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2'-deoxy-2-ethynyladenosyl-L-methionine + fluoride
2'-deoxy-2-ethynyl-5'-fluoroadenosine + L-methionine
-
-
-
r
2'-deoxyadenosyl-L-methionine + fluoride
2'-deoxy-5'-fluoroadenosine + L-methionine
5'-deoxy-5'-chloroadenosine + L-methionine
S-adenosyl-L-methionine + chloride
-
-
-
r
5'-deoxy-5'-chloroadenosine + L-selenomethionine
S-adenosyl-L-selenomethionine + chloride
use of L-selenomethionine increases the yield by around 2fold
-
-
r
5'-deoxy-5'-fluoroadenosine + L-selenomethionine
Se-adenosyl-L-selenomethionine + fluoride
-
-
-
r
5-deoxy-5'-bromoadenosine + fluoride
5-deoxy-5'-fluoroadenosine + bromide
-
-
-
r
5-deoxy-5'-chloroadenosine + L-methionine
S-adenosyl-L-methionine + chloride
-
-
-
r
5-deoxy-5'-iodoadenosine + fluoride
5-deoxy-5'-fluoroadenosine + iodide
-
-
-
r
methylaza-S-adenosyl-L-methionine + fluoride
?
S-(2-amino-6-deaminoadenosyl)-L-methionine + fluoride
2-amino-5-deamino-5'-deoxy-5'-fluoroadenosine + L-methionine
-
-
-
?
S-(2-aminoadenosyl)-L-methionine + fluoride
2-amino-5'-deoxy-5'-fluoroadenosine + L-methionine
-
-
-
?
S-(2-chloroadenosyl)-L-methionine + fluoride
2-chloro-5'-deoxy-5'-fluoroadenosine + L-methionine
-
-
-
?
S-(2-ethynyladenosyl)-L-methionine + fluoride
2-ethynyl-5'-deoxy-5'-fluoroadenosine + L-methionine
-
-
-
?
S-adenosyl-L-methionine + chloride
5'-deoxy-5'-chloroadenosine + L-methionine
S-adenosyl-L-methionine + fluoride
5'-deoxy-5'-fluoroadenosine + L-methionine
additional information
?
-
2'-deoxyadenosyl-L-methionine + fluoride
2'-deoxy-5'-fluoroadenosine + L-methionine
-
-
-
r
2'-deoxyadenosyl-L-methionine + fluoride
2'-deoxy-5'-fluoroadenosine + L-methionine
-
-
in the reverse reaction the enzyme shows 10% activity with the 2'-deoxy compound compared to the activity with the 5'-derivative
-
r
2'-deoxyadenosyl-L-methionine + fluoride
2'-deoxy-5'-fluoroadenosine + L-methionine
-
C-F bond formation, substrate binding structure, NMR and mass spectrometry, overview
in the reverse reaction the enzyme shows 10% activity with the 2'-deoxy compound compared to the activity with the 5'-derivative
-
r
2'-deoxyadenosyl-L-methionine + fluoride
2'-deoxy-5'-fluoroadenosine + L-methionine
-
-
-
?
methylaza-S-adenosyl-L-methionine + fluoride
?
optimal molar ratio of substrate to enzyme in this reaction equals to 112:1 for methylaza-S-adenosyl-L-methionine, modelling of methylaza-S-adenosyl-L-methionine bound in the active site using crystal structure with PDB ID 2V7U, reaction kinetics
-
-
?
methylaza-S-adenosyl-L-methionine + fluoride
?
optimal molar ratio of substrate to enzyme in this reaction equals to 112:1 for methylaza-S-adenosyl-L-methionine, modelling of methylaza-S-adenosyl-L-methionine bound in the active site using crystal structure with PDB ID 2V7U, reaction kinetics
-
-
?
S-adenosyl-L-methionine + chloride
5'-deoxy-5'-chloroadenosine + L-methionine
-
-
-
-
r
S-adenosyl-L-methionine + chloride
5'-deoxy-5'-chloroadenosine + L-methionine
-
-
-
r
S-adenosyl-L-methionine + fluoride
5'-deoxy-5'-fluoroadenosine + L-methionine
-
-
-
?
S-adenosyl-L-methionine + fluoride
5'-deoxy-5'-fluoroadenosine + L-methionine
-
-
-
?
S-adenosyl-L-methionine + fluoride
5'-deoxy-5'-fluoroadenosine + L-methionine
-
-
-
?
S-adenosyl-L-methionine + fluoride
5'-deoxy-5'-fluoroadenosine + L-methionine
-
-
-
-
?
S-adenosyl-L-methionine + fluoride
5'-deoxy-5'-fluoroadenosine + L-methionine
-
-
-
?
S-adenosyl-L-methionine + fluoride
5'-deoxy-5'-fluoroadenosine + L-methionine
-
-
-
?
S-adenosyl-L-methionine + fluoride
5'-deoxy-5'-fluoroadenosine + L-methionine
-
-
-
-
?
S-adenosyl-L-methionine + fluoride
5'-deoxy-5'-fluoroadenosine + L-methionine
-
-
-
-
r
S-adenosyl-L-methionine + fluoride
5'-deoxy-5'-fluoroadenosine + L-methionine
-
-
-
?
