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Information on EC 2.7.7.2 - FAD synthase
for references in articles please use BRENDA:EC2.7.7.2
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EC Tree 2 Transferases
2.7 Transferring phosphorus-containing groups
2.7.7 Nucleotidyltransferases
2.7.7.2 FAD synthase
IUBMB Comments
Requires Mg2+ and is highly specific for ATP as phosphate donor . 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 . While monofunctional FAD synthetase is found in eukaryotes and in some prokaryotes, most prokaryotes have a bifunctional enzyme that exhibits both this activity and that of EC 2.7.1.26, riboflavin kinase [3,5].
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
- 2.7.7.2
-
desaturase
-
polyunsaturated
-
arachidonic
-
docosahexaenoic
-
linoleic
-
eicosapentaenoic
-
desaturation
- elongase
-
elovl2
-
omega-6
-
delta-5
-
lcpufas
- ammoniagenes
-
srebf1
-
gene-diet
- flavokinase
- synthesis
- nutrition
showSynonyms
fads1, flad1, fad synthase, fad pyrophosphorylase, flavin adenine dinucleotide synthetase, atribf1, atribf2, atp:fmn adenylyltransferase, mj1179, fmn:atp adenylyltransferase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
adenosine triphosphate-riboflavin mononucleotide transadenylase
-
-
-
-
adenosine triphosphate-riboflavine mononucleotide transadenylase
-
-
-
-
FAD pyrophosphorylase
-
-
-
-
FAD synthase
FAD synthetase
FADS
FADS2
FMN adenylyltransferase
FMN pyrophosphorylase
-
-
-
-
FMNAT
lysZ
-
-
-
-
ribF
riboflavin adenine dinucleotide pyrophosphorylase
-
-
-
-
riboflavin mononucleotide adenylyltransferase
-
-
-
-
riboflavine adenine dinucleotide adenylyltransferase
-
-
-
-
additional information
FMN adenylyltransferase
-
-
-
-
additional information
-
bifunctional enzyme with EC 2.7.1.26 and EC 2.7.7.2 activity
additional information
-
bifunctional enzyme with EC 2.7.1.26 and EC 2.7.7.2 activity
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + FMN = diphosphate + FAD
-
-
-
-
ATP + FMN = diphosphate + FAD
product release may be the rate-limiting step of the reaction
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
nucleotidyl group transfer
nucleotidyl group transfer
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
flavin biosynthesis I (bacteria and plants), flavin biosynthesis II (archaea), flavin biosynthesis III (fungi), flavin salvage
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SYSTEMATIC NAME
IUBMB Comments
ATP:FMN adenylyltransferase
Requires Mg2+ and is highly specific for ATP as phosphate donor [5]. 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 [3]. While monofunctional FAD synthetase is found in eukaryotes and in some prokaryotes, most prokaryotes have a bifunctional enzyme that exhibits both this activity and that of EC 2.7.1.26, riboflavin kinase [3,5].
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CAS REGISTRY NUMBER
COMMENTARY
9026-37-3
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + 4'-butyl-FMN
diphosphate + 4'-butylflavin adenine dinucleotide
-
Substrates: -
Products: -
Products: -
?
ATP + 5'-pentyl-FMN
diphosphate + 5'-pentylflavin adenine dinucleotide
-
Substrates: -
Products: -
Products: -
?
ATP + 7,8-dibromo-FMN
diphosphate + 7,8-dibromoflavin adenine dinucleotide
-
Substrates: -
Products: -
Products: -
?
ATP + 7,8-dichloro-FMN
diphosphate + 7,8-dichloroflavin adenine dinucleotide
-
Substrates: -
Products: -
Products: -
?
ATP + 7-chloro-FMN
diphosphate + 7-chloroflavin adenine dinucleotide
-
Substrates: -
Products: -
Products: -
?
ATP + 8-chloro-FMN
diphosphate + 8-chloroflavin adenine dinucleotide
-
Substrates: -
Products: -
Products: -
?
ATP + iso-FMN
diphosphate + isoflavin adenine dinucleotide
-
Substrates: -
Products: -
Products: -
?
ATP + roseoflavin mononucleotide
diphosphate + roseoflavin adenine dinucleotide
-
Substrates: -
Products: -
Products: -
?
CTP + FMN
diphosphate + flavin cytidine dinucleotide
Substrates: -
Products: -
Products: -
?
GTP + FMN
diphosphate + flavin guanidine dinucleotide
Substrates: weak specific activity
Products: -
Products: -
?
ATP + FMN
diphosphate + FAD
Substrates: -
Products: -
Products: -
?
ATP + FMN
diphosphate + FAD
Substrates: essential for flavin metabolism
Products: -
Products: -
r
ATP + FMN
diphosphate + FAD
-
Substrates: -
Products: -
Products: -
r
ATP + FMN
diphosphate + FAD
-
Substrates: -
Products: -
Products: -
r
ATP + FMN
diphosphate + FAD
-
Substrates: 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
Products: -
Products: -
r
ATP + FMN
diphosphate + FAD
-
Substrates: catalyzes 2 sequential steps in the biosynthesis of FAD, phosphorylation of riboflavin to produce FMN and subsequent adenylylation of FMN to form FAD
Products: -
Products: -
r
ATP + FMN
diphosphate + FAD
Substrates: engineered mutant
Products: -
Products: -
?
