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ATP + 4'-butyl-FMN
diphosphate + 4'-butylflavin adenine dinucleotide
-
-
-
-
?
ATP + 5'-pentyl-FMN
diphosphate + 5'-pentylflavin adenine dinucleotide
-
-
-
-
?
ATP + 7,8-dibromo-FMN
diphosphate + 7,8-dibromoflavin adenine dinucleotide
-
-
-
-
?
ATP + 7,8-dichloro-FMN
diphosphate + 7,8-dichloroflavin adenine dinucleotide
-
-
-
-
?
ATP + 7-chloro-FMN
diphosphate + 7-chloroflavin adenine dinucleotide
-
-
-
-
?
ATP + 8-chloro-FMN
diphosphate + 8-chloroflavin adenine dinucleotide
-
-
-
-
?
ATP + FMN
diphosphate + FAD
ATP + iso-FMN
diphosphate + isoflavin adenine dinucleotide
-
-
-
-
?
ATP + roseoflavin mononucleotide
diphosphate + roseoflavin adenine dinucleotide
-
-
-
-
?
CTP + FMN
diphosphate + flavin cytidine dinucleotide
-
-
-
?
diphosphate + FAD
ATP + FMN
FMN + ATP
FAD + diphosphate
GTP + FMN
diphosphate + flavin guanidine dinucleotide
weak specific activity
-
-
?
additional information
?
-
ATP + FMN

diphosphate + FAD
-
-
-
?
ATP + FMN
diphosphate + FAD
-
-
r
ATP + FMN
diphosphate + FAD
essential for flavin metabolism
-
r
ATP + FMN
diphosphate + FAD
-
-
-
r
ATP + FMN
diphosphate + FAD
-
-
-
r
ATP + FMN
diphosphate + FAD
-
-
-
-
?
ATP + FMN
diphosphate + FAD
-
-
-
-
?
ATP + FMN
diphosphate + FAD
-
-
-
r
ATP + FMN
diphosphate + FAD
-
-
r
ATP + FMN
diphosphate + FAD
-
-
-
r
ATP + FMN
diphosphate + FAD
-
-
-
r
ATP + FMN
diphosphate + FAD
-
-
-
r
ATP + FMN
diphosphate + FAD
-
-
-
-
r
ATP + FMN
diphosphate + FAD
-
-
-
ATP + FMN
diphosphate + FAD
-
-
-
?
ATP + FMN
diphosphate + FAD
-
-
-
-
?
ATP + FMN
diphosphate + FAD
-
adenylation of FMN is reversible, FAD and diphosphate can be converted to FMN and ATP by the enzyme, under the conditions studied phosphorylation of riboflavin is irreversible
-
r
ATP + FMN
diphosphate + FAD
-
catalyzes 2 sequential steps in the biosynthesis of FAD, phosphorylation of riboflavin to produce FMN and subsequent adenylylation of FMN to form FAD
-
r
ATP + FMN
diphosphate + FAD
-
engineered mutant
-
-
?
ATP + FMN
diphosphate + FAD
-
-
-
r
ATP + FMN
diphosphate + FAD
-
-
-
-
?
ATP + FMN
diphosphate + FAD
-
-
-
?
ATP + FMN
diphosphate + FAD
-
-
-
-
r
ATP + FMN
diphosphate + FAD
the enzyme does not catalyze the reverse reaction to produce FMN and ATP from FAD and diphosphate
-
-
ir
ATP + FMN
diphosphate + FAD
-
-
-
ir
ATP + FMN
diphosphate + FAD
-
-
-
ir
ATP + FMN
diphosphate + FAD
-
-
-
ir
ATP + FMN
diphosphate + FAD
-
-
-
r
ATP + FMN
diphosphate + FAD
-
-
-
?
ATP + FMN
diphosphate + FAD
-
essentially irreversible in the direction of FAD formation
-
ir
ATP + FMN
diphosphate + FAD
-
biosynthesis of FAD is most likely regulated by this coenzyme as a product at the stage of FAD synthetase reaction
-
-
ATP + FMN
diphosphate + FAD
-
biosynthesis of FAD is most likely regulated by this coenzyme as a product at the stage of FAD synthetase reaction
-
ir
ATP + FMN
diphosphate + FAD
-
-
-
?
ATP + FMN
diphosphate + FAD
-
-
-
r
ATP + FMN
diphosphate + FAD
-
-
r
ATP + FMN
diphosphate + FAD
-
-
-
?
ATP + FMN
diphosphate + FAD
-
-
-
-
?
ATP + FMN
diphosphate + FAD
-
-
-
-
?
ATP + riboflavin

