Information on EC 2.7.7.2 - FAD synthetase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea

EC NUMBER
COMMENTARY hide
2.7.7.2
-
RECOMMENDED NAME
GeneOntology No.
FAD synthetase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + FMN = diphosphate + FAD
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
nucleotidyl group transfer
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Biosynthesis of secondary metabolites
-
-
flavin biosynthesis I (bacteria and plants)
-
-
flavin biosynthesis II (archaea)
-
-
flavin biosynthesis III (fungi)
-
-
flavin biosynthesis IV (mammalian)
-
-
Metabolic pathways
-
-
Riboflavin metabolism
-
-
flavin biosynthesis
-
-
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 hide
9026-37-3
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
1012
Uniprot
Manually annotated by BRENDA team
1012
Uniprot
Manually annotated by BRENDA team
bovine
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
cv. Bright Yellow 2
-
-
Manually annotated by BRENDA team
bifunctional flavokinase/flavin adenine dinucleotide synthetase
-
-
Manually annotated by BRENDA team
strain TM379
-
-
Manually annotated by BRENDA team
strain TM379
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
metabolism
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + 4'-butyl-FMN
diphosphate + 4'-butylflavin adenine dinucleotide
show the reaction diagram
-
-
-
-
?
ATP + 5'-pentyl-FMN
diphosphate + 5'-pentylflavin adenine dinucleotide
show the reaction diagram
-
-
-
-
?
ATP + 7,8-dibromo-FMN
diphosphate + 7,8-dibromoflavin adenine dinucleotide
show the reaction diagram
-
-
-
-
?
ATP + 7,8-dichloro-FMN
diphosphate + 7,8-dichloroflavin adenine dinucleotide
show the reaction diagram
-
-
-
-
?
ATP + 7-chloro-FMN
diphosphate + 7-chloroflavin adenine dinucleotide
show the reaction diagram
-
-
-
-
?
ATP + 8-chloro-FMN
diphosphate + 8-chloroflavin adenine dinucleotide
show the reaction diagram
-
-
-
-
?
ATP + FMN
diphosphate + FAD
show the reaction diagram
ATP + iso-FMN
diphosphate + isoflavin adenine dinucleotide
show the reaction diagram
-
-
-
-
?
ATP + riboflavin
?
show the reaction diagram
ATP + roseoflavin mononucleotide
diphosphate + roseoflavin adenine dinucleotide
show the reaction diagram
-
-
-
-
?
CTP + FMN
diphosphate + flavin cytidine dinucleotide
show the reaction diagram
-
-
-
?
diphosphate + FAD
ATP + FMN
show the reaction diagram
FMN + ATP
FAD + diphosphate
show the reaction diagram
GTP + FMN
diphosphate + flavin guanidine dinucleotide
show the reaction diagram
weak specific activity
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + FMN
diphosphate + FAD
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
flavin
presence of a flavin binding site for the adenylylation activity, independent from that related with the phosphorylation actiity
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Cu2+
-
effective for FMN production
Fe2+
the enzyme contains 0.2 mol of iron per protomer
MgCl2
strictly required
Ni2+
weak stimulation of activity
Zn2+
-
effective for FMN production
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,5-Dideaza-FMN
-
-
1-Deaza-FMN
-
-
2-thio-FMN
-
-
5'-sulfo-FMN
-
-
8-Hydroxy-7-methyl-FMN
-
-
D-glucose 6-phosphate
-
-
D-lyxose 5-phosphate
-
-
diphosphate
GDP
-
competitive inhibition
GTP
-
uncompetitive inhibition
hexyl 6-phosphate
-
-
NAD+
-
inhibits FAD cleavage completely
Riboflavin 5'-diphosphate
-
weak cofactor for FAD-requiring enzymes
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
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
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 hide
LITERATURE
IMAGE
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
0.0107 - 0.079
ATP
0.48
CTP
apparent value, in 35 mM TES (K+) buffer (pH 7.2) containing 14 mM dithiothreitol, 7 mM MgCl+, at 70°C
0.114
diphosphate
-
pH 7.6, 25°C
0.0004
FAD
-
pH 7.6, 25°C
0.00035 - 1.5
FMN
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
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0107 - 0.142
ATP
0.000075
FAD
Corynebacterium ammoniagenes
-
pH 7.6, 25°C
0.0000833 - 0.88
FMN
0.07
roseoflavin mononucleotide
Homo sapiens
-
with 24 mM Na2S2O4, in 50 mM potassium phosphate (pH 7.5), at 37°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.16 - 9
ATP
4
0.006
CTP
Methanocaldococcus jannaschii
Q58579
apparent value, in 35 mM TES (K+) buffer (pH 7.2) containing 14 mM dithiothreitol, 7 mM MgCl+, at 70°C
60
0.0311 - 386
FMN
56
0.6
roseoflavin mononucleotide
Homo sapiens
-
with 24 mM Na2S2O4, in 50 mM potassium phosphate (pH 7.5), at 37°C
42464
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.029
1,5-Dideaza-FMN
-
pH 7.1, 37°C
0.283
1-Deaza-FMN
-
pH 7.1, 37°C
0.106
2-thio-FMN
-
pH 7.1, 37°C
0.291
5'-sulfo-FMN
-
pH 7.1, 37°C
0.002
8-Hydroxy-7-methyl-FMN
-
pH 7.1, 37°C
0.013 - 31
ATP
0.019
D-glucose 6-phosphate
-
pH 7.1, 37°C
0.184
D-lyxose 5-phosphate
-
pH 7.1, 37°C
0.00064 - 0.066
diphosphate
0.00075 - 0.012
FAD
0.00085 - 0.00092
FMN
2.5
GDP
-