ATP + FMN
diphosphate + FAD
Substrates: -
Products: -
Products: -
?
ATP + FMN
diphosphate + FAD
Substrates: -
Products: -
Products: -
?
ATP + FMN
diphosphate + FAD
-
Substrates: -
Products: -
Products: -
r
ATP + FMN
diphosphate + FAD
Substrates: the enzyme does not catalyze the reverse reaction to produce FMN and ATP from FAD and diphosphate
Products: -
Products: -
ir
ATP + FMN
diphosphate + FAD
-
Substrates: essentially irreversible in the direction of FAD formation
Products: -
Products: -
ir
ATP + FMN
diphosphate + FAD
-
Substrates: biosynthesis of FAD is most likely regulated by this coenzyme as a product at the stage of FAD synthetase reaction
Products: -
Products: -
?
ATP + FMN
diphosphate + FAD
-
Substrates: biosynthesis of FAD is most likely regulated by this coenzyme as a product at the stage of FAD synthetase reaction
Products: -
Products: -
ir
additional information
?
-
Substrates: bifunctional FAD synthetase which shows FMN adenylyltransferase and flavokinase activities, producing FMN ATP:riboflavin 5'-phosphotransferase EC 2.7.1.26
Products: -
Products: -
?
additional information
?
-
-
Substrates: bifunctional FAD synthetase which shows FMN adenylyltransferase and flavokinase activities, producing FMN ATP:riboflavin 5'-phosphotransferase EC 2.7.1.26
Products: -
Products: -
?
additional information
?
-
Substrates: highly purified 5'-FMN is not accepted as a substrate
Products: -
Products: -
?
additional information
?
-
-
Substrates: highly purified 5'-FMN is not accepted as a substrate
Products: -
Products: -
?
additional information
?
-
Substrates: bifunctional FAD synthetase which shows FMN adenylyltransferase and flavokinase activities, producing FMN ATP:riboflavin 5'-phosphotransferase EC 2.7.1.26
Products: -
Products: -
?
additional information
?
-
Substrates: highly purified 5'-FMN is not accepted as a substrate
Products: -
Products: -
?
additional information
?
-
-
Substrates: bifunctional FAD synthetase which shows FMN adenylyltransferase and flavokinase activities, producing FMN ATP:riboflavin 5'-phosphotransferase EC 2.7.1.26
Products: -
Products: -
?
additional information
?
-
-
Substrates: bifunctional FAD synthetase which shows FMN adenylyltransferase and flavokinase activities, producing FMN ATP:riboflavin 5'-phosphotransferase EC 2.7.1.26
Products: -
Products: -
?
additional information
?
-
Substrates: bifunctional FAD synthetase which shows FMN adenylyltransferase and flavokinase activities, producing FMN ATP:riboflavin 5'-phosphotransferase EC 2.7.1.26
Products: -
Products: -
?
additional information
?
-
-
Substrates: bifunctional FAD synthetase which shows FMN adenylyltransferase and flavokinase activities, producing FMN ATP:riboflavin 5'-phosphotransferase EC 2.7.1.26
Products: -
Products: -
?
additional information
?
-
-
Substrates: bifunctional FAD synthetase which shows FMN adenylyltransferase and flavokinase activities, producing FMN ATP:riboflavin 5'-phosphotransferase EC 2.7.1.26
Products: -
Products: -
?
additional information
?
-
-
Substrates: bifunctional FAD synthetase which shows FMN adenylyltransferase and flavokinase activities, producing FMN ATP:riboflavin 5'-phosphotransferase EC 2.7.1.26
Products: -
Products: -
?
additional information
?
-
-
Substrates: FAD synthetase presents two catalytic modules, a C-terminus with ATP-riboflavin kinase activity and an N-terminus with ATP-flavin mononucleotide adenylyltransferase activity
Products: -
Products: -
?
additional information
?
-
Substrates: bifunctional FAD synthetase exhibiting both the activities of FAD synthetase, EC 2.7.7.2, and riboflavin kinase, EC 2.7.1.26
Products: -
Products: -
?
additional information
?
-
Substrates: bifunctional FAD synthetase exhibiting both the activities of FAD synthetase, EC 2.7.7.2, and riboflavin kinase, EC 2.7.1.26
Products: -
Products: -
?
additional information
?
-
Substrates: bifunctional FAD synthetase exhibiting both the activities of FAD synthetase, EC 2.7.7.2, and riboflavin kinase, EC 2.7.1.26
Products: -
Products: -
?
additional information
?
-
-
Substrates: bifunctional FAD synthetase exhibiting both the activities of FAD synthetase, EC 2.7.7.2, and riboflavin kinase, EC 2.7.1.26
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: bifunctional FAD synthetase which shows FMN adenylyltransferase and flavokinase activities, producing FMN ATP:riboflavin 5'-phosphotransferase EC 2.7.1.26
Products: -
Products: -
?
additional information
?