?
-
-
-
-
?
ATP + riboflavin
?
-
-
-
-
ir
diphosphate + FAD

ATP + FMN
-
-
-
r
diphosphate + FAD
ATP + FMN
-
-
-
-
r
diphosphate + FAD
ATP + FMN
-
low reaction rate
-
-
r
diphosphate + FAD
ATP + FMN
-
-
-
r
FMN + ATP

FAD + diphosphate
-
-
-
?
FMN + ATP
FAD + diphosphate
-
-
-
-
?
FMN + ATP
FAD + diphosphate
-
-
-
-
?
additional information

?
-
-
bifunctional FAD synthetase which shows FMN adenylyltransferase and flavokinase activities, producing FMN ATP:riboflavin 5'-phosphotransferase EC 2.7.1.26
-
-
-
additional information
?
-
bifunctional FAD synthetase which shows FMN adenylyltransferase and flavokinase activities, producing FMN ATP:riboflavin 5'-phosphotransferase EC 2.7.1.26
-
-
-
additional information
?
-
-
highly purified 5'-FMN is not accepted as a substrate
-
-
-
additional information
?
-
highly purified 5'-FMN is not accepted as a substrate
-
-
-
additional information
?
-
-
bifunctional FAD synthetase exhibiting both the activities of FAD synthetase, EC 2.7.7.2, and riboflavin kinase, EC 2.7.1.26
-
-
-
additional information
?
-
-
the flavin motif is involved in flavin ligand binding, role of active site residues in the catalytic mechanism, overview. The isoalloxazine ring is sandwiched between the indole ring of Trp184 and the planar guanidinium group of Arg189, while the hydrophilic pyrimidine ring forms two specific hydrogen bonds between its C4 carbonyl and the main chain amide of Asp181, and between its N3 amide and the side chain of Asp181, respectively. Residues Asn62, Asp66, Asp168, and Arg297 interact either with ATP phosphate groups, or to coordinate the catalytic Mg2+ ion either directly or indirectly through water molecules. Arg297 might be involved in the interaction with the phosphate groups of both substrates, and helps in their positioning for the nucleophilic attack in the adenylyltransfer reaction
-
-
-
additional information
?
-
-
bifunctional FAD synthetase which shows FMN adenylyltransferase and flavokinase activities, producing FMN ATP:riboflavin 5'-phosphotransferase EC 2.7.1.26
-
-
-
additional information
?
-
-
bifunctional FAD synthetase which shows FMN adenylyltransferase and flavokinase activities, producing FMN ATP:riboflavin 5'-phosphotransferase EC 2.7.1.26
-
-
-
additional information
?
-
bifunctional FAD synthetase which shows FMN adenylyltransferase and flavokinase activities, producing FMN ATP:riboflavin 5'-phosphotransferase EC 2.7.1.26
-
-
-
additional information
?
-
-
bifunctional FAD synthetase which shows FMN adenylyltransferase and flavokinase activities, producing FMN ATP:riboflavin 5'-phosphotransferase EC 2.7.1.26
-
-
-
additional information
?
-
-
bifunctional FAD synthetase which shows FMN adenylyltransferase and flavokinase activities, producing FMN ATP:riboflavin 5'-phosphotransferase EC 2.7.1.26
-
-
-
additional information
?
-
-
bifunctional FAD synthetase which shows FMN adenylyltransferase and flavokinase activities, producing FMN ATP:riboflavin 5'-phosphotransferase EC 2.7.1.26
-
-
-
additional information
?
-
-
FAD synthetase presents two catalytic modules, a C-terminus with ATP-riboflavin kinase activity and an N-terminus with ATP-flavin mononucleotide adenylyltransferase activity