at 37°C, in 50 mM Tris-HCl, pH 7.5
1.8
GTP
-
at 37°C, in 50 mM Tris-HCl, pH 7.5
0.266
hexyl 6'-phosphate
-
pH 7.1, 37°C
0.009
Riboflavin 5'-diphosphate
-
-
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
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
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
0.0039
-
-
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
0.0044
-
-
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
0.03
at 37°C
0.59
-
crude cell extract, at 37°C
6.8
-
after 12.5fold purification, at 37°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.1
-
-
7 - 7.4
-
FMN used as substrate
7.8 - 8
-
riboflavin used as substrate
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35 - 37
-
riboflavin used as substrate
37 - 40
-
FMN used as substrate
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.66
-
isoelectric focusing
6
-
calculated from amino acid sequence
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
mature siliques and germinated seeds expresse 50-100% more AtRibF1 mRNA than AtRibF2 mRNA; mature siliques and germinated seeds expresse 50-100% more AtRibF1 mRNA than AtRibF2 mRNA
Manually annotated by BRENDA team
mature siliques and germinated seeds expresse 50-100% more AtRibF1 mRNA than AtRibF2 mRNA; mature siliques and germinated seeds expresse 50-100% more AtRibF1 mRNA than AtRibF2 mRNA
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
PDB
SCOP
CATH
ORGANISM
UNIPROT
Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65)
Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65)
Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65)
Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65)
Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
16600
-
recombinant truncated C-terminal RF kinase domain, gel filtration
17000
2 * 17000, SDS-PAGE
28800
estimated by gel filtration; gel filtration
29200
estimated by gel filtration; gel filtration
33900
1 * 33900, SDS-PAGE and calculated
34000
-
x * 34000, His-tagged recombinant protein, SDS-PAGE
34180
wild-type, gel filtration
34230
mutant RibC, gel filtration
35670
deduced from RibC open reading frame; mass spectroscopy
37120
-
electrospray mass spectrometry, Se-Met-enzyme, 36843.5 is the theoretical value for the native protein
37710
deduced from amino acid sequence
53000
-
2 * 53000, SDS-PAGE
54190
-
calculated from amino acid sequence
54200
-
x * 54200 Da, predicted
55000
SDS-PAGE, T7-tagged enzyme
55840
calculated from amino acid sequence, T7-tagged enzyme
55844
x * 55000, SDS-PAGE, x * 55844, calculated
56537
-
x * 56537, isoform FADS2, calculated from amino acid sequence
57000
-
x * 57000, isoform FADS2, SDS-PAGE
60000
-
SDS-PAGE, isoform 2
63000
-
SDS-PAGE
65270
-
calculated from amino acid sequence
65300
-
x * 65300 Da, predicted
97000
-
gel filtration
140000
-
gel filtration, purified enzyme can be separated into low molecular weight component of MW 140000 and MW 325000 high molecular weight component
325000
-
gel filtration, purified enzyme can be separated into low molecular weight component of MW 140000 and high molecular weight component of MW325000
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
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexamer
homodimer
2 * 17000, SDS-PAGE
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
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
3D structural model for based on the structure of Thermotoga maritima FADS
hanging-drop vapor-diffusion method, 277 K
-
mutant enzyme E268D, hanging drop vapor diffusion method
-
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
-
in complex with FAD, hanging drop vapor diffusion method
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 8.4
-
at pH 6.0 10% as active as at pH 7.5, at pH 8.4 64%
642993
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
purified enzyme is instable
-
thiol maintains stability
-
thiols protects the activity, can partly restore inactivated enzyme
-
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
aerobically isolated enzyme is active only under reducing conditions (with 5.6 mM dithiothreitol)
721625
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 1 mM dithiothreitol, 20% glycerol can be stored without significant loss of activity for 1 week
-
-20°C, stable for at least 2 weeks
3°C, loses 20-30% of its activity in 4 days, 58% in 11 days
-
4°C, activity largely lost within 1 week
-
5°C, if dithiothreitol is removed from the purified enzyme solution enzyme denatures within 12 h
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
; recombinant protein
ammonium sulfate fractionation, Phenyl-Sepharose chromatography, DEAE-Cellulose chromatography
-
by ion exchange chromatography and gel filtration; by Ni-NTA affinity chromatography, ion exchange chromatography and gel filtration; recombinant protein; recombinant protein
DEAE-cellulose column chromatography, phenyl Sepharose column chromatography, and Sephacryl S-200 gel filtration
-
