Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
-
-
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
-
-
-
?
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
-
-
-
?
ATP + FMN
diphosphate + FAD
-
-
-
-
?
ATP + FMN
diphosphate + FAD
-
-
-
r
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 + 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
-
-
-
-
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 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
?
-
-
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
?
-
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
?
-
-
enzyme contains an N-terminal molybdopterin-binding resembling domain with FAD hydrolytic activity in presence of both Co2+ and chemical mercurial reagents
-
-
-
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
-
-
?
additional information
?
-
-
FADS catalyzes the activities of riboflavin kinase (RFK, EC 2.7.1.26), TP:FMN:adenylyltransferase (FMNAT), and FAD diphosphorylase (FADpp). The FMNAT and FADSpp activities require flavin substrates in the reduced state and binding of adenine nucleotide ligands is required for the binding of flavinic substrates/products. FADS does not bind oxidized flavins by itself
-
-
-
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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
0.042 - 0.114
diphosphate
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
0.00691
ATP
pH 7.5, 37°C
0.009
ATP
mutant F128W, pH 7.0, 25°C
0.0095
ATP
mutant V300K, pH 7, 25°C
0.0104
ATP
mutant D298E, pH 7, 25°C
0.0108
ATP
mutant E203A, pH 7, 25°C
0.0115
ATP
mutant L304K, pH 7, 25°C
0.0121
ATP
mutant K202A, pH 7, 25°C
0.0153
ATP
at 37°C, in 50 mM Tris-HCl, pH 7.5
0.0153
ATP
mutant E301K, pH 7, 25°C
0.0158
ATP
pH 7.0, 25°C, recombinant mutant R66A
0.019
ATP
mutant Y106W, pH 7.0, 25°C
0.0197
ATP
mutant E301A, pH 7, 25°C
0.0207
ATP
mutant D298A, pH 7, 25°C
0.0224
ATP
wild-type, pH 7, 25°C
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
0.0252
ATP
mutant F206W, pH 7, 25°C
0.0311
ATP
pH 7.0, 25°C, recombinant mutant R66E
0.0316
ATP
-
pH 7.0, 25°C
0.0347
ATP
mutant EL04A, pH 7, 25°C
0.03568
ATP
-
wild type enzyme, at 37°C in 20 mM PIPES pH 7.0, 10 mM MgCl2
0.038
ATP
mutant F206A, pH 7, 25°C
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
0.0388
ATP
mutant F206K, pH 7, 25°C
0.043
ATP
wild-type, pH 7.0, 25°C
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
0.0462
ATP
mutant V300A, pH 7, 25°C
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
0.051
ATP
mutant F62W, pH 7.0, 25°C
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
0.121
ATP
pH not specified in the publication, temperature not specified in the publication
0.042
diphosphate
pH 7.5, 37°C
0.114
diphosphate
-
pH 7.6, 25°C
0.00013
FMN
pH 7.5, 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
0.00042
FMN
mutant E301A, pH 7, 25°C
0.0005
FMN
pH and temperature not specified in the publication, mutant N62A
0.00069
FMN
pH 7.0, 25°C, recombinant mutant R66A
0.0007
FMN
mutant E203A, pH 7, 25°C
0.00085
FMN
mutant E301K, pH 7, 25°C
0.00088
FMN
-
mutant enzyme E268A, at 37°C in 20 mM PIPES pH 7.0, 10 mM MgCl2
0.00088
FMN
-
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
0.00095
FMN
mutant D298E, pH 7, 25°C
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
0.0012
FMN
mutant D298A, pH 7, 25°C
0.0014
FMN
mutant V300A, pH 7, 25°C
0.0015
FMN
pH and temperature not specified in the publication, mutant D181A
0.0017
FMN
mutant F206W, pH 7, 25°C
0.0023
FMN
pH and temperature not specified in the publication, mutant R300A
0.0028
FMN
mutant EL04A, pH 7, 25°C
0.0029
FMN
mutant F206A, pH 7, 25°C
0.0029
FMN
mutant K202A, pH 7, 25°C
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
0.0054
FMN
mutant F206K, pH 7, 25°C
0.006
FMN
wild-type, pH 7.0, 25°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
0.0083
FMN
mutant V300K, pH 7, 25°C
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
0.0098
FMN
-
pH 7.0, 25°C
0.0101
FMN
wild-type, pH 7, 25°C
0.0101
