2.7.7.2: FAD synthase
This is an abbreviated version!
For detailed information about FAD synthase, go to the full flat file.
Word Map on EC 2.7.7.2
-
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
- 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
Reaction
Synonyms
adenosine triphosphate-riboflavin mononucleotide transadenylase, adenosine triphosphate-riboflavine mononucleotide transadenylase, ATP-FMN adenylyltransferase, ATP:FMN adenylyl transferase, ATP:FMN adenylyltransferase, AtRibF1, AtRibF2, FAD pyrophosphorylase, FAD synthase, FAD synthetase, FAD synthetase isoform 1, FAD synthetase isoform 2, Fad1, FADS, FADS-6, FADS1, FADS2, FLAD1, flavin adenine dinucleotide synthetase, FMN adenylyltransferase, FMN pyrophosphorylase, FMN:ATP adenylyltransferase, FMNAT, lysZ, MJ1179, More, ribF, RibL, riboflavin adenine dinucleotide pyrophosphorylase, riboflavin mononucleotide adenylyltransferase, riboflavine adenine dinucleotide adenylyltransferase, SPAP_1083
ECTree
2.7.7.2 FAD synthaseAdvanced search results
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results (Substrates Products
Substrates Products on EC 2.7.7.2 - FAD synthase
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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 + roseoflavin mononucleotide
diphosphate + roseoflavin adenine dinucleotide
-
-
-
-
?
CTP + FMN
diphosphate + flavin cytidine dinucleotide
-
-
-
?
GTP + FMN
diphosphate + flavin guanidine dinucleotide
weak specific activity
-
-
?
ATP + FMN
diphosphate + FAD
essential for flavin metabolism
-
r
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
the enzyme does not catalyze the reverse reaction to produce FMN and ATP from FAD and diphosphate
-
-
ir
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
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
?
-
-
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
-
-
?
