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
2.7.1.26
-
RECOMMENDED NAME
GeneOntology No.
riboflavin kinase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
ATP + riboflavin = ADP + FMN
show the reaction diagram
ordered bi bi mechanism in which riboflavin binds first followed by ATP. ADP is released first followed by FMN
-
ATP + riboflavin = ADP + FMN
show the reaction diagram
ordered reaction mechanism, FMN binding o the binary enzyme-MgADP complex induces important conformational changes
-
ATP + riboflavin = ADP + FMN
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
phospho group transfer
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
5,6-dimethylbenzimidazole 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].
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
AtFMN/FHy
-
bifunctional enzyme has riboflavin kinase and FMN hydrolase activities
ATP: riboflavin kinase
-
-
ATP:riboflavin kinase
Q59263
-
FAD synthetase
Q59263
bifunctional enzyme, the C-terminal is associated with ATP:riboflavin kinase activity and the N-terminal associated with ATP:FMN adenylyltransferase activity
FK
-
-
-
-
flavokinase
-
-
-
-
flavokinase
-
-
flavokinase/FAD synthetase
-
-
flavokinase/FAD synthetase
A3FM23
-
flavokinase/flavin adenine dinucleotide synthetase
-
bifunctional enzyme EC 2.7.1.26/EC 2.7.2.2
flavokinase/flavin adenine dinucleotide synthetase
A3FM23
bifunctional enzyme EC 2.7.1.26/EC 2.7.2.2
kinase, riboflavin
-
-
-
-
riboflavin kinase
-
-
riboflavin kinase
-
-
riboflavin kinase/FMN adenylyltransferase
-
FADS, bifunctional enzyme, the C-terminus exhibits ATP: riboflavin kinase activity
riboflavine kinase
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9032-82-0
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
ecotype Columbia
-
-
Manually annotated by BRENDA team
monofunctional enzyme
-
-
Manually annotated by BRENDA team
RibC from wild-type strain 1012 and RibC820 from riboflavin-overproducing mitant strain RB52.ribC wild-type gene product has both flavokinase and flavin adenine dinucleotide synthetase activity
Uniprot
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 ACCESSION NO.
COMMENTARY
LITERATURE
physiological function
-
riboflavin kinase is a TNF-receptor-1 binding protein that couples TNF-receptor-1 to NADPH oxidase
physiological function
-
the enzyme plays a critical role in the KD548-Fc-mediated reactive oxygen species accumulation and downstream signaling. The enzyme is essential in recruiting Nox1 to death receptor4/5
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2'-dATP + riboflavin
2'-dADP + riboflavin 5'-phosphate
show the reaction diagram
-
-
-
-
?
2'-dATP + riboflavin
2'-dADP + riboflavin 5'-phosphate
show the reaction diagram
-
50% of the activity with ATP
-
-
?
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
-
60% of the activity with riboflavin
-
-
?
ATP + 2-thioriboflavin
ADP + 2-thioriboflavin 5'-phosphate
show the reaction diagram
-
30% of the activity with riboflavin
-
-
-
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-deazariboflavin
ADP + 5-deazariboflavin 5'-phosphate
show the reaction diagram
-
-
-
-
?
ATP + 5-deazariboflavin
ADP + 5-deazariboflavin 5'-phosphate
show the reaction diagram
-
-
-
-
?
ATP + 5-deazariboflavin
ADP + 5-deazariboflavin 5'-phosphate
show the reaction diagram
-
15% of the activity with riboflavin
-
-
?
ATP + 5-deazariboflavin
ADP + 5-deazariboflavin 5'-phosphate
show the reaction diagram
-
as active as riboflavin
-
-
-
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
-
35% of the activity with riboflavin
-
-
?
ATP + 6,7-dichloro-9-(D-1'-ribityl)isoalloxazine
ADP + 6,7-dichloro-9-(D-1'-ribityl)isoalloxazine phosphate
show the reaction diagram
-
52% of the activity with riboflavin
-
-
-
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
-
35% of the activity with riboflavin
-
-
?
