Information on EC 2.5.1.63 - adenosyl-fluoride synthase

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The expected taxonomic range for this enzyme is: Streptomyces cattleya

EC NUMBER
COMMENTARY hide
2.5.1.63
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RECOMMENDED NAME
GeneOntology No.
adenosyl-fluoride synthase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + fluoride = 5'-deoxy-5'-fluoroadenosine + L-methionine
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
adenosyl group transfer
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-
-
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halogenation
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-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
fluoroacetate and fluorothreonine biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:fluoride adenosyltransferase
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CAS REGISTRY NUMBER
COMMENTARY hide
438583-16-5
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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UniProt
Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
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first enzyme in the fluorometabolite pathway to produce the mammalian toxin fluoroacetate and the antibiotic 4-fluorothreonine
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2'-deoxyadenosyl-L-methionine + fluoride
2'-deoxy-5'-fluoroadenosine + L-methionine
show the reaction diagram
S-adenosyl-L-methionine + chloride
5'-deoxy-5'-chloroadenosine + L-methionine
show the reaction diagram
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-
-
-
r
S-adenosyl-L-methionine + fluoride
5'-deoxy-5'-fluoroadenosine + L-methionine
show the reaction diagram
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
S-adenosyl-L-methionine + fluoride
5'-deoxy-5'-fluoroadenosine + L-methionine
show the reaction diagram
additional information
?
-
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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
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K+
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in the coupled assay with SAM synthase and fluorinase
Mg2+
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in the coupled assay with SAM synthase and fluorinase
additional information
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Mg2+ at 1 mM does not affect enzyme activity
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
S-adenosyl-L-homocysteine
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competent, competitive
sinefungin
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weak
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
EDTA
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1 mM increases enzyme activity by 25%
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.36 - 36.8
fluoride
0.0008 - 0.42
S-adenosyl-L-methionine
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000012 - 2
fluoride
0.000083 - 0.074
S-adenosyl-L-methionine
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.029
S-adenosyl-homocysteine
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-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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development of a coupled assay with SAM synthase and fluorinase
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.9
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assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
180000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexamer
additional information
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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-sheet
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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 25C 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 replacement
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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 b
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
water stabilizes the enzyme, thus water-absorbing polymer and ionic liquid is used to immobilize the enzyme and keep it surrounded by water
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
nickel-affinity column
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recombinant His-tagged enzyme from Escherichia coli by nickel affinity chromatography and gel filtration
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli BL21; expression in Escherichia coli BL21(DE3)
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expression of His-tagged enzyme in Escherichia coli BL21(DE3) pLysS with plasmid pET28b+
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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 enzyme
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mutant enzymes expressed in Escherichia coli C43 (DE3) cells
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D16A
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inactive
D16N
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3% activity compared to the wild type enzyme
D16S
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inactive
F156A
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3% activity compared to the wild type enzyme
F156V
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25% activity compared to the wild type enzyme
S158A
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38% activity compared to the wild type enzyme
S158G
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8% activity compared to the wild type enzyme
T80A
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15% activity compared to the wild type enzyme
T80S
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95% activity compared to the wild type enzyme
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
biotechnology
synthesis