Information on EC 2.5.1.63 - adenosyl-fluoride synthase:
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The expected taxonomic range for this enzyme is: Streptomyces cattleya

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EC NUMBERCOMMENTARY
2.5.1.63-

RECOMMENDED NAMEGeneOntology No.
adenosyl-fluoride synthaseGO:0033846

REACTIONREACTION DIAGRAMCOMMENTARYORGANISM UNIPROT ACCESSION NO.LITERATURE
S-adenosyl-L-methionine + fluoride = 5'-deoxy-5'-fluoroadenosine + L-methionine
show the reaction diagram		----
S-adenosyl-L-methionine + fluoride = 5'-deoxy-5'-fluoroadenosine + L-methionine
show the reaction diagram		reaction mechanism, inversion of configuration consistent with a SN2 reaction mechanismStreptomyces cattleya, Streptomyces cattleya NRRL 8057-658449
S-adenosyl-L-methionine + fluoride = 5'-deoxy-5'-fluoroadenosine + L-methionine
show the reaction diagram		substrate binding structure involving F156, S158, Y177, and T80, nucleophilic substitution reaction mechanismStreptomyces cattleya, Streptomyces cattleya NRRL 8057-660001
S-adenosyl-L-methionine + fluoride = 5'-deoxy-5'-fluoroadenosine + L-methionine
show the reaction diagram		C-F bond formation, the enzyme catalyses an SN2 type reaction mechanismStreptomyces cattleya, Streptomyces cattleya NRRL 8057-673043
S-adenosyl-L-methionine + fluoride = 5'-deoxy-5'-fluoroadenosine + L-methionine
show the reaction diagram		reaction mechanism, overviewStreptomyces cattleya, Streptomyces cattleya NRRL 8057-675161

REACTION TYPEORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
adenosyl group transfer----
halogenation----

PATHWAYKEGG LinkMetaCyc Link
fluoroacetate and fluorothreonine biosynthesis-PWY-6644

SYSTEMATIC NAMEIUBMB Comments
S-adenosyl-L-methionine:fluoride adenosyltransferase-

SYNONYMSORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
5'-deoxy-5'-fluoroadenosine synthaseStreptomyces cattleya--660001
5'-FDA synthaseStreptomyces cattleya--658449, 675161
5'-FDASStreptomyces cattleya--658449, 660001, 673043
5'-fluoro-5'-deoxy adenosine synthetaseStreptomyces cattleya--687280
5'-fluoro-5'-deoxyadenosine synthaseStreptomyces cattleya--673043, 675161, 703173
5’-fluorodeoxyadenosine synthase----
adenosyl-fluoride synthaseStreptomyces cattleya--709552
FDASStreptomyces cattleya--687280
flAStreptomyces cattleya--703173
flA proteinStreptomyces cattleya--703173
fluorinase----
fluorinaseStreptomyces cattleya NRRL 8057--673043, 675161
fluorinaseStreptomyces cattleya--673043, 675161, 676276, 703173, 710863
fluorinase enzymeStreptomyces cattleya--707137
fluorinase, S-adenosyl-L-methionine----
fluorination enzymeStreptomyces cattleya--660001
SAM fluorinase----

CAS REGISTRY NUMBERCOMMENTARY
438583-16-5-

ORGANISMCOMMENTARYLITERATURESEQUENCE CODESEQUENCE DB SOURCE
Streptomyces cattleya-637250, 637251, 658449, 673043, 675161, 676276, 687280, 703173, 707137, 709552, 710863--Manually annotated by BRENDA team
Streptomyces cattleyagene flA660001--Manually annotated by BRENDA team

GENERAL INFORMATIONORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
metabolismStreptomyces cattleya, Streptomyces cattleya NRRL 8057-first enzyme in the fluorometabolite pathway to produce the mammalian toxin fluoroacetate and the antibiotic 4-fluorothreonine703173
physiological functionStreptomyces cattleya NRRL 8057, Streptomyces cattleya-part of 4-fluorothreonine biosynthesis703173