ATP + 8-demethylriboflavin
ADP + 8-demethylriboflavin 5'-phosphate
show the reaction diagram
-
110% of the activity with riboflavin
-
-
?
ATP + 8-dimethylamino-8-demethylriboflavin
ADP + 8-dimethylamino-8-demethylriboflavin 5'-phosphate
show the reaction diagram
-
110% of the activity with riboflavin
-
-
?
ATP + 8-dimethylamino-8-demethylriboflavin
ADP + 8-dimethylamino-8-demethylriboflavin 5'-phosphate
show the reaction diagram
-
70% of the activity with riboflavin
-
-
?
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
-
14% of the activity with riboflavin
-
-
?
ATP + arabitylflavin
ADP + arabitylflavin phosphate
show the reaction diagram
-
slightly more active than riboflavin
-
-
?
ATP + D-erythroflavin
ADP + D-erythroflavin 5'-phosphate
show the reaction diagram
-
-
-
-
-
ATP + D-erythroflavin
ADP + D-erythroflavin 5'-phosphate
show the reaction diagram
-
-
-
-
?
ATP + D-erythroflavin
ADP + D-erythroflavin 5'-phosphate
show the reaction diagram
-
10-(D-erythro)flavin, 33% of the activity with riboflavin
-
-
?
ATP + riboflavin
ADP + FMN
show the reaction diagram
-
-
-
-
?
ATP + riboflavin
ADP + FMN
show the reaction diagram
-
-
-
-
?
ATP + riboflavin
ADP + FMN
show the reaction diagram
P54575
-
-
-
?
ATP + riboflavin
ADP + FMN
show the reaction diagram
-
-
-
-
?
ATP + riboflavin
ADP + FMN
show the reaction diagram
-, Q969G6
-
-
-
?
ATP + riboflavin
ADP + FMN
show the reaction diagram
-
-
-
-
?
ATP + riboflavin
ADP + FMN
show the reaction diagram
-
-
-
-
ir
ATP + riboflavin
ADP + FMN
show the reaction diagram
-
-
-
-
?
ATP + riboflavin
ADP + FMN
show the reaction diagram
-
-
-
-
?
ATP + riboflavin
ADP + FMN
show the reaction diagram
-
-
-
-
?
ATP + riboflavin
ADP + FMN
show the reaction diagram
-
-
-
-
?
ATP + riboflavin
ADP + FMN
show the reaction diagram
-
-
-
-
?
ATP + riboflavin
ADP + FMN
show the reaction diagram
O74866, -
-
-
-
?
ATP + riboflavin
ADP + FMN
show the reaction diagram
-
-
-
-
?
ATP + riboflavin
ADP + FMN
show the reaction diagram
-
-
-
-
?
ATP + riboflavin
ADP + FMN
show the reaction diagram
Q59263
-
-
-
?
ATP + riboflavin
ADP + FMN
show the reaction diagram
A3FM23, -
-
-
-
?
ATP + riboflavin
ADP + FMN
show the reaction diagram
-
specific for the reduced form of riboflavin
-
-
?
ATP + riboflavin
ADP + FMN
show the reaction diagram
-, Q969G6
essential enzyme catalyzing the phosphorylation of riboflavin to form FMN, an obligatory step in vitamin B2 utilization and flavin cofactor synthesis
-
-
?
ATP + riboflavin
ADP + FMN
show the reaction diagram
-
key enzyme in flavin biosynthesis
-
-
?
ATP + riboflavin
ADP + FMN
show the reaction diagram
-
key enzyme in flavin biosynthesis
-
-
?
ATP + riboflavin
ADP + FMN
show the reaction diagram
P54575
ribC is essential for growth of Bacillus subtilis. RibC is not directly involved in the riboflavin regulatory system
-
-
?
ATP + riboflavin
ADP + FMN
show the reaction diagram
-
substrate and product binding structure, overview
-
-
ir
ATP + riboflavin
ADP + FMN
show the reaction diagram
-
the flavokinase activity appears to be localized to the N-terminal domain of the protein. RibR specifically interacts in vivo with the nontranslated wild-type leader of the mRNA of the riboflavin biosynthetic operon. In RibR itself, interaction was localized to the carboxy-terminate part of the protein
-
-
?