FMN
pH 7.0, 25°C, recombinant wild-type enzyme
0.012
FMN
mutant Y106W, pH 7.0, 25°C
0.01501
FMN
-
mutant enzyme N210D, at 37°C in 20 mM PIPES pH 7.0, 10 mM MgCl2
0.0152
FMN
mutant L304K, pH 7, 25°C
0.0311
FMN
-
FADS trimer, 10 mM MgCl2 in 50 mM TrisHCl (pH 8.0), at 37°C
0.042
FMN
mutant F62W, pH 7.0, 25°C
0.047
FMN
pH not specified in the publication, temperature not specified in the publication
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
0.108
FMN
mutant F128W, pH 7.0, 25°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
MichaelisMenten model
-
additional information
additional information
-
MichaelisMenten model
-
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
D298A
mutation at the macromolecular interface between two protomers within the trimer
D298E
mutation at the macromolecular interface between two protomers within the trimer
E203A
mutation at the macromolecular interface between two protomers within the trimer
E301A
mutation at the macromolecular interface between two protomers within the trimer
E301K
mutation at the macromolecular interface between two protomers within the trimer
F128A
loss of NMNAT activity
F128K
loss of NMNAT activity
F128W
mutant retains NMNAT activity
F206A
mutation at the macromolecular interface between two protomers within the trimer
F206K
mutation at the macromolecular interface between two protomers within the trimer
F206W
mutation at the macromolecular interface between two protomers within the trimer
F62A
loss of NMNAT activity
F62K
loss of NMNAT activity
F62W
mutant retains NMNAT activity
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
K202A
mutation at the macromolecular interface between two protomers within the trimer
L304K
mutation at the macromolecular interface between two protomers within the trimer
L98A
mutation totally prevents the binding of FMN and/or FAD. Residues P56, P58 and L98 shape the isoalloxazine site to place the FMN- and FAD-reacting phosphates in optimal geometry for catalysis
L98K
mutation totally prevents the binding of FMN and/or FAD. Residues P56, P58 and L98 shape the isoalloxazine site to place the FMN- and FAD-reacting phosphates in optimal geometry for catalysis
L98W
residues P56, P58 and L98 shape the isoalloxazine site to place the FMN- and FAD-reacting phosphates in optimal geometry for catalysis
P56A/P58A
variant exhibits lower KdATP values and altered thermodynamic profile for ATP binding. Residues P56, P58 and L98 shape the isoalloxazine site to place the FMN- and FAD-reacting phosphates in optimal geometry for catalysis
P56W
variant exhibits lower KdATP values and altered thermodynamic profile for ATP binding. Residues P56, P58 and L98 shape the isoalloxazine site to place the FMN- and FAD-reacting phosphates in optimal geometry for catalysis
P58W
residues P56, P58 and L98 shape the isoalloxazine site to place the FMN- and FAD-reacting phosphates in optimal geometry for catalysis
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
V300A
mutation at the macromolecular interface between two protomers within the trimer
V300K
mutation at the macromolecular interface between two protomers within the trimer
Y106A
loss of NMNAT activity
Y106K
loss of NMNAT activity
Y106W
mutant retains NMNAT activity
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
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
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
R297A
involved in substrate binding
R297A
site-directed mutagenesis, the mutant shows a 2fold increased activity compared to the wild-type enzyme
additional information
recombinant protein has FAD synthetase activity, but not riboflavin kinase activity
additional information
recombinant protein has FAD synthetase activity, but not riboflavin kinase activity
additional information
recombinant protein has FAD synthetase activity, but not riboflavin kinase activity
additional information
-
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Yamada, Y.; Merrill, A.; McCormick, D.N.