-
-
-
additional information
?
-
bifunctional FAD synthetase exhibiting both the activities of FAD synthetase, EC 2.7.7.2, and riboflavin kinase, EC 2.7.1.26
-
-
-
additional information
?
-
-
bifunctional FAD synthetase exhibiting both the activities of FAD synthetase, EC 2.7.7.2, and riboflavin kinase, EC 2.7.1.26
-
-
-
additional information
?
-
-
bifunctional FAD synthetase exhibiting both the activities of FAD synthetase, EC 2.7.7.2, and riboflavin kinase, EC 2.7.1.26
-
-
-
additional information
?
-
-
the engineered FAD synthetase from Corynebacterium ammoniagenes with deleted N-terminal adenylation domain is a biocatalyst that is stable and efficient for direct and quantitative phosphorylation of riboflavin and riboflavin analogues to their corresponding FMN cofactors at preparative-scale, method evaluation, overview
-
-
-
additional information
?
-
-
bifunctional FAD synthetase which shows FMN adenylyltransferase and flavokinase activities, producing FMN ATP:riboflavin 5'-phosphotransferase EC 2.7.1.26
-
-
-
additional information
?
-
-
does not use 8-demethyl-8-amino-riboflavin mononucleotide as substrate
-
-
-
additional information
?
-
-
the enzyme does not function as a glycerol-3-phosphate cytidylyltransferase because it fails to catalyze the formation of glycerol cytidine dinucleotide when incubated with DL-glycerol 3-phosphate and CTP
-
-
-
additional information
?
-
the enzyme does not function as a glycerol-3-phosphate cytidylyltransferase because it fails to catalyze the formation of glycerol cytidine dinucleotide when incubated with DL-glycerol 3-phosphate and CTP
-
-
-
additional information
?
-
-
-
-
-
-
additional information
?
-
-
if the hydrogen-bonding capacity of the NH group at position 3 is blocked or removed by substitution, FMN analogues do not act as substrates or inhibitors, 3-deaza-FMN, 7,8-didemethyl-8-hydroxy-5-deaza-FMN, 5-methyl-7,8-didemethyl-8-hydroxy-5-deaza-(5-methyl)-FMN, 5'-sulfate-FMN, 5'-deoxy-FMN, 10-(3-chlorobenzyl)-FMN and 10-(hydroxyethyl)-5-deaza-FMN are no substrates
-
-
-
additional information
?
-
-
in the reverse reaction diphosphate cannot be replaced by orthophosphate or metaphosphate
-
-
-
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0.25
4'-butyl-FMN
-
pH 7.1, 37°C
0.0048 - 0.94
7,8-dibromo-FMN
0.082 - 0.12
7,8-dichloro-FMN
0.0076 - 0.0086
7-chloro-FMN
0.019
8-chloro-FMN
-
pH 7.1, 37°C
0.48
CTP
apparent value, in 35 mM TES (K+) buffer (pH 7.2) containing 14 mM dithiothreitol, 7 mM MgCl+, at 70°C
0.114
diphosphate
-
pH 7.6, 25°C
0.0004
FAD
-
pH 7.6, 25°C
0.015
iso-FMN
-
pH 7.1, 37°C
0.116
roseoflavin mononucleotide
-
with 24 mM Na2S2O4, in 50 mM potassium phosphate (pH 7.5), at 37°C
additional information
additional information
-
0.0048
7,8-dibromo-FMN

-
pH 7.1, 37°C, direct assay
0.94
7,8-dibromo-FMN
-
pH 7.1, 37°C, indirect assay
0.082
7,8-dichloro-FMN

-
pH 7.1, 37°C, indirect assay
0.12
7,8-dichloro-FMN
-
pH 7.1, 37°C, direct assay
0.0076
7-chloro-FMN

-
pH 7.1, 37°C, indirect assay
0.0086
7-chloro-FMN
-
pH 7.1, 37°C, direct assay
0.0107
ATP