-
-
Substrates: does not use 8-demethyl-8-amino-riboflavin mononucleotide as substrate
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme contains an N-terminal molybdopterin-binding resembling domain with FAD hydrolytic activity in presence of both Co2+ and chemical mercurial reagents
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: bifunctional FAD synthetase exhibiting both the activities of FAD synthetase, EC 2.7.7.2, and riboflavin kinase, EC 2.7.1.26
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: in the reverse reaction diphosphate cannot be replaced by orthophosphate or metaphosphate
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + FMN
diphosphate + FAD
Substrates: -
Products: -
Products: -
?
ATP + FMN
diphosphate + FAD
Substrates: essential for flavin metabolism
Products: -
Products: -
r
ATP + FMN
diphosphate + FAD
-
Substrates: -
Products: -
Products: -
r
ATP + FMN
diphosphate + FAD
-
Substrates: -
Products: -
Products: -
r
ATP + FMN
diphosphate + FAD
-
Substrates: catalyzes 2 sequential steps in the biosynthesis of FAD, phosphorylation of riboflavin to produce FMN and subsequent adenylylation of FMN to form FAD
Products: -
Products: -
r
ATP + FMN
diphosphate + FAD
Substrates: engineered mutant
Products: -
Products: -
?
ATP + FMN
diphosphate + FAD
Substrates: -
Products: -
Products: -
?
ATP + FMN
diphosphate + FAD
-
Substrates: -
Products: -
Products: -
r
ATP + FMN
diphosphate + FAD
-
Substrates: biosynthesis of FAD is most likely regulated by this coenzyme as a product at the stage of FAD synthetase reaction
Products: -
Products: -
?
ATP + FMN
diphosphate + FAD
-
Substrates: biosynthesis of FAD is most likely regulated by this coenzyme as a product at the stage of FAD synthetase reaction
Products: -
Products: -
ir
additional information
?
-
Substrates: bifunctional FAD synthetase exhibiting both the activities of FAD synthetase, EC 2.7.7.2, and riboflavin kinase, EC 2.7.1.26
Products: -
Products: -
?
additional information
?
-
Substrates: bifunctional FAD synthetase exhibiting both the activities of FAD synthetase, EC 2.7.7.2, and riboflavin kinase, EC 2.7.1.26
Products: -
Products: -
?
additional information
?
-
Substrates: bifunctional FAD synthetase exhibiting both the activities of FAD synthetase, EC 2.7.7.2, and riboflavin kinase, EC 2.7.1.26
Products: -
Products: -
?
additional information
?
-
-
Substrates: bifunctional FAD synthetase exhibiting both the activities of FAD synthetase, EC 2.7.7.2, and riboflavin kinase, EC 2.7.1.26
Products: -
Products: -
?
additional information
?
-
Substrates: bifunctional FAD synthetase exhibiting both the activities of FAD synthetase, EC 2.7.7.2, and riboflavin kinase, EC 2.7.1.26
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
flavin
presence of a flavin binding site for the adenylylation activity, independent from that related with the phosphorylation actiity
ATP
-
nucleoside triphosphates other than ATP do not act as substrates or inhibitors
ATP
-
nucleoside triphosphates other than ATP do not act as substrates or inhibitors
ATP
the ADP/ATP-binding pocket is closed in the ligand-free structure, structure overview. The ADP molecule establishes hydrogen bonds to residues located in L1c-FlapI: Gly196, Gly198 and Gly201 interact with the alpha- and beta-phosphates of ADP, whereas Pro207 and Thr208 (both belonging to the PTAN motif) form several hydrogen bonds via side-chain and main-chain atoms
ATP
residues Asn62, Asp66, Asp168, and Arg297 interact either with ATP phosphate groups, or coordinate the catalytic Mg2+ ion either directly or indirectly through water moleculese
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Co2+
Mg2+
Mn2+
additional information
Ca2+
Ca2+ gives maximum FAD synthesis equal to 62% of that measured with Mg2+
Co2+
-
Co2+ induces FAD hydrolysis, which is strongly stimulated in the presence of K+, K0.5 value is 0.035 mM
Co2+
in the presence of about 0.5 mM Co2+, the activity is almost equal to that measured with Mg2+
Co2+
the enzyme requires divalent metals for activity, the best activity being observed with Co2+, where the activity is 4times greater than that with Mg2+
Mg2+
Mg2+ and the concerted fit of substrates are required to achieve a catalytically competent geometry
Mg2+
MgCl2 is strictly required for both the synthetic and diphosphorolytic activity, FAD synthesis is abolished in the absence of MgCl2
Mg2+
the enzyme contains 8.4 mol of magnesium per protomer
Mg2+
required, the interaction with the two Mg2+ ion coordinating waters by Asp168 is important for the catalytic activity of the enzym. Residues Asn62, Asp66, Asp168, and Arg297 interact either with ATP phosphate groups, or coordinate the catalytic Mg2+ ion either directly or indirectly through water moleculese
Mg2+
-
required for FAD synthesis, optimal concentration 1.5 mM, inhibition at higher levels
Mn2+
Mn2+ gives maximum FAD synthesis equal to 77% of that measured with Mg2+
Mn2+
the activity with Mn2+ is 4times lower than that with Co2+
additional information
-
not basically effected by Mg2+, FAD production slightly inhibited at high concentrations
additional information
the enzyme activity is not stimulated by Zn2+ and Fe2+
additional information
-
the enzyme activity is not stimulated by Zn2+ and Fe2+
additional information
-
Ba2+, Co2+, Cu2+, Cd2+, Fe2+, Ni2+, Sn2+ and Sr2+ do not show any activity
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(1R,2S,4aS,4bS,7R,8aR,10aS)-7-hydroxy-2,4b-dimethyl-1-[(3-oxo-3H-indol-2-yl)methyl]tetradecahydrophenanthrene-2-carboxylic acid