Mono Q column chromatography
Ni-Sepharose affinity chromatography, anion exchange chromatography, hydrophobic interaction chromatography, gel filtration
-
Ni2+-chelating column chromatography and hydroxyapatite column chromatography
-
Ni2+-chelating Sepharose Fast Flow column chromatography
-
Ni2+-nitrilotriacetic-agarose column chromatography
-
partially by subcellular fractionation and nucleus preparation
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 enzyme
-
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
-
wild-type and recombinant enzyme
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
; FAD synthetase gene cloned and overexpressed in Escherichia coli JM105
; 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
cloned in Escherichia coli; cloned in Escherichia coli; expression in Escherichia coli; expression in Escherichia coli
expressed in Escherichia coli
-
expressed in Escherichia coli BL21 (DE3), a SeMet-version is generated
-
expressed in Escherichia coli BL21(DE3) cells
-
expressed in Escherichia coli BL21-Codon Plus (DE3)-RIL cells
expressed in Escherichia coli strain Rosetta(DE3)
-
expressed in Escherichia coli strain Rosetta(DE3); expression in Escherichia coli
expressed in Escherichia coli strains BL21 and Rosetta (DE3) and in Pichia pastoris strain X33
-
expressed in Escherichia coli; expressed in Escherichia coli, in BHK-21 cell, and Caco-2 cell
-
expression in Escherichia coli
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)
-
His-tagged version expressed in Escherichia coli BL21(DE3)
-
His6-tagged enzyme is expressed in Escherichia coli Rosetta (DE3) cells
-
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
vector pET-23a(+) cloned and overexpressed in Escherichia coli JM109(DE-3)
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D168A
-
site-directed mutagenesis, the mutant shows altered kinetics compared to the wild-type enzyme
D181A
-
site-directed mutagenesis, the mutant shows reduced sensitivity to inhibition by FAD compared to the wild-type enzyme and has a much faster turnover rate than the wild-type enzyme
D66A
-
site-directed mutagenesis, inactive mutant
N62A
-
site-directed mutagenesis, the mutant shows altered kinetics compared to the wild-type enzyme
N62S
-
site-directed mutagenesis, the mutant shows altered kinetics compared to the wild-type enzyme
R297A/R300A
-
site-directed mutagenesis, the mutant shows altered kinetics compared to the wild-type enzyme
R300A
-
site-directed mutagenesis, the mutant shows 93% reduced activity compared to the wild-type enzyme
W184A
-
site-directed mutagenesis, the mutant shows altered kinetics compared to the wild-type enzyme
H28A
loss of both riboflavin kinase and FAD synthetase activities
H28D
loss of both riboflavin kinase and FAD synthetase activities
H31D
residual activity, involved in the stabilisation of the phosphate groups and the adenine moiety of ATP and the phosophate of FMN
R161A
active, residue R161 does not play a critical role in catalysis
R161D
active, residue R161 does not play a critical role in catalysis
R66A
-
site-directed mutagenesis, R66A CaFADS shows a considerable increase in the amount of oligomeric species
R66E
-
site-directed mutagenesis, R66E CaFADS shows a considerable increase in the amount of oligomeric species
R66X
-
point mutations at R66 have only mild effects on ligand binding and kinetic properties of the FMNAT-module (where R66 is located), but considerably impair the RFK activity turnover. Substitutions of R66 also modulate the ratio between monomeric and oligomeric species and modify the quaternary arrangement observed by single-molecule methods
S164A
residual activity, involved in the stabilisation of the phosphate groups and the adenine moiety of ATP and the phosophate of FMN
S164D
residual activity, involved in the stabilisation of the phosphate groups and the adenine moiety of ATP and the phosophate of FMN
T165A
residual activity, involved in the stabilisation of the phosphate groups and the adenine moiety of ATP and the phosophate of FMN
T165D
residual activity, involved in the stabilisation of the phosphate groups and the adenine moiety of ATP and the phosophate of FMN
C126S
the mutation does not reduce the protein's heat stability or solubility, the mutant contains less than 0.8 and less than 0.08 mol of Mg and Fe per protomer. In the presence of MgCl2, the mutant has activity about 2times higher than that of the wild type enzyme. The activity of the mutant in presence of Co2+ is very low
C143S
the mutation does not reduce the protein's heat stability or solubility, the mutant contains less than 0.8 and less than 0.08 mol of Mg and Fe per protomer. In the presence of MgCl2, the mutant has activity approximately wild type activity. The activity of the mutant in presence of Co2+ is very low
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
nutrition
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
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