-
-
0.0111
ATP
at pH 8.5; pH 8.5
0.0131
ATP
at pH 8.5; pH 8.5
0.0153
ATP
-
at 37°C, in 50 mM Tris-HCl, pH 7.5
0.0158
ATP
-
pH 7.0, 25°C, recombinant mutant R66A
0.0224
ATP
-
pH 7.0, 25°C, recombinant wild-type enzyme
0.025
ATP
apparent value, in 35 mM TES (K+) buffer (pH 7.2) containing 14 mM dithiothreitol, 7 mM MgCl+, at 70°C
0.0311
ATP
-
pH 7.0, 25°C, recombinant mutant R66E
0.03568
ATP
-
wild type enzyme, at 37°C in 20 mM PIPES pH 7.0, 10 mM MgCl2
0.0382
ATP
-
mutant enzyme T208D, at 37°C in 20 mM PIPES pH 7.0, 10 mM MgCl2
0.0387
ATP
-
mutant enzyme E268D, at 37°C in 20 mM PIPES pH 7.0, 10 mM MgCl2
0.0435
ATP
-
FADS trimer, 10 mM MgCl2 in 50 mM TrisHCl (pH 8.0), at 37°C
0.04537
ATP
-
mutant enzyme T208A, at 37°C in 20 mM PIPES pH 7.0, 10 mM MgCl2
0.04647
ATP
-
mutant enzyme E268A, at 37°C in 20 mM PIPES pH 7.0, 10 mM MgCl2
0.04704
ATP
-
mutant enzyme N210A, at 37°C in 20 mM PIPES pH 7.0, 10 mM MgCl2
0.071
ATP
-
pH 8.0, 37°C, MgATP
0.07667
ATP
-
mutant enzyme N210D, at 37°C in 20 mM PIPES pH 7.0, 10 mM MgCl2
0.079
ATP
-
FADS monomer, 10 mM MgCl2 in 50 mM TrisHCl (pH 8.0), at 37°C
0.00035
FMN

-
at 37°C, in 50 mM Tris-HCl, pH 7.5
0.00038
FMN
-
pH 7.0, 25°C, recombinant mutant R66E
0.0005
FMN
-
pH and temperature not specified in the publication, mutant N62A
0.00069
FMN
-
pH 7.0, 25°C, recombinant mutant R66A
0.00088
FMN
-
mutant enzyme E268A, at 37°C in 20 mM PIPES pH 7.0, 10 mM MgCl2; mutant enzyme T208D, at 37°C in 20 mM PIPES pH 7.0, 10 mM MgCl2
0.00095
FMN
-
mutant enzyme T208A, at 37°C in 20 mM PIPES pH 7.0, 10 mM MgCl2
0.001
FMN
-
pH and temperature not specified in the publication, wild-type enzyme
0.0011
FMN
-
pH and temperature not specified in the publication, mutant N62S
0.00117
FMN
-
mutant enzyme E268D, at 37°C in 20 mM PIPES pH 7.0, 10 mM MgCl2
0.00119
FMN
-
wild type enzyme, at 37°C in 20 mM PIPES pH 7.0, 10 mM MgCl2
0.0015
FMN
-
pH and temperature not specified in the publication, mutant D181A
0.0023
FMN
-
pH and temperature not specified in the publication, mutant R300A
0.003
FMN
-
pH and temperature not specified in the publication, mutant R297A
0.0054
FMN
-
FADS monomer, 10 mM MgCl2 in 50 mM TrisHCl (pH 8.0), at 37°C
0.0071
FMN
-
pH and temperature not specified in the publication, mutant D168A
0.0079
FMN
-
pH 7.1, 37°C, indirect assay
0.00823
FMN
-
mutant enzyme N210A, at 37°C in 20 mM PIPES pH 7.0, 10 mM MgCl2
0.0091
FMN
-
pH 8.0, 37°C
0.0093
FMN
-
pH and temperature not specified in the publication, mutant R297A/R300A
0.0094
FMN
-
pH 7.5, 37°C
0.0094
FMN
-
pH 7.1, 37°C
0.0095
FMN
-
pH 7.1, 37°C, direct assay
0.0101
FMN
-
pH 7.0, 25°C, recombinant wild-type enzyme
0.01501
FMN
-
mutant enzyme N210D, at 37°C in 20 mM PIPES pH 7.0, 10 mM MgCl2
0.0189
FMN
at pH 8.5; pH 8.5
0.0208
FMN
at pH 8.5; pH 8.5
0.0311
FMN
-
FADS trimer, 10 mM MgCl2 in 50 mM TrisHCl (pH 8.0), at 37°C
0.063
FMN
apparent value, in 35 mM TES (K+) buffer (pH 7.2) containing 14 mM dithiothreitol, 7 mM MgCl+, at 70°C
0.068
FMN
-
with 24 mM Na2S2O4, in 50 mM potassium phosphate (pH 7.5), at 37°C
0.109
FMN
-
without Na2S2O4, in 50 mM potassium phosphate (pH 7.5), at 37°C
0.1994
FMN
-
pH and temperature not specified in the publication, mutant W184A
additional information
additional information