S-adenosyl-L-methionine + fluoride
5'-deoxy-5'-fluoroadenosine + L-methionine
-
-
-
?
S-adenosyl-L-methionine + fluoride
5'-deoxy-5'-fluoroadenosine + L-methionine
-
-
-
-
?
S-adenosyl-L-methionine + fluoride
5'-deoxy-5'-fluoroadenosine + L-methionine
-
-
-
r
S-adenosyl-L-methionine + fluoride
5'-deoxy-5'-fluoroadenosine + L-methionine
-
involved in production of toxic fluoroacetate
-
-
?
S-adenosyl-L-methionine + fluoride
5'-deoxy-5'-fluoroadenosine + L-methionine
-
highly specific for S-adenosyl-L-methionine, which is tightly bound to the enzyme at the interface between C-terminal domain of one monomer and the N-terminal domain of the neighbouring monomer
-
-
?
S-adenosyl-L-methionine + fluoride
5'-deoxy-5'-fluoroadenosine + L-methionine
-
reaction mechanism analysis utilizing a stereospecifically labelled substrate (5'R)-[5'-2H]-ATP in a coupled assay, inversion of configuration consistent with a SN2 reaction mechanism
i.e. 5'-FDA, NMR product analysis
-
?
S-adenosyl-L-methionine + fluoride
5'-deoxy-5'-fluoroadenosine + L-methionine
-
first committed enzymatic step on the biosynthetic pathway to the fluorometabolites fluoroacetate and 4-fluorothreonine
-
-
?
S-adenosyl-L-methionine + fluoride
5'-deoxy-5'-fluoroadenosine + L-methionine
-
C-F bond formation, substrate binding structure, NMR and mass spectrometry, overview
-
-
r
S-adenosyl-L-methionine + fluoride
5'-deoxy-5'-fluoroadenosine + L-methionine
-
C-F bond formation, the enzyme catalyses an SN2 type reaction mechanism
-
-
?
S-adenosyl-L-methionine + fluoride
5'-deoxy-5'-fluoroadenosine + L-methionine
-
18F-tagged substrate with 3 L-amino acid oxidase to remove the byproduct L-methionine enhancing the production reaction, 37°C, 100 mM Tris-HCl buffer, pH 7.5, up to 4 hours, to produce 18F-tagged product, other enzymes can be added to produce several types of nucleosides
-
-
?
S-adenosyl-L-methionine + fluoride
5'-deoxy-5'-fluoroadenosine + L-methionine
-
20 mg water-absorbing polymer in ionic liquid or 50 mM Tris-HCl buffer, pH 8.0, 50 nM S-adenosyl-L-methionine, 4 mircoM KF, 37°C, exteraction of product 5'-deoxy-5'-fluoroadenosine with diethyl ether
-
-
?
S-adenosyl-L-methionine + fluoride
5'-deoxy-5'-fluoroadenosine + L-methionine
optimal molar ratio of substrate to enzyme in this reaction equals to 19:1 for S-adenosyl-L-methionine
-
-
?
S-adenosyl-L-methionine + fluoride
5'-deoxy-5'-fluoroadenosine + L-methionine
-
-
-
?
S-adenosyl-L-methionine + fluoride
5'-deoxy-5'-fluoroadenosine + L-methionine
-
-
-
?
S-adenosyl-L-methionine + fluoride
5'-deoxy-5'-fluoroadenosine + L-methionine
-
-
-
?
S-adenosyl-L-methionine + fluoride
5'-deoxy-5'-fluoroadenosine + L-methionine
optimal molar ratio of substrate to enzyme in this reaction equals to 19:1 for S-adenosyl-L-methionine
-
-
?
S-adenosyl-L-methionine + fluoride
5'-deoxy-5'-fluoroadenosine + L-methionine
-
-
-
?
S-adenosyl-L-methionine + fluoride
5'-deoxy-5'-fluoroadenosine + L-methionine
-
-
-
r
S-adenosyl-L-methionine + fluoride
5'-deoxy-5'-fluoroadenosine + L-methionine
-
-
-
?
S-adenosyl-L-methionine + fluoride
5'-deoxy-5'-fluoroadenosine + L-methionine
-
-
-
?
additional information
?
-
-
fluoroacetate and 4-fluorothreonine accumulate in the fermentation media of Streptomyces cattleya at the mM level, when a fluoride source is added to the growth medium
-
-
?
additional information
?
-
-
fluorinase coupled enzyme systems for the synthesis of various 18F-labelled compounds, overview
-
-
?
additional information
?
-
-
substrate specificity, the enzyme does not require a planar ribose conformation of the substrate to catalyse C-F bond formation, overview, the enzyme catalyzes also transhalogenation from 2'-deoxy-5'-chloroadenosine to 2'-deoxy-fluoroadenosine via 2'-deoxy-SeAM, overview
-
-
?
additional information
?
-
the enzyme binds 5',5'-dideoxy-5'-fluoroadenosine with similar affinity as 5'-deoxy-5'-fluoroadenosine, but does not show formation of Se-adenosyl-L-selenomethionine with added L-selenomethionine as it does with 5'-deoxy-5'-fluoroadenosine. The difluoromethyl group bridges interactions that are essential for activation of the single fluorine in 5'-deoxy-5'-fluoroadenosine. An unusual hydrogen bonding interaction between the hydrogen of the difluoromethyl group and one of the hydroxyl oxygens of the tartrate ligand is also observed. The bridging interactions, coupled with the inherently stronger C-F bond in the difluoromethyl group, offers an explanation for why no reaction is observed
-
-
?
additional information
?