SUBSTRATEPRODUCT                      REACTION DIAGRAMORGANISM UNIPROT ACCESSION NO. COMMENTARY/
Substrate		 LITERATURE/
Substrate		 COMMENTARY/
Product		 LITERATURE/
Product		 Reversibility
r=reversible
ir=irreversible
?=not specified
2'-deoxyadenosyl-L-methionine + fluoride2'-deoxy-5'-fluoroadenosine + L-methionine
show the reaction diagram		Streptomyces cattleya--675161in the reverse reaction the enzyme shows 10% activity with the 2'-deoxy compound compared to the activity with the 5'-derivative-r
S-adenosyl-L-methionine + chloride5'-deoxy-5'-chloroadenosine + L-methionine
show the reaction diagram		Streptomyces cattleya--710863--r
S-adenosyl-L-methionine + fluoride5'-deoxy-5'-fluoroadenosine + L-methionine
show the reaction diagram		Streptomyces cattleya--637250, 637251, 658449, 660001, 673043, 687280, 703173--?
S-adenosyl-L-methionine + fluoride5'-deoxy-5'-fluoroadenosine + L-methionine
show the reaction diagram		Streptomyces cattleya--675161--r
S-adenosyl-L-methionine + fluoride5'-deoxy-5'-fluoroadenosine + L-methionine
show the reaction diagram		Streptomyces cattleya-involved in production of toxic fluoroacetate637250---
S-adenosyl-L-methionine + fluoride5'-deoxy-5'-fluoroadenosine + L-methionine
show the reaction diagram		Streptomyces cattleya-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 monomer660001--?
S-adenosyl-L-methionine + fluoride5'-deoxy-5'-fluoroadenosine + L-methionine
show the reaction diagram		Streptomyces cattleya-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 mechanism658449i.e. 5'-FDA, NMR product analysis-?
S-adenosyl-L-methionine + fluoride5'-deoxy-5'-fluoroadenosine + L-methionine
show the reaction diagram		Streptomyces cattleya-first committed enzymatic step on the biosynthetic pathway to the fluorometabolites fluoroacetate and 4-fluorothreonine676276--?
S-adenosyl-L-methionine + fluoride5'-deoxy-5'-fluoroadenosine + L-methionine
show the reaction diagram		Streptomyces cattleya-C-F bond formation, substrate binding structure, NMR and mass spectrometry, overview676276--r
S-adenosyl-L-methionine + fluoride5'-deoxy-5'-fluoroadenosine + L-methionine
show the reaction diagram		Streptomyces cattleya-C-F bond formation, the enzyme catalyses an SN2 type reaction mechanism673043--?
S-adenosyl-L-methionine + fluoride5'-deoxy-5'-fluoroadenosine + L-methionine
show the reaction diagram		Streptomyces cattleya-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 nucleosides707137--?
S-adenosyl-L-methionine + fluoride5'-deoxy-5'-fluoroadenosine + L-methionine
show the reaction diagram		Streptomyces cattleya-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 ether709552--?
2'-deoxyadenosyl-L-methionine + fluoride2'-deoxy-5'-fluoroadenosine + L-methionine
show the reaction diagram		Streptomyces cattleya-C-F bond formation, substrate binding structure, NMR and mass spectrometry, overview676276in the reverse reaction the enzyme shows 10% activity with the 2'-deoxy compound compared to the activity with the 5'-derivative-r
additional information?-Streptomyces cattleya-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 medium675161---
additional information?-Streptomyces cattleya-fluorinase coupled enzyme systems for the synthesis of various 18F-labelled compounds, overview673043---
additional information?-Streptomyces cattleya-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, overview676276---