ATP + roseoflavin
ADP + roseoflavin 5'-phosphate
show the reaction diagram
-
-
-
-
?
ATP + roseoflavin
ADP + roseoflavin 5'-phosphate
show the reaction diagram
A3FM23, -
-
-
-
?
ATP + roseoflavin
ADP + roseoflavin 5'-phosphate
show the reaction diagram
-
187% of the activity with 8-demethylriboflavin
-
-
?
ATP + roseoflavin
ADP + roseoflavin 5'-phosphate
show the reaction diagram
-
enzyme from intestinal mucosa and liver
-
-
?
ATP + roseoflavin
ADP + roseoflavin 5'-phosphate
show the reaction diagram
-
81% of the activity with riboflavin
-
-
?
ATP + roseoflavin
ADP + roseoflavin 5'-phosphate
show the reaction diagram
-
90% of the activity with riboflavin
-
-
?
CTP + riboflavin
CTP + riboflavin 5'-phosphate
show the reaction diagram
-
50% of the activity with ATP
-
-
?
CTP + riboflavin
CTP + riboflavin 5'-phosphate
show the reaction diagram
-
39% of the activity with ATP
-
-
?
dATP + riboflavin
dADP + FMN
show the reaction diagram
-
-
-
-
?
dATP + riboflavin
dADP + FMN
show the reaction diagram
-
-
-
-
?
GTP + riboflavin
GTP + riboflavin 5'-phosphate
show the reaction diagram
-
no activity
-
-
-
riboflavin + ATP
FMN + ADP
show the reaction diagram
-
-
-
-
?
UTP + riboflavin
UDP + FMN
show the reaction diagram
-
UTP is a poor substrate
-
-
?
UTP + riboflavin
UDP + FMN
show the reaction diagram
-
31% of the activity with ATP
-
-
?
GTP + riboflavin
GTP + riboflavin 5'-phosphate
show the reaction diagram
-
35% of the activity with ATP
-
-
?
additional information
?
-
-
analogs of riboflavin modified at position 8 seem to be good substrates, analogs modified at position 3 are not phosphorylated
-
-
-
additional information
?
-
P54575
ribC wild-type gene product has both flavokinase and flavin adenine dinucleotide synthetase activity
-
-
-
additional information
?
-
-
no phosphorylation of isoriboflavin, galactoflavin, dulcitylflavin, sorbitylflavin
-
-
-
additional information
?
-
-
the riboflavin kinase encoding gene ribR of Bacillus subtilis is a part of a 10 kb operon, which is negatively regulated by the yrzC gene product
-
-
-
additional information
?
-
A3FM23, -
the bifunctional flavokinase/flavin adenine dinucleotide synthetase produces inactive flavin cofactors and is not involved in resistance to the antibiotic roseoflavin
-
-
-
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
ATP + riboflavin
ADP + FMN
show the reaction diagram
-
-
-
-
ir
ATP + riboflavin
ADP + FMN
show the reaction diagram
-, Q969G6
essential enzyme catalyzing the phosphorylation of riboflavin to form FMN, an obligatory step in vitamin B2 utilization and flavin cofactor synthesis
-
-
?
ATP + riboflavin
ADP + FMN
show the reaction diagram
-
key enzyme in flavin biosynthesis
-
-
?
ATP + riboflavin
ADP + FMN
show the reaction diagram
-
key enzyme in flavin biosynthesis
-
-
?
ATP + riboflavin
ADP + FMN
show the reaction diagram
P54575
ribC is essential for growth of Bacillus subtilis. RibC is not directly involved in the riboflavin regulatory system
-
-
?
ATP + riboflavin
ADP + FMN
show the reaction diagram
-
the flavokinase activity appears to be localized to the N-terminal domain of the protein. RibR specifically interacts in vivo with the nontranslated wild-type leader of the mRNA of the riboflavin biosynthetic operon. In RibR itself, interaction was localized to the carboxy-terminate part of the protein
-
-
?
additional information
?