-
the enzyme has a specificity tolerance at the 2-position of the adenine base, replacement of hydrogen with an acetylene group at this position gives the modified substrate 5'-chlorodeoxy-2-ethynyladenosine which is an efficient substrate for transhalogenation in the presence of Se-adenosyl-L-selenomethionine. The fluorinase catalyzes a reversible transhalogenation of 5'-chlorodeoxy-2-ethynyladenosine to 5'-fluorodeoxy-2-ethynyladenosine and vice versa using L-selenomethionine and Cl- or F-, respectively. The enzyme is also active in transhalogenation with 5'-chlorodeoxy-2-ethynyladenosine linked to RGD peptides via a PEG linker, overview. The tolerance of the fluorinase to large multimeric peptides suggests that the C-2 position of a chlorinated nucleoside represents a site for the attachment of a diverse range of peptide cargos for use in enzymatic fluorination
-
-
?
additional information
?
-
the fluorinase catalyzes a transhalogenation of 5'-chlorodeoxy-2-ethynyladenosine to 5'-fluorodeoxy-2-ethynyladenosine, substrate specificity, the enzyme does have a specificity weakness at the C-2 position of adenine, overview
-
-
?
additional information
?
-
the fluorinase catalyzes a transhalogenation of 5'-chlorodeoxy-2-ethynyladenosine to 5'-fluorodeoxy-2-ethynyladenosinesubstrate specificity. A two-step radiolabelling protocol of a cancer relevant cRGD peptide is described where the fluorinase enzyme is used to catalyse a transhalogenation reaction to generate [18F]-5'-fluoro-5'-deoxy-2-ethynyladenosine, followed by a radiolabelling reaction with an azide tethered cRGD peptide
-
-
?
additional information
?
-
by coupling the reactions, conversion of 5'-deoxy-5'-chloroadenosine to 5'-fluoro-5'-deoxyadenosine can be achieved
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
S-adenosyl-L-methionine + fluoride
5'-deoxy-5'-fluoroadenosine + L-methionine
additional information
?
-
-
fluoroacetate and 4-fluorothreonine accumulate in the fermentation media of Streptomyces cattleya at the mM level, when a fluoride source is added to the growth medium
-
-
?
S-adenosyl-L-methionine + fluoride
5'-deoxy-5'-fluoroadenosine + L-methionine
-
-
-
?
S-adenosyl-L-methionine + fluoride
5'-deoxy-5'-fluoroadenosine + L-methionine
-
-
-
?
S-adenosyl-L-methionine + fluoride
5'-deoxy-5'-fluoroadenosine + L-methionine
-
-
-
-
?
S-adenosyl-L-methionine + fluoride
5'-deoxy-5'-fluoroadenosine + L-methionine
-
-
-
?
S-adenosyl-L-methionine + fluoride
5'-deoxy-5'-fluoroadenosine + L-methionine
-
-
-
?
S-adenosyl-L-methionine + fluoride
5'-deoxy-5'-fluoroadenosine + L-methionine
-
-
-
-
?
S-adenosyl-L-methionine + fluoride
5'-deoxy-5'-fluoroadenosine + L-methionine
-
-
-
-
r
S-adenosyl-L-methionine + fluoride
5'-deoxy-5'-fluoroadenosine + L-methionine
-
-
-
?
S-adenosyl-L-methionine + fluoride
5'-deoxy-5'-fluoroadenosine + L-methionine
-
-
-
?
S-adenosyl-L-methionine + fluoride
5'-deoxy-5'-fluoroadenosine + L-methionine
-
-
-
-
?
S-adenosyl-L-methionine + fluoride
5'-deoxy-5'-fluoroadenosine + L-methionine
-
-
-
r
S-adenosyl-L-methionine + fluoride
5'-deoxy-5'-fluoroadenosine + L-methionine
-
involved in production of toxic fluoroacetate
-
-
?
S-adenosyl-L-methionine + fluoride
5'-deoxy-5'-fluoroadenosine + L-methionine
-
first committed enzymatic step on the biosynthetic pathway to the fluorometabolites fluoroacetate and 4-fluorothreonine
-
-
?
S-adenosyl-L-methionine + fluoride
5'-deoxy-5'-fluoroadenosine + L-methionine
-
18F-tagged substrate with 3 L-amino acid oxidase to remove the byproduct L-methionine enhancing the production reaction, 37°C, 100 mM Tris-HCl buffer, pH 7.5, up to 4 hours, to produce 18F-tagged product, other enzymes can be added to produce several types of nucleosides
-
-
?
S-adenosyl-L-methionine + fluoride
5'-deoxy-5'-fluoroadenosine + L-methionine
-
20 mg water-absorbing polymer in ionic liquid or 50 mM Tris-HCl buffer, pH 8.0, 50 nM S-adenosyl-L-methionine, 4 mircoM KF, 37°C, exteraction of product 5'-deoxy-5'-fluoroadenosine with diethyl ether
-
-
?