NATURAL SUBSTRATESNATURAL PRODUCTSREACTION DIAGRAMORGANISM UNIPROT ACCESSION NO.COMMENTARY SUBSTRATELITERATURE
(Substrate)		COMMENTARY PRODUCTLITERATURE
(Product)
S-adenosyl-L-methionine + fluoride5'-deoxy-5'-fluoroadenosine + L-methionine
show the reaction diagram		Streptomyces cattleya--658449, 660001, 673043, 703173, 675161--
S-adenosyl-L-methionine + fluoride5'-deoxy-5'-fluoroadenosine + L-methionine
show the reaction diagram		Streptomyces cattleya-involved in production of toxic fluoroacetate637250--
S-adenosyl-L-methionine + fluoride5'-deoxy-5'-fluoroadenosine + L-methionine
show the reaction diagram		Streptomyces cattleya-first committed enzymatic step on the biosynthetic pathway to the fluorometabolites fluoroacetate and 4-fluorothreonine676276--
S-adenosyl-L-methionine + fluoride5'-deoxy-5'-fluoroadenosine + L-methionine
show the reaction diagram		Streptomyces cattleya-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 nucleosides707137--
S-adenosyl-L-methionine + fluoride5'-deoxy-5'-fluoroadenosine + L-methionine
show the reaction diagram		Streptomyces cattleya-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 ether709552--
additional information?-Streptomyces cattleya-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 medium675161--

COFACTORORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATUREIMAGE
No entries in this field

METALS and IONS ORGANISM UNIPROT ACCESSION NO.COMMENTARY LITERATURE
K+Streptomyces cattleya, Streptomyces cattleya NRRL 8057-in the coupled assay with SAM synthase and fluorinase658449
Mg2+Streptomyces cattleya, Streptomyces cattleya NRRL 8057-in the coupled assay with SAM synthase and fluorinase658449
additional informationStreptomyces cattleya, Streptomyces cattleya NRRL 8057-Mg2+ at 1 mM does not affect enzyme activity637250

INHIBITORSORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
S-adenosyl-L-homocysteineStreptomyces cattleya-competent, competitive637250 2D-image
SinefunginStreptomyces cattleya, Streptomyces cattleya NRRL 8057-weak637250 2D-image

ACTIVATING COMPOUNDORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
EDTAStreptomyces cattleya, Streptomyces cattleya NRRL 8057-1 mM increases enzyme activity by 25%637250 2D-image

KM VALUE [mM]KM VALUE [mM] MaximumSUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
1.36-fluorideStreptomyces cattleya-mutant enzyme S158G, in 20 mM sodium phosphate buffer (pH 7.8), at 25°C687280 2D-image
5.4-fluorideStreptomyces cattleya-mutant enzyme S158A, in 20 mM sodium phosphate buffer (pH 7.8), at 25°C687280 2D-image
8.56-fluorideStreptomyces cattleya--637250 2D-image
10.2-fluorideStreptomyces cattleya-wild type enzyme, in 20 mM sodium phosphate buffer (pH 7.8), at 25°C687280 2D-image
18.4-fluorideStreptomyces cattleya-mutant enzyme T80S, in 20 mM sodium phosphate buffer (pH 7.8), at 25°C687280 2D-image
36.8-fluorideStreptomyces cattleya-mutant enzyme T80A, in 20 mM sodium phosphate buffer (pH 7.8), at 25°C687280 2D-image
0.0008-S-adenosyl-L-methionineStreptomyces cattleya-mutant enzyme S158G, in 20 mM sodium phosphate buffer (pH 7.8), at 25°C687280 2D-image
0.003-S-adenosyl-L-methionineStreptomyces cattleya-mutant enzyme T80A, in 20 mM sodium phosphate buffer (pH 7.8), at 25°C687280 2D-image
0.0047-S-adenosyl-L-methionineStreptomyces cattleya-mutant enzyme T80S, in 20 mM sodium phosphate buffer (pH 7.8), at 25°C687280 2D-image
0.0065-S-adenosyl-L-methionineStreptomyces cattleya-wild type enzyme, in 20 mM sodium phosphate buffer (pH 7.8), at 25°C687280 2D-image
0.0092-S-adenosyl-L-methionineStreptomyces cattleya-mutant enzyme S158A, in 20 mM sodium phosphate buffer (pH 7.8), at 25°C687280 2D-image
0.42-S-adenosyl-L-methionineStreptomyces cattleya--637250 2D-image