Probable reaction mechanisms of flavokinase and FAD synthetase from rat liver
Arch. Biochem. Biophys.
278
125-130
1990
Rattus norvegicus
brenda
Mack, M.; van Loon, A.P.; Hohmann, H.P.
Regulation of riboflavin biosynthesis in Bacillus subtilis is affected by the activity of the flavokinase/flavin adenine dinucleotide synthetase encoded by ribC
J. Bacteriol.
180
950-955
1998
Bacillus subtilis (P54575), Bacillus subtilis, Bacillus subtilis 168 (P54575)
brenda
Schrecker, A.W.; Kornberg, A.
Reversible enzymatic synthesis of flavin-adenine dinucleotide
J. Biol. Chem.
182
795-803
1950
Saccharomyces cerevisiae
brenda
Gomes, B.; McCormick, D.B.
Purification and general characterization of FAD synthetase from rat liver
Proc. Soc. Exp. Biol. Med.
172
250-254
1983
Rattus norvegicus
brenda
Oka, M.; McCormick, D.B.
Complete purification and general characterization of FAD synthetase from rat liver
J. Biol. Chem.
262
7418-7422
1987
Rattus norvegicus
brenda
Bowers-Komro, D.; Yamada, Y.; McCormick, D.B.
Substrate specificity and variables affecting efficiency of mammalian flavin adenine dinucleotide synthetase
Biochemistry
28
8439-8446
1989
Rattus norvegicus
brenda
Hartman, H.A.; Edmondson, D.E.; McCormick, D.B.
Riboflavin 5-pyrophosphate: a contaminant of commercial FAD, a coenzyme for FAD-dependent oxidases, and an inhibitor of FAD synthetase
Anal. Biochem.
202
348-355
1992
Bos taurus
brenda
Hagihara, T.; Fujio, T.; Aisaka, K.
Cloning of FAD synthetase gene from Corynebacterium ammoniagenes and its application to FAD and FMN production
Appl. Microbiol. Biotechnol.
42
724-729
1995
Corynebacterium ammoniagenes
brenda
Nakagawa, S.; Igarashi, A.; Ohta, T.; Hagihara, T.; Fujio, T.; Aisaka, K.
Nucleotide sequence of the FAD synthetase gene from Corynebacterium ammoniagenes and its expression in Escherichia coli
Biosci. Biotechnol. Biochem.
59
694-702
1995
Corynebacterium ammoniagenes, Corynebacterium ammoniagenes (Q59263), Corynebacterium ammoniagenes ATCC 6872
brenda
Wu, M.; Repetto, B.; Glerum, D.M.; Tzagoloff, A.
Cloning and characterization of FAD1, the structural gene for flavin adenine dinucleotide synthetase of Saccharomyces cerevisiae
Mol. Cell. Biol.
15
264-271
1995
Saccharomyces cerevisiae, Saccharomyces cerevisiae (P38913)
brenda
McCormick, D.B.; Oka, M.; Bowers-Komro, D.M.; Yamada, Y.; Hartman, H.A.
Purification and properties of FAD synthetase from liver
Methods Enzymol.
280
407-413
1997
Bos taurus, Corynebacterium ammoniagenes, Rattus norvegicus
brenda
Efimov, I.; Kuusk, V.; Zhang, X.; McIntire, W.S.
Proposed steady-state kinetic mechanism for Corynebacterium ammoniagenes FAD synthetase produced by Escherichia coli
Biochemistry
37
9716-9723
1998
Corynebacterium ammoniagenes
brenda
Krupa, A.; Sandhya, K.; Srinivasan, N.; Jonnalagadda, S.
A conserved domain in prokaryotic bifunctional FAD synthetases can potentially catalyze nucleotide transfer
Trends Biochem. Sci.
28
9-12
2003
Corynebacterium ammoniagenes
brenda
Wang, W.; Kim, R.; Yokota, H.; Kim, S.H.
Crystal structure of flavin binding to FAD synthetase of Thermotoga maritima
Proteins Struct. Funct. Bioinform.