-
R297A mutant protein: increased apparent KM-values for ATP and FMN by about 5 and 3times, respectively, compared to the wild-type enzyme
-
additional information
additional information
-
steady-state kinetic analysis of wild-type and mutant enzymes. The enzyme from Candida glabrata apparently binds its substrates with high affinity, but the overall turnover rate is very slow due to product inhibition
-
additional information
additional information
-
MichaelisMenten model
-
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0.006
CTP
apparent value, in 35 mM TES (K+) buffer (pH 7.2) containing 14 mM dithiothreitol, 7 mM MgCl+, at 70°C
0.6
roseoflavin mononucleotide
-
with 24 mM Na2S2O4, in 50 mM potassium phosphate (pH 7.5), at 37°C
0.16
ATP

apparent value, in 35 mM TES (K+) buffer (pH 7.2) containing 14 mM dithiothreitol, 7 mM MgCl+, at 70°C
1.1
ATP
-
FADS trimer, 10 mM MgCl2 in 50 mM TrisHCl (pH 8.0), at 37°C
2.3
ATP
-
pH 7.0, 25°C, recombinant mutant R66E
3.8
ATP
-
mutant enzyme N210D, at 37°C in 20 mM PIPES pH 7.0, 10 mM MgCl2
4.17
ATP
-
pH 7.0, 25°C, recombinant wild-type enzyme
4.2
ATP
-
FADS monomer, 10 mM MgCl2 in 50 mM TrisHCl (pH 8.0), at 37°C
4.3
ATP
-
mutant enzyme N210A, at 37°C in 20 mM PIPES pH 7.0, 10 mM MgCl2
7.3
ATP
-
mutant enzyme E268A, at 37°C in 20 mM PIPES pH 7.0, 10 mM MgCl2
7.7
ATP
-
mutant enzyme T208A, at 37°C in 20 mM PIPES pH 7.0, 10 mM MgCl2
8
ATP
-
wild type enzyme, at 37°C in 20 mM PIPES pH 7.0, 10 mM MgCl2
8.2
ATP
-
mutant enzyme E268D, at 37°C in 20 mM PIPES pH 7.0, 10 mM MgCl2
8.5
ATP
-
mutant enzyme T208D, at 37°C in 20 mM PIPES pH 7.0, 10 mM MgCl2
9
ATP
-
pH 7.0, 25°C, recombinant mutant R66A
0.0311
FMN