TURNOVER NUMBER [1/s] TURNOVER NUMBER MAXIMUM[1/s] SUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
0.000012-fluorideStreptomyces cattleya-mutant enzyme S158G, in 20 mM sodium phosphate buffer (pH 7.8), at 25°C687280 2D-image
0.000013-fluorideStreptomyces cattleya-mutant enzyme S158G, in 20 mM sodium phosphate buffer (pH 7.8), at 25°C687280 2D-image
0.000067-fluorideStreptomyces cattleya-mutant enzyme T80A, in 20 mM sodium phosphate buffer (pH 7.8), at 25°C687280 2D-image
0.0001-fluorideStreptomyces cattleya-mutant enzyme S158A, in 20 mM sodium phosphate buffer (pH 7.8), at 25°C687280 2D-image
0.001-fluorideStreptomyces cattleya-mutant enzyme T80S, in 20 mM sodium phosphate buffer (pH 7.8), at 25°C; wild type enzyme, in 20 mM sodium phosphate buffer (pH 7.8), at 25°C687280 2D-image
0.001-fluorideStreptomyces cattleya NRRL 8057-mutant enzyme T80S, in 20 mM sodium phosphate buffer (pH 7.8), at 25°C687280 2D-image
0.0012-fluorideStreptomyces cattleya, Streptomyces cattleya NRRL 8057--660001 2D-image
2-fluorideStreptomyces cattleya, Streptomyces cattleya NRRL 8057--660001 2D-image
0.000083-S-adenosyl-L-methionineStreptomyces cattleya-mutant enzyme T80A, in 20 mM sodium phosphate buffer (pH 7.8), at 25°C687280 2D-image
0.00015-S-adenosyl-L-methionineStreptomyces cattleya-mutant enzyme S158A, in 20 mM sodium phosphate buffer (pH 7.8), at 25°C687280 2D-image
0.001-S-adenosyl-L-methionineStreptomyces cattleya, Streptomyces cattleya NRRL 8057-mutant enzyme T80S, in 20 mM sodium phosphate buffer (pH 7.8), at 25°C687280 2D-image
0.0012-S-adenosyl-L-methionineStreptomyces cattleya, Streptomyces cattleya NRRL 8057-wild type enzyme, in 20 mM sodium phosphate buffer (pH 7.8), at 25°C687280 2D-image
0.074-S-adenosyl-L-methionineStreptomyces cattleya--660001 2D-image

kcat/KM VALUE [1/mMs-1]kcat/KM VALUE [1/mMs-1] MaximumSUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

Ki VALUE [mM]Ki VALUE [mM] MaximumINHIBITORORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
0.029-S-adenosyl-homocysteineStreptomyces cattleya, Streptomyces cattleya NRRL 8057--637250 2D-image

IC50 VALUE [mM]IC50 VALUE [mM] MaximumINHIBITORORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

SPECIFIC ACTIVITY [µmol/min/mg] SPECIFIC ACTIVITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
additional information-Streptomyces cattleya, Streptomyces cattleya NRRL 8057-development of a coupled assay with SAM synthase and fluorinase658449

pH OPTIMUMpH MAXIMUMORGANISM UNIPROT ACCESSION NO. COMMENTARYLITERATURE
7.9-Streptomyces cattleya-assay at660001

pH RANGEpH RANGE MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

TEMPERATURE OPTIMUMTEMPERATURE OPTIMUM MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
37-Streptomyces cattleya, Streptomyces cattleya NRRL 8057-assay at658449
37-Streptomyces cattleya, Streptomyces cattleya NRRL 8057-assay at660001
55-Streptomyces cattleya, Streptomyces cattleya NRRL 8057--637250

TEMPERATURE RANGE TEMPERATURE MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

pI VALUEpI VALUE MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

SOURCE TISSUE ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE SOURCE
culture condition:fluoride-grown cellStreptomyces cattleya, Streptomyces cattleya NRRL 8057--660001Manually annotated by BRENDA team

LOCALIZATION ORGANISM UNIPROT ACCESSION NO. COMMENTARY GeneOntology No. LITERATURE SOURCE
No entries in this field