58
246-248
2004
Thermotoga maritima, Thermotoga maritima TM379
-
brenda
Brizio, C.; Galluccio, M.; Wait, R.; Torchetti, E.M.; Bafunno, V.; Accardi, R.; Gianazza, E.; Indiveri, C.; Barile, M.
Over-expression in Escherichia coli and characterization of two recombinant isoforms of human FAD synthetase
Biochem. Biophys. Res. Commun.
344
1008-1016
2006
Homo sapiens (Q8NFF5), Homo sapiens
brenda
Galluccio, M.; Brizio, C.; Torchetti, E.M.; Ferranti, P.; Gianazza, E.; Indiveri, C.; Barile, M.
Over-expression in Escherichia coli, purification and characterization of isoform 2 of human FAD synthetase
Protein Expr. Purif.
52
175-181
2007
Homo sapiens (Q8NFF5), Homo sapiens
brenda
Grill, S.; Busenbender, S.; Pfeiffer, M.; Koehler, U.; Mack, M.
The bifunctional flavokinase/flavin adenine dinucleotide synthetase from Streptomyces davawensis produces inactive flavin cofactors and is not involved in resistance to the antibiotic roseoflavin
J. Bacteriol.
190
1546-1553
2008
Streptomyces davaonensis
brenda
Frago, S.; Martinez-Julvez, M.; Serrano, A.; Medina, M.
Structural analysis of FAD synthetase from Corynebacterium ammoniagenes
BMC Microbiol.
8
160
2008
Corynebacterium ammoniagenes (Q59263)
brenda
Sandoval, F.J.; Zhang, Y.; Roje, S.
Flavin nucleotide metabolism in plants: monofunctional enzymes synthesize FAD in plastids
J. Biol. Chem.
283
30890-30900
2008
Arabidopsis thaliana (Q0WS47), Arabidopsis thaliana (Q8VZR0), Arabidopsis thaliana (Q9FMW8), Arabidopsis thaliana
brenda
Herguedas, B.; Martinez-Julvez, M.; Frago, S.; Medina, M.; Hermoso, J.A.
Crystallization and preliminary X-ray diffraction studies of FAD synthetase from Corynebacterium ammoniagenes
Acta Crystallogr. Sect. F
65
1285-1288
2009
Corynebacterium ammoniagenes
brenda
Giancaspero, T.A.; Locato, V.; de Pinto, M.C.; De Gara, L.; Barile, M.
The occurrence of riboflavin kinase and FAD synthetase ensures FAD synthesis in tobacco mitochondria and maintenance of cellular redox status
FEBS J.
276
219-231
2009
Nicotiana tabacum
brenda
Frago, S.; Velazquez-Campoy, A.; Medina, M.
The puzzle of ligand binding to Corynebacterium ammoniagenes FAD synthetase
J. Biol. Chem.
284
6610-6619
2009
Corynebacterium ammoniagenes
brenda
Huerta, C.; Borek, D.; Machius, M.; Grishin, N.V.; Zhang, H.
Structure and mechanism of a eukaryotic FMN adenylyltransferase
J. Mol. Biol.
389
388-400
2009
[Candida] glabrata (Q6FNA9)
brenda
Torchetti, E.M.; Brizio, C.; Colella, M.; Galluccio, M.; Giancaspero, T.A.; Indiveri, C.; Roberti, M.; Barile, M.
Mitochondrial localization of human FAD synthetase isoform 1
Mitochondrion
10
263-273
2010
Homo sapiens (Q8NFF5), Homo sapiens
brenda
Pedrolli, D.B.; Nakanishi, S.; Barile, M.; Mansurova, M.; Carmona, E.C.; Lux, A.; Gaertner, W.; Mack, M.
The antibiotics roseoflavin and 8-demethyl-8-amino-riboflavin from Streptomyces davawensis are metabolized by human flavokinase and human FAD synthetase
Biochem. Pharmacol.
82
1853-1859
2011
Homo sapiens
brenda
Mashhadi, Z.; Xu, H.; Grochowski, L.L.; White, R.H.