-
FADS trimer, 10 mM MgCl2 in 50 mM TrisHCl (pH 8.0), at 37°C
0.064
FMN
apparent value, in 35 mM TES (K+) buffer (pH 7.2) containing 14 mM dithiothreitol, 7 mM MgCl+, at 70°C
0.83
FMN
-
without Na2S2O4, in 50 mM potassium phosphate (pH 7.5), at 37°C
1.2
FMN
-
with 24 mM Na2S2O4, in 50 mM potassium phosphate (pH 7.5), at 37°C
9
FMN
-
pH 7.0, 25°C, recombinant wild-type enzyme
19.7
FMN
-
mutant enzyme N210D, at 37°C in 20 mM PIPES pH 7.0, 10 mM MgCl2
24.8
FMN
-
mutant enzyme N210A, at 37°C in 20 mM PIPES pH 7.0, 10 mM MgCl2
61.7
FMN
-
FADS monomer, 10 mM MgCl2 in 50 mM TrisHCl (pH 8.0), at 37°C
196.7
FMN
-
pH 7.0, 25°C, recombinant mutant R66E
205
FMN
-
pH 7.0, 25°C, recombinant mutant R66A
238.3
FMN
-
wild type enzyme, at 37°C in 20 mM PIPES pH 7.0, 10 mM MgCl2
270.2
FMN
-
mutant enzyme E268D, at 37°C in 20 mM PIPES pH 7.0, 10 mM MgCl2
365.7
FMN
-
mutant enzyme T208D, at 37°C in 20 mM PIPES pH 7.0, 10 mM MgCl2
369.2
FMN
-
mutant enzyme T208A, at 37°C in 20 mM PIPES pH 7.0, 10 mM MgCl2
386
FMN
-
mutant enzyme E268A, at 37°C in 20 mM PIPES pH 7.0, 10 mM MgCl2
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D168A
-
site-directed mutagenesis, the mutant shows altered kinetics compared to the wild-type enzyme
D181A
-
site-directed mutagenesis, the mutant shows reduced sensitivity to inhibition by FAD compared to the wild-type enzyme and has a much faster turnover rate than the wild-type enzyme
D66A
-
site-directed mutagenesis, inactive mutant
N62A
-
site-directed mutagenesis, the mutant shows altered kinetics compared to the wild-type enzyme
N62S
-
site-directed mutagenesis, the mutant shows altered kinetics compared to the wild-type enzyme
R297A/R300A
-
site-directed mutagenesis, the mutant shows altered kinetics compared to the wild-type enzyme
R300A
-
site-directed mutagenesis, the mutant shows 93% reduced activity compared to the wild-type enzyme
W184A
-
site-directed mutagenesis, the mutant shows altered kinetics compared to the wild-type enzyme
H28A
loss of both riboflavin kinase and FAD synthetase activities
H28D
loss of both riboflavin kinase and FAD synthetase activities
H31D
residual activity, involved in the stabilisation of the phosphate groups and the adenine moiety of ATP and the phosophate of FMN
R161A
active, residue R161 does not play a critical role in catalysis
R161D
active, residue R161 does not play a critical role in catalysis
R66A
-
site-directed mutagenesis, R66A CaFADS shows a considerable increase in the amount of oligomeric species
R66E
-
site-directed mutagenesis, R66E CaFADS shows a considerable increase in the amount of oligomeric species
R66X
-
point mutations at R66 have only mild effects on ligand binding and kinetic properties of the FMNAT-module (where R66 is located), but considerably impair the RFK activity turnover. Substitutions of R66 also modulate the ratio between monomeric and oligomeric species and modify the quaternary arrangement observed by single-molecule methods
S164A
residual activity, involved in the stabilisation of the phosphate groups and the adenine moiety of ATP and the phosophate of FMN
S164D
residual activity, involved in the stabilisation of the phosphate groups and the adenine moiety of ATP and the phosophate of FMN
T165A
residual activity, involved in the stabilisation of the phosphate groups and the adenine moiety of ATP and the phosophate of FMN
T165D
residual activity, involved in the stabilisation of the phosphate groups and the adenine moiety of ATP and the phosophate of FMN
C126S
the mutation does not reduce the protein's heat stability or solubility, the mutant contains less than 0.8 and less than 0.08 mol of Mg and Fe per protomer. In the presence of MgCl2, the mutant has activity about 2times higher than that of the wild type enzyme. The activity of the mutant in presence of Co2+ is very low
C143S
the mutation does not reduce the protein's heat stability or solubility, the mutant contains less than 0.8 and less than 0.08 mol of Mg and Fe per protomer. In the presence of MgCl2, the mutant has activity approximately wild type activity. The activity of the mutant in presence of Co2+ is very low
R297A

