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Information on EC 2.7.7.2 - FAD synthase and Organism(s) Methanocaldococcus jannaschii and UniProt Accession Q58579
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2.7.7.2 FAD synthaseIUBMB 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].
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Word Map
- 2.7.7.2
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desaturase
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polyunsaturated
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arachidonic
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docosahexaenoic
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linoleic
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eicosapentaenoic
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desaturation
- elongase
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elovl2
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omega-6
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delta-5
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lcpufas
- ammoniagenes
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srebf1
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gene-diet
- flavokinase
- synthesis
- nutrition
The taxonomic range for the selected organisms is: Methanocaldococcus jannaschii
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
fads1, flad1, fad synthase, fad pyrophosphorylase, flavin adenine dinucleotide synthetase, atribf1, atribf2, atp:fmn adenylyltransferase, mj1179, fmn:atp adenylyltransferase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
adenosine triphosphate-riboflavin mononucleotide transadenylase
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-
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adenosine triphosphate-riboflavine mononucleotide transadenylase
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-
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FAD pyrophosphorylase
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-
-
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FMN adenylyltransferase
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-
-
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FMN pyrophosphorylase
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-
-
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lysZ
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-
-
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riboflavin adenine dinucleotide pyrophosphorylase
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-
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riboflavin mononucleotide adenylyltransferase
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-
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riboflavine adenine dinucleotide adenylyltransferase
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
nucleotidyl group transfer
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-
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-
PATHWAY SOURCE
PATHWAYS
BRENDA
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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].
CAS REGISTRY NUMBER
COMMENTARY
9026-37-3
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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 + FMN
diphosphate + FAD
the enzyme does not catalyze the reverse reaction to produce FMN and ATP from FAD and diphosphate
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-
ir
CTP + FMN
diphosphate + flavin cytidine dinucleotide
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-
-
?
GTP + FMN
diphosphate + flavin guanidine dinucleotide
weak specific activity
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-
?
additional information
?
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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
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-
?
additional information
?
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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
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-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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+
Mn2+
the activity with Mn2+ is 4times lower than that with Co2+
additional information
Mg2+
the enzyme contains 8.4 mol of magnesium per protomer
additional information
the enzyme activity is not stimulated by Zn2+ and Fe2+
additional information
-
the enzyme activity is not stimulated by Zn2+ and Fe2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.025
ATP
apparent value, in 35 mM TES (K+) buffer (pH 7.2) containing 14 mM dithiothreitol, 7 mM MgCl+, at 70°C
0.48
CTP
apparent value, in 35 mM TES (K+) buffer (pH 7.2) containing 14 mM dithiothreitol, 7 mM MgCl+, at 70°C
0.063
FMN
apparent value, in 35 mM TES (K+) buffer (pH 7.2) containing 14 mM dithiothreitol, 7 mM MgCl+, at 70°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.16
ATP
apparent value, in 35 mM TES (K+) buffer (pH 7.2) containing 14 mM dithiothreitol, 7 mM MgCl+, at 70°C
0.006
CTP
apparent value, in 35 mM TES (K+) buffer (pH 7.2) containing 14 mM dithiothreitol, 7 mM MgCl+, at 70°C
0.064
FMN
apparent value, in 35 mM TES (K+) buffer (pH 7.2) containing 14 mM dithiothreitol, 7 mM MgCl+, at 70°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
31
ATP
in 35 mM TES (K+) buffer (pH 7.2) containing 14 mM dithiothreitol, 7 mM MgCl+, at 70°C
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
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
aerobically isolated enzyme is active only under reducing conditions (with 5.6 mM dithiothreitol)
721625
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21-Codon Plus (DE3)-RIL cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
EXTERNAL LINKS (specific for EC-Number 2.7.7.2)
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