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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

Reaction

ATP
+
FMN
=
diphosphate
 +
FAD

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 Transferases
         2.7 Transferring phosphorus-containing groups
             2.7.7 Nucleotidyltransferases
                2.7.7.2 FAD synthase

Engineering

Engineering on EC 2.7.7.2 - FAD synthase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
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
F128A
loss of NMNAT activity
F128K
loss of NMNAT activity
F128W
mutant retains NMNAT activity
F206A
mutation at the macromolecular interface between two protomers within the trimer
F206K
mutation at the macromolecular interface between two protomers within the trimer
F206W
mutation at the macromolecular interface between two protomers within the trimer
F62A
loss of NMNAT activity
F62K
loss of NMNAT activity
F62W
mutant retains NMNAT activity
H28A
loss of both riboflavin kinase and FAD synthetase activities
H28D
loss of both riboflavin kinase and FAD synthetase activities
H31D
residual activity, involved in the stabilisation of the phosphate groups and the adenine moiety of ATP and the phosophate of FMN
K202A
mutation at the macromolecular interface between two protomers within the trimer
L304K
mutation at the macromolecular interface between two protomers within the trimer
L98A
mutation totally prevents the binding of FMN and/or FAD. Residues P56, P58 and L98 shape the isoalloxazine site to place the FMN- and FAD-reacting phosphates in optimal geometry for catalysis
L98K
mutation totally prevents the binding of FMN and/or FAD. Residues P56, P58 and L98 shape the isoalloxazine site to place the FMN- and FAD-reacting phosphates in optimal geometry for catalysis
L98W
residues P56, P58 and L98 shape the isoalloxazine site to place the FMN- and FAD-reacting phosphates in optimal geometry for catalysis
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
Y106A
loss of NMNAT activity
Y106K
loss of NMNAT activity
Y106W
mutant retains NMNAT activity
C126S
the mutation does not reduce the protein's heat stability or solubility, the mutant contains less than 0.8 and less than 0.08 mol of Mg and Fe per protomer. In the presence of MgCl2, the mutant has activity about 2times higher than that of the wild type enzyme. The activity of the mutant in presence of Co2+ is very low
C143S
the mutation does not reduce the protein's heat stability or solubility, the mutant contains less than 0.8 and less than 0.08 mol of Mg and Fe per protomer. In the presence of MgCl2, the mutant has activity approximately wild type activity. The activity of the mutant in presence of Co2+ is very low
D168A
site-directed mutagenesis, the mutant shows altered kinetics compared to the wild-type enzyme
D181A
site-directed mutagenesis, the mutant shows reduced sensitivity to inhibition by FAD compared to the wild-type enzyme and has a much faster turnover rate than the wild-type enzyme
D66A
site-directed mutagenesis, inactive mutant
N62A
site-directed mutagenesis, the mutant shows altered kinetics compared to the wild-type enzyme
N62S
site-directed mutagenesis, the mutant shows altered kinetics compared to the wild-type enzyme
R297A
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