-
-
the riboflavin kinase encoding gene ribR of Bacillus subtilis is a part of a 10 kb operon, which is negatively regulated by the yrzC gene product
-
-
-
additional information
?
-
A3FM23, -
the bifunctional flavokinase/flavin adenine dinucleotide synthetase produces inactive flavin cofactors and is not involved in resistance to the antibiotic roseoflavin
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Cd2+
-
38% of the activation with Zn2+
Co2+
-
0.1 mM, activation is about 65% of that with 0.2 mM Mg2+
Co2+
-
34% of the activation with Zn2+
Co2+
-
divalent metal ions are essential activators, in the order of decreasing efficiency: Mg2+, Co2+, Zn2+, Cu2+, Cd2+, Fe2+
Mg2+
-
enhances activity
Mg2+
-
activates
Mg2+
-
0.2 mM, Mg2+ or Zn2+ required
Mg2+
-
38% of the activation with Zn2+
Mg2+
-
most effective essential activator
Mg2+
-
required for maximal activity
Mg2+
-
-
Mn2+
-
activation is about 45% of that with 0.2 mM Mg2+
Mn2+
-
31% of the activation with Zn2+
Zn2+
-
enhances activity, more effective than Mg2+
Zn2+
-
activation is 1.8times of that with Mg2+
Zn2+
-
activation is about 90% of that with 0.2 mM Mg2+
Zn2+
-
best divalent metal activator
Zn2+
-
less effective in activation than Mg2+
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
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
-
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
Cd2+
-
maximum inhibition at 1 mM
Cd2+
-
78% inhibition at 1 mM, effect is completely reversed by increasing concentrations of Zn2+, protection by glutathione and dithiothreitol
Cu2+
-
maximum inhibition at 1 mM
FMN
-
product inhibition
Hg2+
-
0.1 mM, complete inhibition
Lumiflavin
-
0.01 mM, 38% inhibition
Lumiflavin
-
0.5 mM, 4% inhibition
PCMB
-
1 mM, 70% inhibition
riboflavin
Q59263
substrate inhibition
Riboflavin 5'-phosphate
-
-
roseoflavin
-
0.4 mM, 8% inhibition
ZnADP-
-
product inhibition
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
Carbonate
-
50 mM, activates
NO3-
-
50 mM, activates
phosphate
-
50 mM, activates
SO42-
-
50 mM, activates
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.025
-
adenosine-5'-O-(3-thiotriphosphate)
-
-
0.0002
-
ATP
-
bifunctional enzyme AtFMN/FHy
0.0037
-
ATP
-
-
0.0065
-
ATP
-
-
0.008
-
ATP
-
enzyme from brain
0.0083
-
ATP
-
pH 7.0, 25C
0.01
-
ATP
Q59263
mutant enzyme S164D, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37C
0.011
-
ATP
Q59263
mutant enzyme R161D, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37C; mutant enzyme T165D, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37C
0.012
-
ATP
Q59263
mutant enzyme H28D, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37C; mutant enzyme R161A, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37C; mutant enzyme S164A, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37C; mutant enzyme T165A, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37C
0.0137
-
ATP
-
apparent value, wild type enzyme, at 37C in 20 mM PIPES pH 7.0, 0.8 mM MgCl2
0.014
-
ATP
Q59263
mutant enzyme H28A, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37C; mutant enzyme H31A, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37C; wild type enzyme, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37C
0.0176
-
ATP
-
apparent value, mutant enzyme E268D, at 37C in 20 mM PIPES pH 7.0, 0.8 mM MgCl2
0.024
-
ATP
Q59263
mutant enzyme N125A, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37C
0.035
-
ATP
Q59263
mutant enzyme N125D, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37C
0.0453
-
ATP
-
apparent value, mutant enzyme N210D, at 37C in 20 mM PIPES pH 7.0, 0.8 mM MgCl2
0.112
-
ATP
-
pH 8, 37C
0.2
-
ATP
-
pH 8, 37C
0.0015
-
D-alloflavin
-
-
0.0011
-
D-erythroflavin
-
-
0.0012
-
D-riboflavin
-
-
2.1e-05
-
MgATP2-
-
pH 8.5, 30C
1.03e-05
-
riboflavin
-
bifunctional enzyme AtFMN/FHy
0.00012
-
riboflavin
-
pH 8.5, 30C
0.00032
-
riboflavin
-
allosteric kinetics
0.0017
-
riboflavin
Q59263
mutant enzyme N125A, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37C
0.0021
-
riboflavin
-
apparent value, mutant enzyme N210D, at 37C in 20 mM PIPES pH 7.0, 0.8 mM MgCl2
0.0041
-
riboflavin
-
apparent value, mutant enzyme E268D, at 37C in 20 mM PIPES pH 7.0, 0.8 mM MgCl2
0.0045
-
riboflavin
Q59263