PDBSCOPCATHORGANISM
1rqp, downloadSCOP (1rqp)CATH (1rqp)Streptomyces cattleya
1rqr, downloadSCOP (1rqr)CATH (1rqr)Streptomyces cattleya
2c2w, downloadSCOP (2c2w)CATH (2c2w)Streptomyces cattleya
2c4t, downloadSCOP (2c4t)CATH (2c4t)Streptomyces cattleya
2c4u, downloadSCOP (2c4u)CATH (2c4u)Streptomyces cattleya
2c5b, downloadSCOP (2c5b)CATH (2c5b)Streptomyces cattleya
2c5h, downloadSCOP (2c5h)CATH (2c5h)Streptomyces cattleya
2cbx, downloadSCOP (2cbx)CATH (2cbx)Streptomyces cattleya
2cc2, downloadSCOP (2cc2)CATH (2cc2)Streptomyces cattleya
2v7t, downloadSCOP (2v7t)CATH (2v7t)Streptomyces cattleya
2v7u, downloadSCOP (2v7u)CATH (2v7u)Streptomyces cattleya
2v7v, downloadSCOP (2v7v)CATH (2v7v)Streptomyces cattleya
2v7w, downloadSCOP (2v7w)CATH (2v7w)Streptomyces cattleya
2v7x, downloadSCOP (2v7x)CATH (2v7x)Streptomyces cattleya

MOLECULAR WEIGHT MOLECULAR WEIGHT MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
180000-Streptomyces cattleya, Streptomyces cattleya NRRL 8057-gel filtration637250

SUBUNITS ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
hexamerStreptomyces cattleya, Streptomyces cattleya NRRL 8057-6 * 32000, SDS-PAGE and electrospray mass spectrometry637250
hexamerStreptomyces cattleya, Streptomyces cattleya NRRL 8057-6 * 34402, (alpha,beta)3, recombinant enzyme, ESI-MS mass spectrometry660001
hexamerStreptomyces cattleya, Streptomyces cattleya NRRL 8057-a dimer of trimers675161
additional informationStreptomyces cattleya NRRL 8057, Streptomyces cattleya-the N-terminal domain has a central seven-stranded beta-sheet, which combines parallel and antiparallel strands sandwiched between alpha-helices, the C-terminal domain is composed of a five- and a four-stranded antiparallel beta-sheet660001

POSTTRANSLATIONAL MODIFICATION ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

Crystallization/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
-Streptomyces cattleya-687280
purified recombinant enzyme, free from tags or bound adenosine, complexed to 2'-deoxy-5'-fluoroadenosine, 4 mg/ml protein is incubated with 20 mM ligand at 25°C for 4 h, followed by crystallization using vapour diffusion against a reservoir containing 30% PEG 1000, 0.1 M phosphate-citrate pH 4.5, 0.2 M Li2SO4, X-ray diffraction structure determination and analysis at 2.4 A resolution, molecular replacementStreptomyces cattleya-676276
purified recombinant wild-type and selenomethionine labelled enzyme with bound S-adenosyl-L-methionine, X-ray diffraction structure determination and analysis at 1.9 A resolution, structure modelling of monomers a and bStreptomyces cattleya-660001
-Streptomyces cattleya NRRL 8057-687280
purified recombinant enzyme, free from tags or bound adenosine, complexed to 2'-deoxy-5'-fluoroadenosine, 4 mg/ml protein is incubated with 20 mM ligand at 25°C for 4 h, followed by crystallization using vapour diffusion against a reservoir containing 30% PEG 1000, 0.1 M phosphate-citrate pH 4.5, 0.2 M Li2SO4, X-ray diffraction structure determination and analysis at 2.4 A resolution, molecular replacementStreptomyces cattleya NRRL 8057-676276
purified recombinant wild-type and selenomethionine labelled enzyme with bound S-adenosyl-L-methionine, X-ray diffraction structure determination and analysis at 1.9 A resolution, structure modelling of monomers a and bStreptomyces cattleya NRRL 8057-660001

pH STABILITYpH STABILITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

TEMPERATURE STABILITYTEMPERATURE STABILITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARYLITERATURE
No entries in this field

GENERAL STABILITYORGANISM UNIPROT ACCESSION NO.LITERATURE
water stabilizes the enzyme, thus water-absorbing polymer and ionic liquid is used to immobilize the enzyme and keep it surrounded by waterStreptomyces cattleya, Streptomyces cattleya NRRL 8057-709552

