Information on EC 1.11.1.23 - (S)-2-hydroxypropylphosphonic acid epoxidase

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

EC NUMBER
COMMENTARY hide
1.11.1.23
-
RECOMMENDED NAME
GeneOntology No.
(S)-2-hydroxypropylphosphonic acid epoxidase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(S)-2-hydroxypropylphosphonate + H2O2 = (1R,2S)-1,2-epoxypropylphosphonate + 2 H2O
show the reaction diagram
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
fosfomycin biosynthesis
-
-
Phosphonate and phosphinate metabolism
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Biosynthesis of antibiotics
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SYSTEMATIC NAME
IUBMB Comments
(S)-2-hydroxypropylphosphonate:hydrogen peroxide epoxidase
This is the last enzyme in the biosynthetic pathway of fosfomycin, a broad-spectrum antibiotic produced by certain Streptomyces species. Contains non heme iron that forms a iron(IV)-oxo (ferryl) complex with hydrogen peroxide, which functions as a proton abstractor from the substrate [7].
CAS REGISTRY NUMBER
COMMENTARY hide
261769-38-4
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(1-fluoro-3-oxopropan-2-yl)phosphonate + H2O2
?
show the reaction diagram
-
-
-
-
?
(1-methoxy-3-oxopropan-2-yl)phosphonate + H2O2
?
show the reaction diagram
-
-
-
-
?
(1-oxobutan-2-yl)phosphonate + H2O2
?
show the reaction diagram
-
-
-
-
?
(1-oxopropan-2-yl)phosphonate + H2O2
?
show the reaction diagram
-
-
-
-
?
(2-cyclopropyl-2-oxoethyl)phosphonate + H2O2
?
show the reaction diagram
-
-
-
-
?
(2-methyl-1-oxopropan-2-yl)phosphonate + H2O2
?
show the reaction diagram
-
-
-
-
?
(2-methylpropanoyl)phosphonate + H2O2
?
show the reaction diagram
-
-
-
-
?
(2-oxoethyl)phosphonate + H2O2
?
show the reaction diagram
-
-
-
-
?
(3,3,3-trifluoropropanoyl)phosphonate + H2O2
?
show the reaction diagram
-
-
-
-
?
(3-cyclopropyloxiran-2-yl)phosphonate + H2O2
?
show the reaction diagram
-
-
-
-
?
(R)-2-hydroxypropylphosphonate + H2O2
2-oxo-propylphosphonic acid + H2O
show the reaction diagram
-
-
-
-
?
(R)-2-hydroxypropylphosphonate + H2O2
2-oxopropylphosphonic acid + H2O
show the reaction diagram
-
-
-
-
?
(R)-2-hydroxypropylphosphonate + H2O2
?
show the reaction diagram
-
-
-
-
?
(R)-2-hydroxypropylphosphonic acid + H2O2
2-oxo-propylphosphonic acid + H2O
show the reaction diagram
-
-
-
-
?
(S)-2-hydroxybutylphosphonic acid + 2 NADH + O2
cis-(1R,2S)-epoxybutylphosphonic acid + 2 H2O + 2 NAD+
show the reaction diagram
-
-
-
?
(S)-2-hydroxypropyl-1-phosphonate + H2O2
(1R,2S)-1,2-epoxypropylphosphonate + H2O
show the reaction diagram
-
-
i.e. fosfomycin
-
?
(S)-2-hydroxypropylphosphonate + H2O2
(1R,2S)-1,2-epoxypropylphosphonate + H2O
show the reaction diagram
-
-
-
-
?
(S)-2-hydroxypropylphosphonic acid + 2 NADH + O2
cis-(1R,2S)-epoxypropylphosphonic acid + 2 H2O + 2 NAD+
show the reaction diagram
[(1R)-1-hydroxy-2-methylpropyl]phosphonate + H2O2
?
show the reaction diagram
-
-
-
-
?
[(1R)-1-hydroxy-3-methoxypropyl]phosphonate + H2O2
?
show the reaction diagram
-
-
-
-
?
[(1R)-1-hydroxybutyl]phosphonate + H2O2
?
show the reaction diagram
-
-
-
-
?
[(1R)-1-hydroxyethyl]phosphonate + H2O2
?
show the reaction diagram
-
-
-
-
?
[(1R)-3,3,3-trifluoro-1-hydroxypropyl]phosphonate + H2O2
?
show the reaction diagram
-
-
-
-
?
[(1R)-3-fluoro-1-hydroxypropyl]phosphonate + H2O2
?
show the reaction diagram
-
-
-
-
?