mutant enzyme H31A, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37C
0.0047
-
riboflavin
-
-
0.0047
-
riboflavin
-
pH 7.2, 37C
0.0056
-
riboflavin
Q59263
mutant enzyme S164D, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37C
0.0077
-
riboflavin
Q59263
mutant enzyme T165D, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37C
0.0088
-
riboflavin
Q59263
mutant enzyme S164A, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37C
0.009
-
riboflavin
-
-
0.01
-
riboflavin
-
pH 8.0, 37C
0.01
-
riboflavin
-
-
0.01
-
riboflavin
-
pH 7.2, 37C
0.01
-
riboflavin
-
pH 8.0, 37C
0.01
-
riboflavin
Q59263
mutant enzyme T165A, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37C
0.011
-
riboflavin
-
-
0.012
-
riboflavin
Q59263
mutant enzyme R161A, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37C
0.013
-
riboflavin
-
apparent value, wild type enzyme, at 37C in 20 mM PIPES pH 7.0, 0.8 mM MgCl2
0.013
-
riboflavin
Q59263
mutant enzyme R161D, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37C; wild type enzyme, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37C
0.0153
-
riboflavin
-
pH 7.0, 25C
0.016
-
riboflavin
Q59263
mutant enzyme N125D, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37C
0.023
-
riboflavin
Q59263
mutant enzyme H28A, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37C
0.025
-
riboflavin
Q59263
mutant enzyme H28D, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37C
0.04
-
riboflavin
A3FM23, -
37C
0.055
-
riboflavin
-
37C
0.18
-
riboflavin
-
pH 8, 37C
0.03
-
roseoflavin
-
37C
0.03
-
roseoflavin
A3FM23, -
37C
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.042
-
ATP
-
apparent value, mutant enzyme N210D, at 37C in 20 mM PIPES pH 7.0, 0.8 mM MgCl2
0.07
-
ATP
-
apparent value, mutant enzyme E268D, at 37C in 20 mM PIPES pH 7.0, 0.8 mM MgCl2
0.75
-
ATP
Q59263
mutant enzyme H28A, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37C; mutant enzyme T165D, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37C
0.77
-
ATP
Q59263
mutant enzyme N125A, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37C
0.92
-
ATP
Q59263
mutant enzyme H28D, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37C; mutant enzyme S164D, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37C
0.97
-
ATP
Q59263
mutant enzyme H31A, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37C
0.98
-
ATP
Q59263
mutant enzyme S164A, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37C
1.08
-
ATP
Q59263
mutant enzyme R161A, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37C
1.1
-
ATP
Q59263
mutant enzyme T165A, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37C
1.13
-
ATP
-
apparent value, wild type enzyme, at 37C in 20 mM PIPES pH 7.0, 0.8 mM MgCl2
1.13
-
ATP
Q59263
mutant enzyme R161D, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37C; wild type enzyme, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37C
1.33
-
ATP
Q59263
mutant enzyme N125D, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37C
0.1
-
MgATP2-
-
pH 8.5, 30C
0.045
-
riboflavin
-
apparent value, mutant enzyme E268D, at 37C in 20 mM PIPES pH 7.0, 0.8 mM MgCl2
0.085
-
riboflavin
-
apparent value, mutant enzyme N210D, at 37C in 20 mM PIPES pH 7.0, 0.8 mM MgCl2
0.1
-
riboflavin
-
pH 8.5, 30C
0.3
-
riboflavin
A3FM23, -
37C
0.7
-
riboflavin
-
37C
1.85
-
riboflavin
Q59263
mutant enzyme N125A, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37C
2.82
-
riboflavin
Q59263
mutant enzyme H31A, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37C
2.85
-
riboflavin
Q59263
mutant enzyme T165A, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37C
3
-
riboflavin
Q59263
mutant enzyme T165D, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37C
3.08
-
riboflavin
Q59263
mutant enzyme S164D, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37C
4.32
-
riboflavin
Q59263
mutant enzyme S164A, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37C
4.78
-
riboflavin
Q59263
mutant enzyme H28D, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37C
5
-
riboflavin
-
apparent value, wild type enzyme, at 37C in 20 mM PIPES pH 7.0, 0.8 mM MgCl2
5
-
riboflavin
Q59263
mutant enzyme R161A, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37C; mutant enzyme R161D, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37C
5.02
-