ORGANIC SOLVENT ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

OXIDATION STABILITY ORGANISM UNIPROT ACCESSION NO. LITERATURE
No entries in this field

STORAGE STABILITY ORGANISM UNIPROT ACCESSION NO. LITERATURE
No entries in this field

Purification/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
-Streptomyces cattleya-637250, 703173
nickel-affinity columnStreptomyces cattleya-709552
recombinant His-tagged enzyme from Escherichia coli by nickel affinity chromatography and gel filtrationStreptomyces cattleya-660001
-Streptomyces cattleya NRRL 8057-637250, 703173
recombinant His-tagged enzyme from Escherichia coli by nickel affinity chromatography and gel filtrationStreptomyces cattleya NRRL 8057-660001

Cloned/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
expression in Escherichia coli BL21; expression in Escherichia coli BL21(DE3)Streptomyces cattleya-703173
expression of His-tagged enzyme in Escherichia coli BL21(DE3) pLysS with plasmid pET28b+Streptomyces cattleya-709552
gene flA, DNA sequence determination and analysis, overexpression of His-tagged enzyme in Escherichia coli strain BL21(DE3) and in strain B834(DE3), the latter results in the selenomethionine labeled enzymeStreptomyces cattleya-660001
mutant enzymes expressed in Escherichia coli C43 (DE3) cellsStreptomyces cattleya-687280
expression in Escherichia coli BL21; expression in Escherichia coli BL21(DE3)Streptomyces cattleya NRRL 8057-703173
gene flA, DNA sequence determination and analysis, overexpression of His-tagged enzyme in Escherichia coli strain BL21(DE3) and in strain B834(DE3), the latter results in the selenomethionine labeled enzymeStreptomyces cattleya NRRL 8057-660001
mutant enzymes expressed in Escherichia coli C43 (DE3) cellsStreptomyces cattleya NRRL 8057-687280

EXPRESSION ORGANISM UNIPROT ACCESSION NO. LITERATURE
No entries in this field

ENGINEERINGORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
D16AStreptomyces cattleya-inactive687280
D16NStreptomyces cattleya-3% activity compared to the wild type enzyme687280
D16SStreptomyces cattleya-inactive687280
F156AStreptomyces cattleya-3% activity compared to the wild type enzyme687280
F156VStreptomyces cattleya-25% activity compared to the wild type enzyme687280
S158AStreptomyces cattleya-38% activity compared to the wild type enzyme687280
S158GStreptomyces cattleya-8% activity compared to the wild type enzyme687280
T80AStreptomyces cattleya-15% activity compared to the wild type enzyme687280
T80SStreptomyces cattleya-95% activity compared to the wild type enzyme687280
D16NStreptomyces cattleya NRRL 8057-3% activity compared to the wild type enzyme687280
S158AStreptomyces cattleya NRRL 8057-38% activity compared to the wild type enzyme687280
S158GStreptomyces cattleya NRRL 8057-8% activity compared to the wild type enzyme687280
T80AStreptomyces cattleya NRRL 8057-15% activity compared to the wild type enzyme687280
T80SStreptomyces cattleya NRRL 8057-95% activity compared to the wild type enzyme687280

Renatured/COMMENTARYORGANISM UNIPROT ACCESSION NO.LITERATURE
No entries in this field

APPLICATIONORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
analysisStreptomyces cattleya-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, overview673043
analysisStreptomyces cattleya-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 brain675161
biotechnologyStreptomyces cattleya-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-fluorothreonine703173
biotechnologyStreptomyces cattleya-production of radiolabelled nucleosides as tracers for cancer cell uptake studies via positron emission tomography707137
biotechnologyStreptomyces cattleya-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 enzyme709552
synthesisStreptomyces cattleya-the enzyme is used in biotransformation reaction for production of fluorinated compounds, biotransformation protocols for coupled reaction systems, overview675161
analysisStreptomyces cattleya NRRL 8057-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, overview673043
analysisStreptomyces cattleya NRRL 8057-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 brain675161
biotechnologyStreptomyces cattleya NRRL 8057-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-fluorothreonine703173
biotechnologyStreptomyces cattleya NRRL 8057-production of radiolabelled nucleosides as tracers for cancer cell uptake studies via positron emission tomography707137
synthesisStreptomyces cattleya NRRL 8057-the enzyme is used in biotransformation reaction for production of fluorinated compounds, biotransformation protocols for coupled reaction systems, overview675161

