain
-
partial, affinity chromatography
-
presence of ATP:riboflavin 5'-phosphotransferase and ATP:FMN adenylyltransferase on a single polypeptide
-
recombinant enzyme
recombinant, His-tagged enzyme by nickel affinity chromatography, removal of His-tag by TEV-protease treatment
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
amplification, cloning and expression of ribR gene in Escherichia coli; expression of ribC gene in Escherichia coli
-
expressed in Escherichia coli
-
expressed in Escherichis coli BL-21pLysS (DE3), C-terminal glutathione S-transferase fusionprotein
-
expression of ribC gene in Escherichia coli
overproduced in Escherichia coli
the functional overexpression of the individual domains in Escherichia coli establishes that the riboflavin kinase and FMN hydrolase activities reside, respectively, in the C-terminal (AtFMN) and N-terminal (AtFHy) domains of AtFMN/FHy
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E268D
-
the mutant shows strongly reduced catalytic efficiency compared to the wild type enzyme
H28A
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
H28D
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
H31A
the mutant shows increased catalytic efficiency compared to the wild type enzyme
N125A
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
N125D
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
N210D
-
the mutant shows strongly reduced catalytic efficiency compared to the wild type enzyme
R161A
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
R161D
the mutant shows wild type catalytic efficiency
S164A
the mutant shows increased catalytic efficiency compared to the wild type enzyme
S164D
the mutant shows increased catalytic efficiency compared to the wild type enzyme
T165A
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
T165D
the mutant shows wild type catalytic efficiency
E86Q
-
destroying the kinase domain, purified as C-terminal glutathione S-transferase fusionprotein
N36D
-
purified as C-terminal glutathione S-transferase fusionprotein
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
-
immobilized enzyme is effective for phosphorylating riboflavin and numerous riboflavin analogs and provides a facile method for preparing exclusively other synthetic methods, the 5'-phosphates
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