riboflavin
Q59263
wild type enzyme, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37C
6.92
-
riboflavin
Q59263
mutant enzyme N125D, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37C
7.12
-
riboflavin
Q59263
mutant enzyme H28A, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37C
0.4
-
roseoflavin
-
37C
0.5
-
roseoflavin
A3FM23, -
37C
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.83
-
ATP
-
apparent value, mutant enzyme N210D, at 37C in 20 mM PIPES pH 7.0, 0.8 mM MgCl2
22040
3.83
-
ATP
-
apparent value, mutant enzyme E268D, at 37C in 20 mM PIPES pH 7.0, 0.8 mM MgCl2
22040
31.7
-
ATP
Q59263
mutant enzyme N125A, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37C
22040
38.3
-
ATP
Q59263
mutant enzyme N125D, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37C
22040
51.7
-
ATP
Q59263
mutant enzyme H28A, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37C
22040
68.3
-
ATP
Q59263
mutant enzyme T165D, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37C
22040
71.7
-
ATP
Q59263
mutant enzyme H31A, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37C
22040
78.3
-
ATP
Q59263
mutant enzyme H28D, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37C
22040
81.7
-
ATP
Q59263
wild type enzyme, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37C
22040
82.17
-
ATP
-
apparent value, wild type enzyme, at 37C in 20 mM PIPES pH 7.0, 0.8 mM MgCl2
22040
83.3
-
ATP
Q59263
mutant enzyme S164A, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37C
22040
88.3
-
ATP
Q59263
mutant enzyme S164D, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37C
22040
90
-
ATP
Q59263
mutant enzyme T165A, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37C
22040
93.3
-
ATP
Q59263
mutant enzyme R161A, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37C
22040
101.7
-
ATP
Q59263
mutant enzyme R161D, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37C
22040
10.83
-
riboflavin
-
apparent value, mutant enzyme E268D, at 37C in 20 mM PIPES pH 7.0, 0.8 mM MgCl2
16192
40.3
-
riboflavin
-
apparent value, mutant enzyme N210D, at 37C in 20 mM PIPES pH 7.0, 0.8 mM MgCl2
16192
200
-
riboflavin
Q59263
mutant enzyme H28D, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37C
16192
283
-
riboflavin
Q59263
mutant enzyme T165A, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37C
16192
300
-
riboflavin
Q59263
mutant enzyme H28A, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37C
16192
383
-
riboflavin
Q59263
mutant enzyme R161D, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37C; mutant enzyme T165D, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37C; wild type enzyme, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37C
16192
386
-
riboflavin
-
apparent value, wild type enzyme, at 37C in 20 mM PIPES pH 7.0, 0.8 mM MgCl2
16192
417
-
riboflavin
Q59263
mutant enzyme R161A, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37C
16192
433
-
riboflavin
Q59263
mutant enzyme N125D, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37C
16192
483
-
riboflavin
Q59263
mutant enzyme S164A, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37C
16192
550
-
riboflavin
Q59263
mutant enzyme S164D, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37C
16192
617
-
riboflavin
Q59263
mutant enzyme H31A, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37C
16192
1083
-
riboflavin
Q59263
mutant enzyme N125A, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37C
16192
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
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
-
riboflavin
Q59263
mutant enzyme H28A, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37C
0.0019
-
riboflavin
Q59263
mutant enzyme H28D, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37C
0.0032
-
riboflavin
Q59263
mutant enzyme T165A, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37C
0.0033
-
riboflavin
Q59263
mutant enzyme N125D, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37C
0.004
-
riboflavin
Q59263
wild type enzyme, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37C
0.0041
-
riboflavin
Q59263
mutant enzyme T165D, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37C
0.0044
-
riboflavin
Q59263
mutant enzyme S164A, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37C
0.0046