S-adenosyl-L-methionine + fluoride
5'-deoxy-5'-fluoroadenosine + L-methionine
-
-
-
?
S-adenosyl-L-methionine + fluoride
5'-deoxy-5'-fluoroadenosine + L-methionine
-
-
-
?
S-adenosyl-L-methionine + fluoride
5'-deoxy-5'-fluoroadenosine + L-methionine
-
-
-
?
S-adenosyl-L-methionine + fluoride
5'-deoxy-5'-fluoroadenosine + L-methionine
-
-
-
?
S-adenosyl-L-methionine + fluoride
5'-deoxy-5'-fluoroadenosine + L-methionine
-
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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0.0084 - 0.0593
5'-deoxy-5'-chloroadenosine
0.0097
5-deoxy-5'-bromoadenosine
37°C, direct displacement reaction in the absence of L-methionine or S-adenosyl-L-methionine, pH not specified in the publication
0.0008 - 0.42
S-adenosyl-L-methionine
0.0084
5'-deoxy-5'-chloroadenosine
wild-type, pH not specified in the publication, temperature not specified in the publication
0.0095
5'-deoxy-5'-chloroadenosine
mutant F213Y/A279L, pH not specified in the publication, temperature not specified in the publication
0.0593
5'-deoxy-5'-chloroadenosine
mutant A279Y, pH not specified in the publication, temperature not specified in the publication
1.36
fluoride
-
mutant enzyme S158G, in 20 mM sodium phosphate buffer (pH 7.8), at 25°C
2.167
fluoride
pH 7.5, 26°C, recombinant enzyme
4.153
fluoride
pH 7.5, 26°C, recombinant enzyme
5.4
fluoride
-
mutant enzyme S158A, in 20 mM sodium phosphate buffer (pH 7.8), at 25°C
8.2
fluoride
pH not specified in the publication, temperature not specified in the publication
10
fluoride
about, during turnover, pH and temperature not specified in the publication
10.2
fluoride
-
wild type enzyme, in 20 mM sodium phosphate buffer (pH 7.8), at 25°C
18.4
fluoride
-
mutant enzyme T80S, in 20 mM sodium phosphate buffer (pH 7.8), at 25°C
36.8
fluoride
-
mutant enzyme T80A, in 20 mM sodium phosphate buffer (pH 7.8), at 25°C
0.0008
S-adenosyl-L-methionine
-
mutant enzyme S158G, in 20 mM sodium phosphate buffer (pH 7.8), at 25°C
0.003
S-adenosyl-L-methionine
-
mutant enzyme T80A, in 20 mM sodium phosphate buffer (pH 7.8), at 25°C
0.0047
S-adenosyl-L-methionine
-
mutant enzyme T80S, in 20 mM sodium phosphate buffer (pH 7.8), at 25°C
0.0065
S-adenosyl-L-methionine
-
wild type enzyme, in 20 mM sodium phosphate buffer (pH 7.8), at 25°C
0.007
S-adenosyl-L-methionine
pH not specified in the publication, temperature not specified in the publication
0.0092
S-adenosyl-L-methionine
-
mutant enzyme S158A, in 20 mM sodium phosphate buffer (pH 7.8), at 25°C
0.0092
S-adenosyl-L-methionine
mutant F213Y/A279L, pH not specified in the publication, temperature not specified in the publication
0.01
S-adenosyl-L-methionine
about, during turnover, pH and temperature not specified in the publication
0.0222
S-adenosyl-L-methionine
mutant A279Y, pH not specified in the publication, temperature not specified in the publication
0.0346
S-adenosyl-L-methionine
wild-type, pH not specified in the publication, temperature not specified in the publication
0.0351
S-adenosyl-L-methionine
(LELELKLK)2-tagged enzyme, pH 6.0, 40°C
0.0362
S-adenosyl-L-methionine
wild-type, pH 6.0, 40°C
0.0411
S-adenosyl-L-methionine
LLLLLLKD-tagged enzyme, pH 6.0, 50°C
0.0721
S-adenosyl-L-methionine
EWLKAFYEKVLEKLKELF-tagged enzyme, pH 6.0, 60°C
0.21
S-adenosyl-L-methionine
pH 7.5, 26°C, recombinant enzyme
0.416
S-adenosyl-L-methionine
pH 7.5, 26°C, recombinant enzyme
0.42
S-adenosyl-L-methionine
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.0022 - 0.0643
5'-deoxy-5'-chloroadenosine
0.0003
5-deoxy-5'-bromoadenosine
37°C, direct displacement reaction in the absence of L-methionine or S-adenosyl-L-methionine, pH not specified in the publication
0.000083 - 0.074
S-adenosyl-L-methionine
0.0022
5'-deoxy-5'-chloroadenosine
wild-type, pH not specified in the publication, temperature not specified in the publication
0.0088
5'-deoxy-5'-chloroadenosine
mutant A279Y, pH not specified in the publication, temperature not specified in the publication
0.0643
5'-deoxy-5'-chloroadenosine
mutant F213Y/A279L, pH not specified in the publication, temperature not specified in the publication
0.000012
fluoride
-
mutant enzyme S158G, in 20 mM sodium phosphate buffer (pH 7.8), at 25°C
0.000013
fluoride
-
mutant enzyme S158G, in 20 mM sodium phosphate buffer (pH 7.8), at 25°C
0.000067
fluoride
-
mutant enzyme T80A, in 20 mM sodium phosphate buffer (pH 7.8), at 25°C
0.0001
fluoride
-
mutant enzyme S158A, in 20 mM sodium phosphate buffer (pH 7.8), at 25°C
0.001
fluoride
-
mutant enzyme T80S, in 20 mM sodium phosphate buffer (pH 7.8), at 25°C
0.001
fluoride
-
wild type enzyme, in 20 mM sodium phosphate buffer (pH 7.8), at 25°C
0.0012
fluoride
pH 7.5, 26°C, recombinant enzyme
0.0018
fluoride
pH 7.5, 26°C, recombinant enzyme
0.000083
S-adenosyl-L-methionine
-
mutant enzyme T80A, in 20 mM sodium phosphate buffer (pH 7.8), at 25°C
0.00015
S-adenosyl-L-methionine
-
mutant enzyme S158A, in 20 mM sodium phosphate buffer (pH 7.8), at 25°C
0.0003
S-adenosyl-L-methionine
mutant F213Y/A279L, pH not specified in the publication, temperature not specified in the publication
0.001
S-adenosyl-L-methionine
-
mutant enzyme T80S, in 20 mM sodium phosphate buffer (pH 7.8), at 25°C
0.0012
S-adenosyl-L-methionine
-
wild type enzyme, in 20 mM sodium phosphate buffer (pH 7.8), at 25°C