inhibitor of the activity of the flavin adenylyl transferase module of the FADS
2-([1-[4-(trifluoromethyl)pyrimidin-2-yl]piperidin-4-yl]carbamoyl)benzoic acid
inhibitor of the activity of the flavin adenylyl transferase module of the FADS
2-([[(9H-fluoren-9-yl)methoxy]carbonyl]amino)benzoic acid
inhibitor of the activity of the flavin adenylyl transferase module of the FADS, able to inhibit growth of Corynebacterium ammoniagenes and Mycobacterium tuberculosis
methyl 2-[(4-chlorophenyl)carbamoyl]-N-(3,5-dimethyl-1,2-oxazole-4-sulfonyl)hydrazine-1-carboximidothioate
56% resiudal activity at 0.25 mM, inhibitor of the activity of the flavin adenylyl transferase module of the FADS
N-(5-nitrothiophene-3-carbonyl)-2-[[4-(propan-2-yl)phenyl]carbamothioyl]hydrazine-1-carboxamide
inhibitor of the activity of the flavin adenylyl transferase module of the FADS, able to inhibit growth of Corynebacterium ammoniagenes and Mycobacterium tuberculosis
Urea
the enzymatic activity of isoform FADS2 decreases dramatically at increasing urea concentration, with a mid-point for activity loss at 2.1 m urea
additional information
-
no detectable inhibition with 2-[(hydroxyethyl)amino]-FMN, 2-morpholinyl-FMN, 2-(phenylamino)-FMN, 3-methyl-FMN, 3-(carboxymethyl)-FMN, 8-alpha-imidazolyl-FMN, 8-alpha-(N-methylimidazolyl)-FMN, 5'-phosphothionate, DL-glycerol 3-phosphate and propyl 3-phosphate
-
ATP
substrate inhibition; substrate inhibition; substrate inhibition
FAD
product inhibition, wild-type enzyme FMNAT is strongly inhibited by FAD, whereas D181A mutant enzyme has an attenuated product inhibition
FAD
-
strong product inhibitor, 50% inhibition at 0.006 mM, competitive inhibition against ATP, mixed inhibition against FMN
FAD
-
strong product inhibitor, 50% inhibition at 0.006 mM, competitive inhibition against ATP, mixed inhibition against FMN
FMN
substrate inhibition; substrate inhibition; substrate inhibition
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ATP
the enzyme reaches its maximal activity at an ATP concentration of about 1.4 mM. The enzyme activity decreases by 20% when the concentration of ATP is higher than the physiologically relevant concentration (about 5 mM)
CTP
the activity of the enzyme reaches its maximal activity at a CTP concentration of about 1.4 mM. The maximal activity decreases by 68 and 95% when the concentration of CTP is 5.7 and 11.4 mM, respectively
Dithionite
-
presence of sodium dithionite is required for the transformation of FMN into FAD
dithiothreitol
-
FMNAT activity is very poor in the presence of milder reducing agents such as DTT
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.48
CTP
apparent value, in 35 mM TES (K+) buffer (pH 7.2) containing 14 mM dithiothreitol, 7 mM MgCl+, at 70°C
0.116
roseoflavin mononucleotide
-
with 24 mM Na2S2O4, in 50 mM potassium phosphate (pH 7.5), at 37°C
0.025
ATP
apparent value, in 35 mM TES (K+) buffer (pH 7.2) containing 14 mM dithiothreitol, 7 mM MgCl+, at 70°C
0.03568
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
0.07667
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
0.0005
FMN
pH and temperature not specified in the publication, mutant N62A
0.00088
FMN
-
mutant enzyme T208D, at 37°C in 20 mM PIPES pH 7.0, 10 mM MgCl2
0.00088
FMN
-
mutant enzyme E268A, 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
0.00823
FMN
-
mutant enzyme N210A, at 37°C in 20 mM PIPES pH 7.0, 10 mM MgCl2
0.0093
FMN
pH and temperature not specified in the publication, mutant R297A/R300A
0.01501
FMN
-
mutant enzyme N210D, at 37°C in 20 mM PIPES pH 7.0, 10 mM MgCl2
0.0311
FMN
-
FADS trimer, 10 mM MgCl2 in 50 mM TrisHCl (pH 8.0), at 37°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
0.1994
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
-
additional information
additional information
-
MichaelisMenten model
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.07
roseoflavin mononucleotide
-
with 24 mM Na2S2O4, in 50 mM potassium phosphate (pH 7.5), at 37°C
0.0107
ATP
recombinant enzyme purified under native conditions, at pH 8.5
0.0128
ATP
recombinant enzyme purified under native conditions, at pH 8.5
0.01
FMN
pH and temperature not specified in the publication, mutant R300A
0.0108
FMN
recombinant enzyme purified under native conditions, at pH 8.5
0.012
FMN
pH and temperature not specified in the publication, mutant R297A/R300A
0.0128
FMN
recombinant enzyme purified under native conditions, at pH 8.5
0.017
FMN
pH and temperature not specified in the publication, mutant N62S
0.017
FMN
pH and temperature not specified in the publication, mutant D168A
0.042
FMN
pH and temperature not specified in the publication, mutant N62A
0.047
FMN
-
FADS trimer, 10 mM MgCl2 in 50 mM TrisHCl (pH 8.0), at 37°C
0.089
FMN
pH and temperature not specified in the publication, wild-type enzyme
0.21
FMN
pH and temperature not specified in the publication, mutant R297A
0.26
FMN
pH and temperature not specified in the publication, mutant W184A
0.33
FMN
-
FADS monomer, 10 mM MgCl2 in 50 mM TrisHCl (pH 8.0), at 37°C
0.88
FMN
pH and temperature not specified in the publication, mutant D181A
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
3.8
ATP
-
mutant enzyme N210D, at 37°C in 20 mM PIPES pH 7.0, 10 mM MgCl2
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
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
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