-
involved in substrate binding
R297A
-
site-directed mutagenesis, the mutant shows a 2fold increased activity compared to the wild-type enzyme
E268A

active, involved in riboflavin kinase activity
E268A
-
the mutant shows increased catalytic efficiency for FMN and reduced catalytic efficiency for ATP compared to the wild type enzyme
E268D

active, involved in riboflavin kinase activity
E268D
-
the mutant shows about wild type catalytic efficiencies for ATP and FMN
N210A

active, involved in riboflavin kinase activity
N210A
-
the mutant shows strongly reduced catalytic efficiencies for FMN and ATP compared to the wild type enzyme
N210D

active, involved in riboflavin kinase activity
N210D
-
the mutant shows strongly reduced catalytic efficiencies for FMN and ATP compared to the wild type enzyme
T208A

active, involved in riboflavin kinase activity
T208A
-
the mutant shows increased catalytic efficiency for FMN and reduced catalytic efficiency for ATP compared to the wild type enzyme
T208D

active, involved in riboflavin kinase activity
T208D
-
the mutant shows increased catalytic efficiency for FMN and increased catalytic efficiency for ATP compared to the wild type enzyme
additional information

-
recombinant protein has FAD synthetase activity, but not riboflavin kinase activity; recombinant protein has FAD synthetase activity, but not riboflavin kinase activity
additional information
recombinant protein has FAD synthetase activity, but not riboflavin kinase activity; recombinant protein has FAD synthetase activity, but not riboflavin kinase activity
additional information
recombinant protein has FAD synthetase activity, but not riboflavin kinase activity; recombinant protein has FAD synthetase activity, but not riboflavin kinase activity
additional information
recombinant protein has FAD synthetase activity, but not riboflavin kinase activity; recombinant protein has FAD synthetase activity, but not riboflavin kinase activity
additional information
-
C-terminal domain delta(1-182)
additional information
-
engineering of the FAD synthetase from Corynebacterium ammoniagenes by deleting its N-terminal adenylation domain leads to a biocatalyst that is stable and efficient for direct and quantitative phosphorylation of riboflavin and riboflavin analogues to their corresponding FMN cofactors at preparative-scale. Deletion of the N-terminal adenosyl transfer domain in the truncated C-terminal RF kinase domain, tcRFK, variants results in a drop in the TM value from 40°C (parental CaFADS) to 35°C for tcRFK. Addition of the C-terminal poly-His tag further reduces the TM to 30°C, presumably due to the conformationally flexible tail formed by the extra amino acids
additional information
-
functional expression does not confer roseoflavin resistance to a FAD-synthetase defective Bacillus subtilis strain
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Aggressive Periodontitis
[Association between FADS1 rs174537 polymorphism and serum proteins in patients with aggressive periodontitis].
Asthma
FADS gene cluster modulates the effect of breastfeeding on asthma. Results from the GINIplus and LISAplus studies.
Carcinogenesis
Decreased Expression of FADS1 Predicts a Poor Prognosis in Patients with Esophageal Squamous Cell Carcinoma.
Carcinoma
Decreased Expression of FADS1 Predicts a Poor Prognosis in Patients with Esophageal Squamous Cell Carcinoma.
Cardiovascular Diseases
Fatty acid desaturase 1 knockout mice are lean with improved glycemic control and decreased development of atheromatous plaque.
Cardiovascular Diseases
Genetic variation in FADS1 has little effect on the association between dietary PUFA intake and cardiovascular disease.
Cardiovascular Diseases
[Desaturases of fatty acids (FADS) and their physiological and clinical implication].
Coronary Artery Disease
Polymorphisms in FADS1 and FADS2 alter plasma fatty acids and desaturase levels in type 2 diabetic patients with coronary artery disease.
Coronary Disease
Genetic variants in the metabolism of omega-6 and omega-3 fatty acids: their role in the determination of nutritional requirements and chronic disease risk.
Diabetes Mellitus, Type 2