0.0018
S-adenosyl-L-methionine
mutant A279Y, pH not specified in the publication, temperature not specified in the publication
0.0021
S-adenosyl-L-methionine
pH 7.5, 26°C, recombinant enzyme
0.0022
S-adenosyl-L-methionine
(LELELKLK)2-tagged enzyme, pH 6.0, 40°C
0.0023
S-adenosyl-L-methionine
pH 7.5, 26°C, recombinant enzyme
0.0026
S-adenosyl-L-methionine
wild-type, pH 6.0, 40°C
0.0034
S-adenosyl-L-methionine
LLLLLLKD-tagged enzyme, pH 6.0, 50°C
0.0037
S-adenosyl-L-methionine
wild-type, pH not specified in the publication, temperature not specified in the publication
0.0046
S-adenosyl-L-methionine
pH not specified in the publication, temperature not specified in the publication
0.0047
S-adenosyl-L-methionine
EWLKAFYEKVLEKLKELF-tagged enzyme, pH 6.0, 60°C
0.074
S-adenosyl-L-methionine
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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D16N
-
3% activity compared to the wild type enzyme
F156A
-
3% activity compared to the wild type enzyme
F156V
-
25% activity compared to the wild type enzyme
S158A
-
38% activity compared to the wild type enzyme
S158G
-
8% activity compared to the wild type enzyme
T80A
-
15% activity compared to the wild type enzyme
T80S
-
95% activity compared to the wild type enzyme
A279L
mutant with increased activity towards unnatural substrates
A279Y
about 3fold improved conversion of the non-native substrate 5'-deoxy-5'-chloroadenosine into 5'-fluoro-5'-deoxyadenosine. Mutant displays an improved kcat value in the conversion of 5'-deoxy-5'-chloroadenosine into S-adenosyl-L-methionine but a reduced kcat value in the conversion of S-adenosyl-L-methionine into 5'-fluoro-5'-deoxyadenosine
F213Y
mutant with increased activity towards unnatural substrates
F213Y/ A279L
mutant with increased activity towards unnatural substrates
F213Y/A279L
about 3fold improved conversion of the non-native substrate 5'-deoxy-5'-chloroadenosine into 5'-fluoro-5'-deoxyadenosine. Mutant displays an improved kcat value in the conversion of 5'-deoxy-5'-chloroadenosine into S-adenosyl-L-methionine but a reduced kcat value in the conversion of S-adenosyl-L-methionine into 5'-fluoro-5'-deoxyadenosine
D16E
complete loss of activity, residue is crucial for substrate SAM binding
F156A
complete loss of activity, residue provides the rear of the hydrophobic pocket
S158A
20% of wild-type activity
T80A
complete loss of activity
T80S
40% loss of activity
Y77A
almost complete loss of activity
S158A
site-directed mutagenesis, recombinant mutant protein NobA-S158A completely loses fluorination activity
S158A
-
site-directed mutagenesis, recombinant mutant protein NobA-S158A completely loses fluorination activity
-
additional information
engineering of the enzyme by substrate modulation: An acetylene functionality at the C-2 position of the adenosine substrate projects from the active site into the solvent, for 18F fluorination of bioconjugated peptides by the enzyme, extending a polyethylene glycol linker from the terminus of the acetylene allows the presentation of bioconjugation cargo to the enzyme for 18F labelling, method development and evaluation, overview
additional information
immobilization of the purified recombinant enzyme on poly(glycidyl methacrylate-co-ethylene glycol dimethacrylate) (2:1) polymer monoliths, method development to imporve immobilization yields and enzyme activity, determination of stability of the immobilized enzyme and enzyme leakage, overview. The enzyme shows over 80% activity during 4 reaction cycles, and 20% activity remaining after the 6th cycle
additional information
the enzyme is used for [18F]-radiolabelling of bioactive peptides, overview
additional information
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immobilization of the purified recombinant enzyme on poly(glycidyl methacrylate-co-ethylene glycol dimethacrylate) (2:1) polymer monoliths, method development to imporve immobilization yields and enzyme activity, determination of stability of the immobilized enzyme and enzyme leakage, overview. The enzyme shows over 80% activity during 4 reaction cycles, and 20% activity remaining after the 6th cycle
-
additional information
fusion of self-assembling amphipathic peptides into the C-terminus of fluorinase leads to proteins capable of self-assembly to form nano-sized particles with different dimensions in aqueous solutions. Peptide LLLLLLKD-tagged enzyme displays improved enzyme activity, thermostability and reusability
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pharmacology
a two-step radiolabelling protocol of a cancer relevant cRGD peptide is described where the fluorinase enzyme is used to catalyse a transhalogenation reaction to generate [18F]-5'-fluoro-5'-deoxy-2-ethynyladenosine, followed by a click reaction to an azide tethered cRGD peptide. This protocol offers efficient radiolabelling of a biologically relevant peptide construct in water at pH 7.8, 37°C in 2 hours, which is metabolically stable in rats and retains high affinity for alphavbeta3 integrin
analysis
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the enzyme is applied as a catalyst for the efficient incorporation of [18F]-fluoride into [18F]-59-fluoro-59-deoxyadenosine, [18F]-59-fluoro-59-deoxyinosine and [18F]-5-fluoro-5-deoxyribose for positron emission tomography, PET, applications, useful for imaging tumors, monitoring the distribution of drugs and identifying cell and receptor degeneration in the brain