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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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
Ki value for diphosphate against ATP not determined because Lineweaver-Burk plots of inhibition by diphosphate with varying concentrations of ATP are nonlinear
-
0.01302
ATP
recombinant enzyme purified under native conditions, at pH 8.5
0.01868
ATP
recombinant enzyme purified under native conditions, at pH 8.5
31
ATP
in 35 mM TES (K+) buffer (pH 7.2) containing 14 mM dithiothreitol, 7 mM MgCl+, at 70°C
0.01
FAD
versus ATP, pH and temperature not specified in the publication, wild-type enzyme
0.012
FAD
versus FMN, pH and temperature not specified in the publication, wild-type enzyme
0.00085
FMN
recombinant enzyme purified under native conditions, at pH 8.5
0.00092
FMN
recombinant enzyme purified under native conditions, at pH 8.5
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.238
(1R,2S,4aS,4bS,7R,8aR,10aS)-7-hydroxy-2,4b-dimethyl-1-[(3-oxo-3H-indol-2-yl)methyl]tetradecahydrophenanthrene-2-carboxylic acid
Corynebacterium ammoniagenes
pH 7.0, 25°C
0.1543
2-([1-[4-(trifluoromethyl)pyrimidin-2-yl]piperidin-4-yl]carbamoyl)benzoic acid
Corynebacterium ammoniagenes
pH 7.0, 25°C
0.053
2-([[(9H-fluoren-9-yl)methoxy]carbonyl]amino)benzoic acid
Corynebacterium ammoniagenes
pH 7.0, 25°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.001
using GTP as cosubstrate, in 35 mM TES (K+) buffer (pH 7.2) containing 14 mM dithiothreitol, 7 mM MgCl+, at 70°C
0.004
using CTP as cosubstrate, in 35 mM TES (K+) buffer (pH 7.2) containing 14 mM dithiothreitol, 7 mM MgCl+, at 70°C
0.01
using ATP as cosubstrate, in 35 mM TES (K+) buffer (pH 7.2) containing 14 mM dithiothreitol, 7 mM MgCl+, at 70°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
bifunctional riboflavin kinase/FMN adenylyltransferase, cf. EC 2.7.1.26
UniProt
brenda
bifunctional flavokinase/flavin adenine dinucleotide synthetase
-
-
brenda
ATCC6872 and KY13315, previously Brevibacterium ammoniagenes
-
-
brenda
bifunctional enzyme, displays activities of EC 2.7.7.2 and EC 2.7.1.26
SwissProt
brenda
bifunctional riboflavin kinase/FMN adenylyltransferase, cf. EC 2.7.1.26
SwissProt
brenda
baker's yeast, brewers' yeast, beer yeast, FAD1 nucleotide sequence
SwissProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
mature siliques and germinated seeds expresse 50-100% more AtRibF1 mRNA than AtRibF2 mRNA
brenda
mature siliques and germinated seeds expresse 50-100% more AtRibF1 mRNA than AtRibF2 mRNA
brenda
additional information
relative expression levels show little or no variation among the organs and at the developmental stages examined. Exceptions are mature siliques and germinated seeds, which expresse 50-100% more AtRibF1 mRNA than AtRibF2 mRNA
brenda
additional information
relative expression levels show little or no variation among the organs and at the developmental stages examined. Exceptions are mature siliques and germinated seeds, which expresse 50-100% more AtRibF1 mRNA than AtRibF2 mRNA
brenda
additional information
relative expression levels show little or no variation among the organs and at the developmental stages examined. Exceptions are mature siliques and germinated seeds, which expresse 50-100% more AtRibF1 mRNA than AtRibF2 mRNA
brenda
additional information
-
relative expression levels show little or no variation among the organs and at the developmental stages examined. Exceptions are mature siliques and germinated seeds, which expresse 50-100% more AtRibF1 mRNA than AtRibF2 mRNA
brenda
additional information
expression levels of AtRibF1 show little or no variation among the organs and at the developmental stages examined, 2 exceptions are mature siliques and germinated seeds, which express 50-100% more AtRibF1 mRNA, AtRibF1 is a housekeeping enzyme needed by all plant organs throughout development
brenda
additional information
expression levels of AtRibF1 show little or no variation among the organs and at the developmental stages examined, 2 exceptions are mature siliques and germinated seeds, which express 50-100% more AtRibF1 mRNA, AtRibF1 is a housekeeping enzyme needed by all plant organs throughout development
brenda
additional information
expression levels of AtRibF1 show little or no variation among the organs and at the developmental stages examined, 2 exceptions are mature siliques and germinated seeds, which express 50-100% more AtRibF1 mRNA, AtRibF1 is a housekeeping enzyme needed by all plant organs throughout development
brenda
additional information
-
expression levels of AtRibF1 show little or no variation among the organs and at the developmental stages examined, 2 exceptions are mature siliques and germinated seeds, which express 50-100% more AtRibF1 mRNA, AtRibF1 is a housekeeping enzyme needed by all plant organs throughout development
brenda
additional information
expression levels of AtRibF2 show little or no variation among the organs and at the developmental stages examined, AtRibF2 are housekeeping enzyme needed by all plant organs throughout development
brenda
additional information
expression levels of AtRibF2 show little or no variation among the organs and at the developmental stages examined, AtRibF2 are housekeeping enzyme needed by all plant organs throughout development
brenda
additional information
expression levels of AtRibF2 show little or no variation among the organs and at the developmental stages examined, AtRibF2 are housekeeping enzyme needed by all plant organs throughout development