-
riboflavin
Q59263
mutant enzyme N125A, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37C
0.0051
-
riboflavin
Q59263
mutant enzyme R161A, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37C; mutant enzyme R161D, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37C
0.0058
-
riboflavin
Q59263
mutant enzyme S164D, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37C
0.0063
-
riboflavin
Q59263
mutant enzyme H31A, in 20 mM PIPES, 0.8 mM MgCl2, pH 7.0, at 37C
0.018
-
Riboflavin 5'-phosphate
-
pH 8, 37C
0.023
-
ZnADP-
-
pH 8.0, 37C, against ZnATP2-
0.12
-
ZnADP-
-
pH 8.0, 37C, against riboflavin
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.00023
-
-
-
0.0083
-
-
continuous fluorometric assay
0.0129
-
-
-
0.716
-
-
enzyme from brain
additional information
-
-
bioluminescent assay
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7
-
-
-
8.5
9
-
Tris-HCl buffer
9
-
-
enzyme from brain
9
-
-
enzyme from intestinal mucosa
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5
8.5
-
enzyme is active between pH 5 and 8.5
5
9
-
pH 5.0: about 30% of maximal activity, pH 9.0: about 65% of maximal activity
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
35
-
-
-
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
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 ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
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
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
13500
-
-
gel filtration
27000
-
-
gel filtration
27250
-
-
gel filtration
34200
-
P54575
gel filtration
35000
-
-
gel filtration
35500
-
-
gel filtration
40000
-
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
monomer
-
1 * 13500, SDS-PAGE
monomer
-
1 * 28000, SDS-PAGE
monomer
-
1 * 30000, SDS-PAGE
monomer
-
1 * 40000, SDS-PAGE
monomer
-
1 * 35500, SDS-PAGE
monomer
P54575
1 * 36000, SDS-PAGE
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
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
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
-
-
enzyme immobilized by amide linkage to omega aminoalkyl-agarose-beads has a half-life of three weeks
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
loss of activity during repeated freezing and thawing
-
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
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
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 ACCESSION NO.
LITERATURE
recombinant enzyme
P54575
presence of ATP:riboflavin 5'-phosphotransferase and ATP:FMN adenylyltransferase on a single polypeptide
-
recombinant, His-tagged enzyme by nickel affinity chromatography, removal of His-tag by TEV-protease treatment
-
partial, affinity chromatography
-
enzyme from brain
-
recombinant enzyme
A3FM23, -
affinity chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
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
-
amplification, cloning and expression of ribR gene in Escherichia coli; expression of ribC gene in Escherichia coli
-
expression of ribC gene in Escherichia coli
P54575
expressed in Escherichis coli BL-21pLysS (DE3), C-terminal glutathione S-transferase fusionprotein
-
expressed in Escherichia coli
-
overproduced in Escherichia coli
A3FM23, -
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
E268D
-
the mutant shows strongly reduced catalytic efficiency compared to the wild type enzyme
H28A
Q59263
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
H28D
Q59263
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
H31A
Q59263
the mutant shows increased catalytic efficiency compared to the wild type enzyme
N125A
Q59263
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
N125D
Q59263
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
Q59263
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
R161D
Q59263
the mutant shows wild type catalytic efficiency
S164A
Q59263
the mutant shows increased catalytic efficiency compared to the wild type enzyme
S164D
Q59263
the mutant shows increased catalytic efficiency compared to the wild type enzyme
T165A
Q59263
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
T165D
Q59263
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 ACCESSION NO.
COMMENTARY
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