analysis
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the fluorinase enzyme from Streptomyces cattleya is applied as a catalyst for the efficient incorporation of [18F]-fluoride into [18F]-59-fluoro-59-deoxyadenosine, [18F]-59-fluoro-59-deoxyinosine and [18F]-5-fluoro-5-deoxyribose for positron emission tomography, PET, applications, useful for imaging tumors, monitoring the distribution of drugs and identifying cell and receptor degeneration in the brain, coupled enzyme system, overview
biotechnology
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fluorochemical production (18F-labelled organic compounds) for medicinal chemistry research (positron emission tomography), when enzyme acts together with other enzymes in the fluorometabolite production (purine nucleoside phosphorylase, isomerase, aldolase, enzyme generating fluoroacetaldehyde in a retro-aldol reaction, fluoroacetaldehyde dehydrogenase or pyridoxal phosphate-dependent enzyme) to generate fluoroacetaldehyde and 4-fluorothreonine
biotechnology
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production of radiolabelled nucleosides as tracers for cancer cell uptake studies via positron emission tomography
biotechnology
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the rate of the enzymatic fluorination reaction can be enhanced by using ionic liquids and immobilizing the enzyme with a water-absorbing polymer which stabilizes the enzyme, 1-octyl-3-methylimidazolium hexafluorophosphate and 1-hexyl-3-methylimidazolium hexafluorophosphate raise the conversion yield 2.4times or 1.6times compared to Tris-HCl buffer, pH 8.0, 1-hexyl-3-methylimidazolium tetrafluoroborate, 1-octyl-3-methylimidazolium tetrafluoroborate, 1-octyl-3-methylimidazolium hexafluorophosphate, and 1-hexyl-3-methylimidazolium hexafluorophosphate increase total conversation yields 2.2times to 4times more in immobilized compared to non-immobilized enzyme
biotechnology
the enzyme is used for [18F]-radiolabelling of bioactive peptides, overview
synthesis
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the enzyme is used in biotransformation reaction for production of fluorinated compounds, biotransformation protocols for coupled reaction systems, overview
synthesis
induced production of fluorosalinosporamide by replacing the chlorinase gene salL from Salinispora tropica with the fluorinase gene flA. Maximum yields of 4 mg/l fluorosalinosporamide production are detected at pH 6.0. The fluorosalinosporamide production yields are comparable to those attained through mutasynthesis. The major fluorinated component in the Salinispora tropica salL- flA+ extract is fluorosalinosporamide
synthesis
one-pot three-step continuous enzymatic synthesis of 5-fluoro-5-deoxy-D-ribose from ATP and L-methionine using S-adenosyl-L-methionine synthase, fluorinase and methylthioadenosine nucleosidase in the presence of fluoride ions. The conversion yield is 22.6% of 5-fluoro-5-deoxy-D-ribose from ATP, while the fluoride ions are generated from BF4 ionic liquids and/or the biodegradation of benzotrifluoride in the synthetic process
synthesis
preparation of sodium [18F]-fluoroacetate by generation of 5'-[18F]-fluoro-5'-deoxyadenosine by a fluorinase catalysed reaction of S-adenosyl-L-methionine with no carrier added [18F]-fluoride and then oxidation to [18F]-fluoroacetate by a Kuhn-Roth oxidative degradation. Na [18F]-fluoroacetate can be synthesized in 96% radiochemical purity
synthesis
a two-step radiolabelling protocol of a cancer relevant cRGD peptide is described where the fluorinase enzyme is used to catalyse a transhalogenation reaction to generate [18F]-5'-fluoro-5'-deoxy-2-ethynyladenosine, followed by a click reaction to an azide tethered cRGD peptide. This protocol offers efficient radiolabelling of a biologically relevant peptide construct in water at pH 7.8, 37°C in 2 hours, which is metabolically stable in rats and retains high affinity for alphavbeta3 integrin
synthesis
substrate tolerance allows a peptide cargo to be tethered to a 5'-chloro-5'-deoxynucleoside substrate for transhalogenation by the enzyme to a 5'-fluoro-5-deoxynucleoside. The reaction is successfully extended from that previously reported for a monomeric cyclic peptide (cRGD) to cargoes of dendritic scaffolds carrying two and four cyclic peptide motifs. The RGD peptide sequence is known to bind upregulated alphaVbeta3 integrin motifs on the surface of cancer cells and it is demonstrated that the fluorinated products have a higher affinity to alphaVbeta3 integrin than their monomeric counterparts. Tolerance of the fluorinase to these large multimeric peptides suggests that the C-2 position of a chlorinated nucleoside represents a site for the attachment of a diverse range of peptide cargos for use in enzymatic fluorination
synthesis