brenda
additional information
-
expression levels of AtRibF2 show little or no variation among the organs and at the developmental stages examined, AtRibF2 are housekeeping enzyme needed by all plant organs throughout development
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
presence of mitochondrial FAD synthetase activity in strains transformed with FAD1 on a high-copy-number plasmid, but not in mitochondria of wild-type strains
brenda
existence of FAD synthesizing and hydrolyzing activities involved in maintaining FAD homeostasis in isolated rat liver nuclei, overview
brenda
-
existence of FAD synthesizing and hydrolyzing activities involved in maintaining FAD homeostasis in isolated rat liver nuclei, overview
-
brenda
additional information
subcellular localization analysis of the enzyme, overview
-
brenda
additional information
-
subcellular localization analysis of the enzyme, overview
-
-
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
metabolism
physiological function
additional information
evolution
whereas the N-terminal module of FADS lacks structural homology to eukaryotic FMNATs, the kinase module is homologous to monofunctional RFKs
evolution
eukaryotic FMNAT is related to phosphoadenosine phosphosulfate (PAPS) reductase family proteins and contains a core domain with a modified Rossman-fold topology and a C-terminal extension
metabolism
the enzyme catalyzes the last step in the metabolic pathway producing FAD, redox cofactor ensuring the activity of many flavoenzymes mainly located in mitochondria but also relevant for nuclear redox activities
metabolism
-
the enzyme catalyzes the last step in the metabolic pathway producing FAD, redox cofactor ensuring the activity of many flavoenzymes mainly located in mitochondria but also relevant for nuclear redox activities
-
physiological function
the essential cofactors of flavoproteins and flavoenzymes, flavin mononucleotide (FMN) and flavin adenine dinucleotide (FAD), are synthesized from riboflavin in two sequential reactions: riboflavin phosphorylation is catalysed by an ATP-riboflavin kinase (RFK, EC 2.7.1.26) to produce FMN, which can be then converted to FAD by an FMN:ATP adenylyltranferase (FMNAT, EC 2.7.7.2). Bacteria contain a single bifunctional polypeptide called FAD synthetase (FADS)
physiological function
flavocoenzymes, including flavin mononucleotide (FMN) and flavin adenine dinucleotide (FAD), are versatile redox cofactors involved in many fundamental cellular processes in all living organisms. FAD is synthesized from riboflavin obtained from the diet via two enzymatic steps catalyzed by riboflavin kinase (RFK, EC 2.7.1.26) and essential FMN adenylyltransferase (FMNAT,EC 2.7.7.2). Phosphorylation of riboflavin by RFK is crucial for specific absorption of the vitamin and is the physiologically rate-limiting step in the biosynthesis of flavocoenzymes, whereas product (FAD) feedback inhibition is observed for mammalian FMNAT, suggesting that biosynthesis of FAD is also regulated at the FMNAT reaction step
physiological function
the enzyme catalyzes the last step in the metabolic pathway producing FAD, redox cofactor ensuring the activity of many flavoenzymes mainly located in mitochondria but also relevant for nuclear redox activities
physiological function
distortion of aromaticity at the FMNAT isoalloxazine binding cavity prevents FMN and FAD from correct accommodation in their binding cavity and decreases the efficiency of the FMNAT activity. The side-chains of F62, Y106 and F128 are relevant in the formation of the catalytic competent complex during FMNAT catalysis in bifunctional FAD synthase
physiological function
in a truncated FADS variant consisting in the isolated C-terminal ATP:riboflavin kinase RFK module, RFK activity is similar to that of the full-length enzyme. Inhibition of the RFK activity by the RF substrate is independent of the FMN:ATP adenylyltransferase module, and FMN production, in addition to being inhibited by an excess of riboflavin, is also inhibited by both of the reaction products. Mg2+ and the concerted fit of substrates are required to achieve a catalytically competent geometry
physiological function
molecular docking and molecular dynamics simulations with ATP/Mg2+ and FMN in both the monomeric and dimer-of-trimers assemblies. For the dimer-of-trimers conformation, the RFK module negatively influences FMN binding at the interacting FMNAT module. FMN binds to the monomer but not to the dimer-of-trimers. The presence of the RFK module (residues E268, D298, and V300) considerably impairs FMN binding at the FMNAT active site and decreases the FMNAT catalytic efficiency
physiological function
-
the enzyme catalyzes the last step in the metabolic pathway producing FAD, redox cofactor ensuring the activity of many flavoenzymes mainly located in mitochondria but also relevant for nuclear redox activities
-
additional information
molecular dynamics simulations of riboflavin kinase domain bound to FMN, ADP, and Mg2+, structure-function analysis, flavin-binding site structure in the RFK module of CaFADS, overview
additional information
residue E268 is the catalytic base of the kinase reaction. The salt bridge between E268 at the RFK site and R66 at the FMNAT-module is important for the riboflavinkinase activity. Cross-talk between the RFK- and FMNAT-modules of neighboring protomers in the CaFADS enzyme, and participation of R66 in the modulation of the geometry of the RFK active site during catalysis