Effects of 34 Risk Loci for Type 2 Diabetes or Hyperglycemia on Lipoprotein Subclasses and Their Composition in 6,580 Nondiabetic Finnish Men.
Diabetes Mellitus, Type 2
FADS Gene Polymorphisms, Fatty Acid Desaturase Activities, and HDL-C in Type 2 Diabetes.
Diabetes, Gestational
GCK, GCKR, FADS1, DGKB/TMEM195 and CDKAL1 Gene Polymorphisms in Women with Gestational Diabetes.
Dyslipidemias
Interaction between a common variant in FADS1 and erythrocyte polyunsaturated fatty acids on lipid profile in Chinese Hans.
Eczema
Variants of the FADS1 FADS2 gene cluster, blood levels of polyunsaturated fatty acids and eczema in children within the first 2 years of life.
Esophageal Squamous Cell Carcinoma
Decreased Expression of FADS1 Predicts a Poor Prognosis in Patients with Esophageal Squamous Cell Carcinoma.
Fatty Liver
Fads1 and 2 are promoted to meet instant need for long-chain polyunsaturated fatty acids in goose fatty liver.
Hyperglycemia
Effects of 34 Risk Loci for Type 2 Diabetes or Hyperglycemia on Lipoprotein Subclasses and Their Composition in 6,580 Nondiabetic Finnish Men.
Hypersensitivity
[Desaturases of fatty acids (FADS) and their physiological and clinical implication].
Hypertension
A case-control study between gene polymorphisms of polyunsaturated fatty acid metabolic rate-limiting enzymes and acute coronary syndrome in Chinese Han population.
Hypertension
[Desaturases of fatty acids (FADS) and their physiological and clinical implication].
Infection
Flavin metabolism during respiratory infection in mice.
Insulin Resistance
Abnormal Expression of Genes Involved in Inflammation, Lipid Metabolism, and Wnt Signaling in the Adipose Tissue of Polycystic Ovary Syndrome.
Insulin Resistance
Fatty Acid desaturase gene polymorphisms and metabolic measures in schizophrenia and bipolar patients taking antipsychotics.
Insulin Resistance
Gene Expression Signature in Adipose Tissue of Acromegaly Patients.
Insulin Resistance
Genetic loci associated with lipid concentrations and cardiovascular risk factors in a Korean population.
Lung Neoplasms
Reduced Expression of FADS1 Predicts Worse Prognosis in Non-Small-Cell Lung Cancer.
Metabolic Syndrome
[Desaturases of fatty acids (FADS) and their physiological and clinical implication].
Mouth Neoplasms
FADS1 rs174549 Polymorphism May Predict a Favorable Response to Chemoradiotherapy in Oral Cancer Patients.
Mouth Neoplasms
Novel polymorphism in FADS1 gene and fish consumption on risk of oral cancer: A case-control study in southeast China.
Neoplasms
Decreased Expression of FADS1 Predicts a Poor Prognosis in Patients with Esophageal Squamous Cell Carcinoma.
Neoplasms
Genetic variation of the FADS1 FADS2 gene cluster and n-6 PUFA composition in erythrocyte membranes in the European Prospective Investigation into Cancer and Nutrition-Potsdam study.
Neoplasms
Reduced Expression of FADS1 Predicts Worse Prognosis in Non-Small-Cell Lung Cancer.
Neoplasms
[Desaturases of fatty acids (FADS) and their physiological and clinical implication].
Obesity
Association of variations in the FTO, SCG3 and MTMR9 genes with metabolic syndrome in a Japanese population.
Obesity
Fatty acid desaturase 1 knockout mice are lean with improved glycemic control and decreased development of atheromatous plaque.
Obesity
Gene-diet interaction of a common FADS1 variant with marine polyunsaturated fatty acids for fatty acid composition in plasma and erythrocytes among men.
Riboflavin Deficiency
Effect of riboflavin status on hepatic activities of flavin-metabolizing enzymes in rats.
Stomach Neoplasms
Chemical genomic screening for methylation-silenced genes in gastric cancer cell lines using 5-aza-2'-deoxycytidine treatment and oligonucleotide microarray.
Stomach Neoplasms
Dietary n-3 and n-6 polyunsaturated fatty acids, the FADS gene, and the risk of gastric cancer in a Korean population.
Stroke
Genetic variation in FADS1 has little effect on the association between dietary PUFA intake and cardiovascular disease.
Vascular System Injuries
Fatty acid desaturase 1 knockout mice are lean with improved glycemic control and decreased development of atheromatous plaque.
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