the enzyme is applicated in positron emission tomography (PET) as a result of its ability to catalyze C-18F bond formation in the presence of [18F]fluoride as the nucleophile. The enzymatic process has a technical advantage in the PET context because [18F]fluoride is generated in the cyclotron as a dilute solution in [18O]water, and the enzyme can use this form of aqueous fluoride directly. This feature obviates the usual requirement to secure dry [18F]fluoride by ion-exchange chromatography. The enzymatic process therefore offers the possibility to directly radiolabel biomolecules in the aqueous phase
synthesis
deveopment of a coupled chlorinase-fluorinase system for rapid transhalogenation. The chlorinase shares a substrate tolerance with the fluorinase, enabling these two enzymes to cooperatively produce 5'-fluorodeoxy-2-ethynyladenosine (5'-FDEA) in up to 91.6% yield in 1 h
synthesis
-
preparation of sodium [18F]-fluoroacetate by generation of 5'-[18F]-fluoro-5'-deoxyadenosine by a fluorinase catalysed reaction of S-adenosyl-L-methionine with no carrier added [18F]-fluoride and then oxidation to [18F]-fluoroacetate by a Kuhn-Roth oxidative degradation. Na [18F]-fluoroacetate can be synthesized in 96% radiochemical purity
-
synthesis
-
induced production of fluorosalinosporamide by replacing the chlorinase gene salL from Salinispora tropica with the fluorinase gene flA. Maximum yields of 4 mg/l fluorosalinosporamide production are detected at pH 6.0. The fluorosalinosporamide production yields are comparable to those attained through mutasynthesis. The major fluorinated component in the Salinispora tropica salL- flA+ extract is fluorosalinosporamide
-
synthesis
-
one-pot three-step continuous enzymatic synthesis of 5-fluoro-5-deoxy-D-ribose from ATP and L-methionine using S-adenosyl-L-methionine synthase, fluorinase and methylthioadenosine nucleosidase in the presence of fluoride ions. The conversion yield is 22.6% of 5-fluoro-5-deoxy-D-ribose from ATP, while the fluoride ions are generated from BF4 ionic liquids and/or the biodegradation of benzotrifluoride in the synthetic process
-
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Isolation and characterisation of 5-fluorodeoxyadenosine synthase, a fluorination enzyme from Streptomyces cattleya
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Streptomyces cattleya
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Biosynthesis of an organofluorine molecule
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Streptomyces cattleya
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Streptomyces cattleya
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Crystal structure and mechanism of a bacterial fluorinating enzyme
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Streptomyces cattleya
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Fluorinase mediated C-18F bond formation, an enzymatic tool for PET labelling
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Recent developments on the fluorinase from Streptomyces cattleya
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Streptomyces cattleya
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Substrate specificity in enzymatic fluorination. The fluorinase from Streptomyces cattleya accepts 2-deoxyadenosine substrates
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2006
Streptomyces cattleya
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Mechanism of enzymatic fluorination in Streptomyces cattleya
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Streptomyces cattleya
brenda
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Streptomyces cattleya
brenda
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Fluorinase-coupled base swaps: Synthesis of 18F-5'-Deoxy-5'-fluorouridines
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2008
Streptomyces cattleya
brenda
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Utility of ionic liquid for improvement of fluorination reaction with immobilized fluorinase
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2009
Streptomyces cattleya
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The fluorinase from Streptomyces cattleya is also a chlorinase
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45
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2006
Streptomyces cattleya
brenda
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44
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Fluorinase mediated chemoenzymatic synthesis of [18F]-fluoroacetate
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46
7819-7821
2010
Streptomyces cattleya (F8JPG4), Streptomyces cattleya ATCC 35852 (F8JPG4)
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One-pot three-step continuous enzymatic synthesis of 5-fluoro-5-deoxy-D-ribose
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2011
Streptomyces cattleya (F8JPG4), Streptomyces cattleya NBRC14057 (F8JPG4)
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brenda
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Engineering fluorometabolite production: fluorinase expression in Salinispora tropica yields fluorosalinosporamide
J. Nat. Prod.
73
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2010
Streptomyces cattleya (F8JPG4), Streptomyces cattleya, Streptomyces cattleya ATCC 35852 (F8JPG4)
brenda
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A localized tolerance in the substrate specificity of the fluorinase enzyme enables last-step 18F fluorination of a RGD peptide under ambient aqueous conditions
Angew. Chem. Int. Ed. Engl.