additional information
-
residue E268 is the catalytic base of the kinase reaction. The salt bridge between E268 at the RFK site and R66 at the FMNAT-module is important for the riboflavinkinase activity. Cross-talk between the RFK- and FMNAT-modules of neighboring protomers in the CaFADS enzyme, and participation of R66 in the modulation of the geometry of the RFK active site during catalysis
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
140000
-
gel filtration, purified enzyme can be separated into low molecular weight component of MW 140000 and MW 325000 high molecular weight component
16600
recombinant truncated C-terminal RF kinase domain, gel filtration
28800
29200
325000
-
gel filtration, purified enzyme can be separated into low molecular weight component of MW 140000 and high molecular weight component of MW325000
34200
35670
36000
37120
-
electrospray mass spectrometry, Se-Met-enzyme, 36843.5 is the theoretical value for the native protein
38000
additional information
the elution profile of full-length FADS shows two characteristic peaks at molecular weights corresponding to its monomeric and trimeric forms, while the tcRFK elutes as a single peak at an estimated molecular weight of 16.6 kDa, consistent with monomeric enzyme
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
hexamer
monomer
oligomer
the enzyme forms transient oligomers during catalysis stabilized by several interactions between the RFK and FMNAT sites from neighboring protomers, which otherwise are separated in the monomeric enzyme
additional information
hexamer
dimer-of-trimers organization with the catalytic sites of two modules of neighbouring protomers approaching each other
monomer
x * 16600, recombinant truncated C-terminal RF kinase domain, SDS-PAGE
additional information
prokaryotic FAD synthetases (FADSs) are bifunctional enzymes composed of two modules, the C-terminal module with ATP:riboflavin kinase (RFK) activity, and the N-terminus with ATP:FMN adenylyltransferase (FMNAT) activity
additional information
-
prokaryotic FAD synthetases (FADSs) are bifunctional enzymes composed of two modules, the C-terminal module with ATP:riboflavin kinase (RFK) activity, and the N-terminus with ATP:FMN adenylyltransferase (FMNAT) activity
additional information
the enzyme contains a core domain with a modified Rossman-fold topology and a C-terminal extension. The substrate binding and catalytic site is located at the interface of the two domains
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
3D structural model for based on the structure of Thermotoga maritima FADS
crystal structure predicts a dimer of trimers organization
purified recombinant DELTA(1-182)CaFADS module in binary complex with ADP-Ca2+ and in ternary complex with FMN-ADP-Mg2+, mixing of 0.002 ml of 7.5-10 mg/ml protein in 20 mM Tris-HCl, pH 8.0, 150 mM NaCl, 1 mM MgCl2, 1mM FMN and/or 1 mM ADP, with 0.002 ml of reservoir solution containing 10-14% PEG 8000, 20% glycerol, 0.1 M MES-NaOH pH 6.5, 200 mM CaCl2 for the binary complex, or with 0.002 ml of reservoir solution containing 26-30% PEG 4000, 200 mM Li2SO4, 100 mM sodium acetate, pH 5.0, as well as 0.002 ml of 1 M NaI solution, for the ternary complex, X-ray diffraction structure determination and analysis at 1.65-2.15 A resolution, modelling
purified recombinant enzyme mutant R66A and R66E, mixing of equal volumes of 10 mg/ml protein in 20mMTris/HCl, pH 8.0, and 1 mM DTT, with reservoir solution containing 1.5 M Li2SO4, 0.1 M HEPES/NaOH, pH 7.5, X-ray diffraction structure determination and analysis, molecular replacment and modelling using the native CaFADS structure, PDB ID 2X0K, as search model
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
E268A
E268D
E301A
mutation at the macromolecular interface between two protomers within the trimer
E301K
mutation at the macromolecular interface between two protomers within the trimer
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
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
N210A
N210D
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
T208A
T208D
V300A
mutation at the macromolecular interface between two protomers within the trimer
V300K
mutation at the macromolecular interface between two protomers within the trimer
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
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
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
additional information
E268A
-
the mutant shows increased catalytic efficiency for FMN and reduced catalytic efficiency for ATP compared to the wild type enzyme
E268D
-
the mutant shows about wild type catalytic efficiencies for ATP and FMN
N210A
-
the mutant shows strongly reduced catalytic efficiencies for FMN and ATP compared to the wild type enzyme
N210D
-
the mutant shows strongly reduced catalytic efficiencies for FMN and ATP compared to the wild type enzyme
T208A
-
the mutant shows increased catalytic efficiency for FMN and reduced catalytic efficiency for ATP compared to the wild type enzyme
T208D
-
the mutant shows increased catalytic efficiency for FMN and increased catalytic efficiency for ATP compared to the wild type enzyme
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
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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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
55
55
-
enzyme denatured as temperature increases, completely inactivated above, bovine serum albumin stabilizes up to 45°C