Archaeal RibL: a new FAD synthetase that is air sensitive
Biochemistry
49
8748-8755
2010
Methanocaldococcus jannaschii (Q58579), Methanocaldococcus jannaschii
brenda
Marcuello, C.; Arilla-Luna, S.; Medina, M.; Lostao, A.
Detection of a quaternary organization into dimer of trimers of Corynebacterium ammoniagenes FAD synthetase at the single-molecule level and at the in cell level
Biochim. Biophys. Acta
1834
665-676
2013
Corynebacterium ammoniagenes (Q59263)
brenda
Serrano, A.; Frago, S.; Herguedas, B.; Martinez-Julvez, M.; Velazquez-Campoy, A.; Medina, M.
Key residues at the riboflavin kinase catalytic site of the bifunctional riboflavin kinase/FMN adenylyltransferase from Corynebacterium ammoniagenes
Cell Biochem. Biophys.
65
57-68
2013
Corynebacterium ammoniagenes
brenda
Torchetti, E.; Bonomi, F.; Galluccio, M.; Gianazza, E.; Giancaspero, T.; Iametti, S.; Indiveri, C.; Barile, M.
Human FAD synthase (isoform 2): A component of the machinery that delivers FAD to apo-flavoproteins
FEBS J.
278
4435-4449
2011
Homo sapiens (Q8NFF5)
-
brenda
Leulliot, N.; Blondeau, K.; Keller, J.; Ulryck, N.; Quevillon-Cheruel, S.; van Tilbeurgh, H.
Crystal structure of yeast FAD synthetase (Fad1) in complex with FAD
J. Mol. Biol.
398
641-646
2010
Saccharomyces cerevisiae (P38913)
brenda
Herguedas, B.; Martinez-Julvez, M.; Frago, S.; Medina, M.; Hermoso, J.A.
Oligomeric state in the crystal structure of modular FAD synthetase provides insights into its sequential catalysis in prokaryotes
J. Mol. Biol.
400
218-230
2010
Corynebacterium ammoniagenes
brenda
Herguedas, B.; Lans, I.; Sebastian, M.; Hermoso, J.A.; Martinez-Julvez, M.; Medina, M.
Structural insights into the synthesis of FMN in prokaryotic organisms
Acta Crystallogr. Sect. D
71
2526-2542
2015
Corynebacterium ammoniagenes (Q59263)
brenda
Huerta, C.; Grishin, N.V.; Zhang, H.
The super mutant of yeast FMN adenylyltransferase enhances the enzyme turnover rate by attenuating product inhibition
Biochemistry
52
3615-3617
2013
[Candida] glabrata (Q6FNA9)
brenda
Serrano, A.; Sebastian, M.; Arilla-Luna, S.; Baquedano, S.; Pallares, M.C.; Lostao, A.; Herguedas, B.; Velazquez-Campoy, A.; Martinez-Julvez, M.; Medina, M.
Quaternary organization in a bifunctional prokaryotic FAD synthetase: Involvement of an arginine at its adenylyltransferase module on the riboflavin kinase activity
Biochim. Biophys. Acta
1854
897-906
2015
Corynebacterium ammoniagenes (Q59263), Corynebacterium ammoniagenes
brenda
Giancaspero, T.A.; Busco, G.; Panebianco, C.; Carmone, C.; Miccolis, A.; Liuzzi, G.M.; Colella, M.; Barile, M.
FAD synthesis and degradation in the nucleus create a local flavin cofactor pool
J. Biol. Chem.
288
29069-29080
2013
Rattus norvegicus (D4A4P4), Rattus norvegicus Wistar (D4A4P4)
brenda
Iamurri, S.M.; Daugherty, A.B.; Edmondson, D.E.; Lutz, S.
Truncated FAD synthetase for direct biocatalytic conversion of riboflavin and analogs to their corresponding flavin mononucleotides
Protein Eng. Des. Sel.
26
791-795
2013
Corynebacterium ammoniagenes (Q59263)
brenda
Sebastian, M.; Serrano, A.; Velazquez-Campoy, A.; Medina, M.