53
8913-8918
2014
Streptomyces cattleya (Q70GK9)
brenda
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Exploration of a potential difluoromethyl-nucleoside substrate with the fluorinase enzyme
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64
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2016
Streptomyces cattleya (Q70GK9)
brenda
Thompson, S.; Onega, M.; Ashworth, S.; Fleming, I.N.; Passchier, J.; OHagan, D.
A two-step fluorinase enzyme mediated (18)F labelling of an RGD peptide for positron emission tomography
Chem. Commun. (Camb.)
51
13542-13545
2015
Streptomyces cattleya (Q70GK9)
brenda
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Enzymatic fluorination and biotechnological developments of the fluorinase
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115
634-649
2015
Nocardia brasiliensis, Streptomyces xinghaiensis (A0A068VNW5), Streptomyces cattleya (Q70GK9), Actinoplanes sp. (R4LHX8), Streptomyces sp. (W0W999), Streptomyces xinghaiensis NRRL B-24674 (A0A068VNW5), Actinoplanes sp. N902-109 (R4LHX8)
brenda
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Characterization of a SAM-dependent fluorinase from a latent biosynthetic pathway for fluoroacetate and 4-fluorothreonine formation in Nocardia brasiliensis
F1000Res.
3
61-73
2014
Streptomyces cattleya (Q70GK9), Streptomyces cattleya, Nocardia brasiliensis (W8JNL4), Nocardia brasiliensis, Nocardia brasiliensis ATCC 700358 (W8JNL4), Nocardia brasiliensis ATCC 700358, Streptomyces cattleya DSM 46488 (Q70GK9)
brenda
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Polymer-immobilized fluorinase: recyclable catalyst for fluorination reactions
J. Mol. Catal. B
92
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2013
Streptomyces cattleya (F8JPG4), Streptomyces cattleya NBRC14057 (F8JPG4)
-
brenda
Sergeev, M.; Morgia, F.; Javed, M.; Doi, M.; Keng, P.
Enzymatic radiofluorination: fluorinase accepts methylaza-analog of SAM as substrate for FDA synthesis
J. Mol. Catal. B
97
74-79
2013
Streptomyces cattleya (F8JPG4), Streptomyces cattleya NBRC14057 (F8JPG4)
-
brenda
Thompson, S.; Fleming, I.N.; OHagan, D.
Enzymatic transhalogenation of dendritic RGD peptide constructs with the fluorinase
Org. Biomol. Chem.
14
3120-3129
2016
Streptomyces cattleya (Q70GK9)
brenda
Sun, H.; Yeo, W.L.; Lim, Y.H.; Chew, X.; Smith, D.J.; Xue, B.; Chan, K.P.; Robinson, R.C.; Robins, E.G.; Zhao, H.; Ang, E.L.
Directed evolution of a fluorinase for improved fluorination efficiency with a non-native substrate
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55
14277-14280
2016
Streptomyces sp. MA37 (W0W999)
brenda
Tu, C.; Zhou, J.; Peng, L.; Man, S.; Ma, L.
Self-assembled nano-aggregates of fluorinases demonstrate enhanced enzymatic activity, thermostability and reusability
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8
648-656
2020
Streptomyces xinghaiensis (A0A068VNW5)
brenda
Yeo, W.; Chew, X.; Smith, D.; Chan, K.; Sun, H.; Zhao, H.; Lim, Y.; Ang, E.
Probing the molecular determinants of fluorinase specificity
Chem. Commun. (Camb.)
53
2559-2562
2017
Streptomyces sp. MA37 (W0W999)
brenda
Sun, H.; Zhao, H.; Ang, E.
A coupled chlorinase-fluorinase system with a high efficiency of trans-halogenation and a shared substrate tolerance
Chem. Commun. (Camb.)
54
9458-9461
2018
Streptomyces sp. MA37 (W0W999)
brenda
Lowe, P.T.; Cobb, S.L.; OHagan, D.
An enzymatic Finkelstein reaction fluorinase catalyses direct halogen exchange
Org. Biomol. Chem.
17
7493-7496
2019
Streptomyces cattleya (Q70GK9), Streptomyces cattleya
brenda
Sooklal, S.; De Koning, C.; Brady, D.; Rumbold, K.
Identification and characterisation of a fluorinase from Actinopolyspora mzabensis
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166
105508
2020
Actinopolyspora mzabensis (A0A1G9FQX8), Actinopolyspora mzabensis
brenda
Ma, L.; Li, Y.; Meng, L.; Deng, H.; Li, Y.; Zhang, Q.; Diao, A.
Biological fluorination from the sea Discovery of a SAM-dependent nucleophilic fluorinating enzyme from the marine-derived bacterium Streptomyces xinghaiensis NRRL B24674
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6
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2016
Streptomyces xinghaiensis (A0A068VNW5)
-
brenda