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
aerobically isolated enzyme is active only under reducing conditions (with 5.6 mM dithiothreitol)
721625
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 1 mM dithiothreitol, 20% glycerol can be stored without significant loss of activity for 1 week
-
5°C, if dithiothreitol is removed from the purified enzyme solution enzyme denatures within 12 h
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate fractionation, Phenyl-Sepharose chromatography, DEAE-Cellulose chromatography
-
by Ni-NTA affinity chromatography, ion exchange chromatography and gel filtration
DEAE-cellulose column chromatography, phenyl Sepharose column chromatography, and Sephacryl S-200 gel filtration
Ni-Sepharose affinity chromatography, anion exchange chromatography, hydrophobic interaction chromatography, gel filtration
Ni2+-chelating column chromatography and hydroxyapatite column chromatography
phenyl Sepharose column chromatography and DEAE-cellulose column chromatography
-
recombinant C-terminally poly-His-tagged N-terminally truncated mutant_187-338 from Escherichia coli by ion exchange chromatography and gel filtration
recombinant protein
recombinant RFK module of enzyme FADS, DELTA(1-182)CaFADS, from Escherichia coli strain BL21(DE3)
recombinant wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by ammonium sulfate fractionation, hydrophobic interaction and ion exchange chromatography, followed by dialysis
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
expressed in Escherichia coli BL21 (DE3), a SeMet-version is generated
-
expressed in Escherichia coli BL21-Codon Plus (DE3)-RIL cells
expressed in Escherichia coli strain Rosetta(DE3)
expressed in Escherichia coli strains BL21 and Rosetta (DE3) and in Pichia pastoris strain X33
-
expression in Escherichia coli
FAD synthetase gene cloned and overexpressed in Escherichia coli JM105
FAD synthetase overproducing recombinant Corynebacterium ammoniagenes KY13315 constructed from ATCC6872, gene cannot be expressed in Escherichia coli
-
gene ribF, individual expression of the riboflavin kinase, RFK, module of enzyme FAD synthetase, FADS, i.e. DELTA(1-182)CaFADS, in Escherichia coli strain BL21(DE3)
gene ribF, recombinant expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
recombinant expression of C-terminally poly-His-tagged N-terminally truncated mutant in Escherichia coli
ribC encodes a bifunctional flavokinase/FAD-synthetase, cloned and overexpressed in Escherichia coli BL21
structural gene FAD1, essential yeast protein, disruption of the gene induces a lethal phenotype, cloned from a genomic library, vector pATH26 transformed into Saccharomyces cerevisiae and Escherichia coli RR1 on a multicopy plasmid
vector pET-23a(+) cloned and overexpressed in Escherichia coli JM109(DE-3)
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
nutrition
synthesis
nutrition
-
industrial production of FAD and FMN as nutrient additives, pharmaceuticals and biochemical agents
synthesis
the enzyme is used for the preparation of flavin mononucleotide (FMN) and FMN analogues from their corresponding riboflavin precursors, which is performed in a two-step procedure. After initial enzymatic conversion of riboflavin to FAD by the bifunctional FAD synthetase, the adenyl moiety of FAD is hydrolyzed with snake venom phosphodiesterase to yield FMN. 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
synthesis
purified recombinant FADSCf can be used for the biosynthesis of FAD. Under optimized conditions (0.5 mM FMN, 5 mM ATP and 10 mM Mg2+), the production of FAD reaches 80 mM per mg of enzyme after a 21-hour reaction
synthesis
modular engineering of Escherichia coli to improve flavin production and the conversion ratio of riboflavin RF to FMN/FAD. The RF operon and the bifunctional RF kinase/FAD synthetase are divided into two separate modules and expressed at different levels to produce different RF:ribF. The best strain respectively produces 324.1 and 171.6 mg/l of FAD and FMN in shake flask fermentation. Error-prone of the RibF gene further increase production up to 586.1 mg/l in shake flask cultivation
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Yamada, Y.; Merrill, A.; McCormick, D.N.
Probable reaction mechanisms of flavokinase and FAD synthetase from rat liver
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Rattus norvegicus
brenda
Mack, M.; van Loon, A.P.; Hohmann, H.P.
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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
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1950
Saccharomyces cerevisiae
brenda
Gomes, B.; McCormick, D.B.
Purification and general characterization of FAD synthetase from rat liver
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172
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Rattus norvegicus
brenda
Oka, M.; McCormick, D.B.
Complete purification and general characterization of FAD synthetase from rat liver
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262
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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 (Q9FMW8), Arabidopsis thaliana (Q8VZR0), 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
Nakaseomyces glabratus (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
Nakaseomyces glabratus (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
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