Kinetics and thermodynamics of the protein-ligand interactions in the riboflavin kinase activity of the FAD synthetase from Corynebacterium ammoniagenes
Sci. Rep.
7
7281
2017
Corynebacterium ammoniagenes (Q59263), Corynebacterium ammoniagenes
brenda
Lans, I.; Seco, J.; Serrano, A.; Burbano, R.; Cossio, P.; Daza, M.C.; Medina, M.
The dimer-of-trimers assembly prevents catalysis at the transferase site of prokaryotic FAD synthase
Biophys. J.
115
988-995
2018
Corynebacterium ammoniagenes (Q59263), Corynebacterium ammoniagenes
brenda
Leone, P.; Galluccio, M.; Brizio, C.; Barbiroli, A.; Iametti, S.; Indiveri, C.; Barile, M.
The hidden side of the human FAD synthase 2
Int. J. Biol. Macromol.
138
986-995
2019
Homo sapiens
brenda
Arilla-Luna, S.; Serrano, A.; Medina, M.
Specific features for the competent binding of substrates at the FMN adenylyltransferase site of FAD synthase from Corynebacterium ammoniagenes
Int. J. Mol. Sci.
20
5083
2019
Corynebacterium ammoniagenes (Q59263), Corynebacterium ammoniagenes
brenda
Serrano, A.; Arilla-Luna, S.; Medina, M.
Insights into the fmnat active site of FAD synthase Aromaticity is essential for flavin binding and catalysis
Int. J. Mol. Sci.
21
3738
2020
Corynebacterium ammoniagenes (Q59263), Corynebacterium ammoniagenes
brenda
Liu, S.; Diao, N.; Wang, Z.; Lu, W.; Tang, Y.J.; Chen, T.
Modular engineering of the flavin pathway in Escherichia coli for improved flavin mononucleotide and flavin adenine dinucleotide production
J. Agric. Food Chem.
67
6532-6540
2019
Escherichia coli (P0AG40)
brenda
Leone, P.; Galluccio, M.; Barbiroli, A.; Eberini, I.; Tolomeo, M.; Vrenna, F.; Gianazza, E.; Iametti, S.; Bonomi, F.; Indiveri, C.; Barile, M.
Bacterial production, characterization and protein modeling of a novel monofuctional isoform of FAD synthase in humans An emergency protein?
Molecules
23
116
2018
Homo sapiens (Q8NFF5), Homo sapiens
brenda
Lans, I.; Anoz-Carbonell, E.; Palacio-Rodriguez, K.; Ainsa, J.A.; Medina, M.; Cossio, P.
In silico discovery and biological validation of ligands of FAD synthase, a promising new antimicrobial target
PLoS Comput. Biol.
16
e1007898
2020
Corynebacterium ammoniagenes (Q59263), Corynebacterium ammoniagenes
brenda
Zhou, G.; Pan, Q.; Hu, Z.; Qiu, J.; Yu, Z.
Heterologous expression and characterization of flavinadenine dinucleotide synthetase from Candida famata for flavin adenine dinucleotide production
Protein Pept. Lett.
28
229-239
2020
Debaryomyces hansenii (A0A5J6E2Y6)
brenda
Serrano, A.; Sebastian, M.; Arilla-Luna, S.; Baquedano, S.; Herguedas, B.; Velazquez-Campoy, A.; Martinez-Julvez, M.; Medina, M.
The trimer interface in the quaternary structure of the bifunctional prokaryotic FAD synthetase from Corynebacterium ammoniagenes
Sci. Rep.
7
404
2017
Corynebacterium ammoniagenes (Q59263)
brenda
Sebastian, M.; Lira-Navarrete, E.; Serrano, A.; Marcuello, C.; Velazquez-Campoy, A.; Lostao, A.; Hurtado-Guerrero, R.; Medina, M.; Martinez-Julvez, M.
The FAD synthetase from the human pathogen Streptococcus pneumoniae a bifunctional enzyme exhibiting activity-dependent redox requirements
Sci. Rep.
7
7609
2017
Streptococcus pneumoniae
brenda