REF. AUTHORS TITLE JOURNAL VOL. PAGES YEAR ORGANISM (UNIPROT ACCESSION NO.)LINK TO PUBMEDSOURCE
637250Schaffrath, C.; Deng, H.; O’Hagan, D.Isolation and characterisation of 5’-fluorodeoxyadenosine synthase, a fluorination enzyme from Streptomyces cattleyaFEBS Lett.547111-1142003Streptomyces cattleya PubMed
637251O’Hagan, D.; Schaffrath, C.; Cobb, L.; Hamilton, J.T.G.; Murphy, C.D.Biosynthesis of an organofluorine moleculeNature4162792002Streptomyces cattleya PubMed
658449Cadicamo, C.D.; Courtieu, J.; Deng, H.; Meddour, A.; O'Hagan, D.Enzymatic fluorination in Streptomyces cattleya takes place with an inversion of configuration consistent with an SN2 reaction mechanismChembiochem5685-6902004Streptomyces cattleya PubMed
660001Dong, C.; Huang, F.; Deng, H.; Schaffrath, C.; Spencer, J.B.; O'Hagan, D.; Naismith, J.H.Crystal structure and mechanism of a bacterial fluorinating enzymeNature427561-5652004Streptomyces cattleya PubMed
673043Deng, H.; Cobb, S.L.; Gee, A.D.; Lockhart, A.; Martarello, L.; McGlinchey, R.P.; OHagan, D.; Onega, M.Fluorinase mediated C-18F bond formation, an enzymatic tool for PET labellingChem. Commun. (Camb.)2006652-6542006Streptomyces cattleya-
675161O'Hagan, D.Recent developments on the fluorinase from Streptomyces cattleyaJ. Fluor. Chem.1271479-14832006Streptomyces cattleya-
676276Cobb, S.L.; Deng, H.; McEwan, A.R.; Naismith, J.H.; OHagan, D.; Robinson, D.A.Substrate specificity in enzymatic fluorination. The fluorinase from Streptomyces cattleya accepts 2-deoxyadenosine substratesOrg. Biomol. Chem.41458-14602006Streptomyces cattleya PubMed
687280Zhu, X.; Robinson, D.A.; McEwan, A.R.; OHagan, D.; Naismith, J.H.Mechanism of enzymatic fluorination in Streptomyces cattleyaJ. Am. Chem. Soc.12914597-146042007Streptomyces cattleya PubMed
703173Deng, H.; Cross, S.M.; McGlinchey, R.P.; Hamilton, J.T.; OHagan, D.In vitro reconstituted biotransformation of 4-fluorothreonine from fluoride ion: application of the fluorinaseChem. Biol.151268-12762008Streptomyces cattleya, Streptomyces cattleya (B6VP39) PubMed
707137Winkler, M.; Domarkas, J.; Schweiger, L.; OHagan, D.Fluorinase-coupled base swaps: Synthesis of 18F-5'-Deoxy-5'-fluorouridinesAngew. Chem. Int. Ed.4710141-101432008Streptomyces cattleya PubMed
709552Iwai, N.; Tanaka, T.; Kitazume, T.Utility of ionic liquid for improvement of fluorination reaction with immobilized fluorinaseJ. Mol. Catal. B59131-1332009Streptomyces cattleya-
710863Deng, H.; Cobb, S.L.; McEwan, A.R.; McGlinchey, R.P.; Naismith, J.H.; O’Hagan, D.; Robinson, D.A.; Spencer, J.B.The fluorinase from Streptomyces cattleya is also a chlorinaseAngew. Chem.45759-7622006Streptomyces cattleya PubMed

LINKS TO OTHER DATABASES (specific for EC-Number 2.5.1.63)
ExplorEnz
ExPASy
KEGG
MetaCyc
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
SYSTERS
Protein Mutant Database
InterPro (database of protein families, domains and functional sites)