[(1S)-1-hydroxy-2-methylpropyl]phosphonate + H2O2
?
show the reaction diagram
-
-
-
-
?
[(2R)-2-cyclopropyl-2-hydroxyethyl]phosphonate + H2O2
?
show the reaction diagram
-
-
-
-
?
[(2R)-2-hydroxy-2-[(1R)-2-methylidenecyclopropyl]ethyl]phosphonate + H2O2
?
show the reaction diagram
-
-
-
-
?
[(2R)-2-hydroxy-2-[(1S)-2-methylidenecyclopropyl]ethyl]phosphonate + H2O2
?
show the reaction diagram
-
-
-
-
?
[(2R)-3-cyclopropyloxiran-2-yl]phosphonate + H2O2
?
show the reaction diagram
-
-
-
-
?
[(2R,3S)-3-[(1R)-2-methylidenecyclopropyl]oxiran-2-yl]phosphonate + H2O2
?
show the reaction diagram
-
-
-
-
?
[(2R,3S)-3-[(1S)-2-methylidenecyclopropyl]oxiran-2-yl]phosphonate + H2O2
?
show the reaction diagram
-
-
-
-
?
[(2S)-2-cyclopropyl-2-hydroxyethyl]phosphonate + H2O2
?
show the reaction diagram
-
-
-
-
?
[(2S)-2-hydroxy-2-(2-methylidenecyclopropyl)ethyl]phosphonate + H2O2
?
show the reaction diagram
-
-
-
-
?
[(2S)-2-hydroxy-2-[(1R)-2-methylidenecyclopropyl]ethyl]phosphonic acid + H2O2
?
show the reaction diagram
-
-
-
-
?
[2-[(1S)-2-methylidenecyclopropyl]-2-oxoethyl]phosphonate + H2O2
?
show the reaction diagram
-
-
-
-
?
[3-(2-methylidenecyclopropyl)oxiran-2-yl]phosphonate + H2O2
?
show the reaction diagram
-
-
-
-
?
additional information
?
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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
(R)-2-hydroxypropylphosphonate + H2O2
2-oxo-propylphosphonic acid + H2O
show the reaction diagram
-
-
-
-
?
(R)-2-hydroxypropylphosphonate + H2O2
2-oxopropylphosphonic acid + H2O
show the reaction diagram
-
-
-
-
?
(R)-2-hydroxypropylphosphonic acid + H2O2
2-oxo-propylphosphonic acid + H2O
show the reaction diagram
-
-
-
-
?
(S)-2-hydroxypropyl-1-phosphonate + H2O2
(1R,2S)-1,2-epoxypropylphosphonate + H2O
show the reaction diagram
-
-
i.e. fosfomycin
-
?
(S)-2-hydroxypropylphosphonate + H2O2
(1R,2S)-1,2-epoxypropylphosphonate + H2O
show the reaction diagram
-
-
-
-
?
(S)-2-hydroxypropylphosphonic acid + 2 NADH + O2
cis-(1R,2S)-epoxypropylphosphonic acid + 2 H2O + 2 NAD+
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Zn2+
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the recombinant enzyme is active, when reconstituted with Zn2+ or Fe2+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
[(2R)-2-hydroxy-2-(2-methylidenecyclopropyl)ethyl]phosphonate
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[(2R)-2-hydroxy-2-[(1S)-2-methylidenecyclopropyl]ethyl]phosphonate
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highly effective inhibitor
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[(2S)-1,1-difluoro-2-hydroxypropyl]phosphonic acid
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tight binding inhibitor
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0028
(S)-2-hydroxypropylphosphonic acid
Pseudomonas syringae
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pH 7.5
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
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assay at
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
68000
gel filtration
73000
-
gel filtration
89000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homotetramer
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4 * 21400, crystalligraphic data
tetramer
trimer
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3 * 21000, SDS-PAGE; 3 * 21315, calculated from sequence
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
side-chain modification
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystal structures of holoenzyme and the complex with fosfomycin are determined and reveal a two-domain combination and Zn2+ in the active site
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hanging drop vapour diffusion method, six X-ray structures of this enzyme: the apoenzyme at 2.0 A resolution, a native Fe2+-bound form at 2.4 A resolution; a tris(hydroxymethyl)aminomethane-Co2+-enzyme complex structure at 1.8 A resolution, a substrate-Co2+-enzyme complex structure at 2.5 A resolution; and two substrate-Fe2+-enzyme complexes at 2.1 and 2.3 A resolution
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vapour diffusion method. The hexagonal form displays symmetry consistent with space group P6(1/5)22 and unit-cell parameters a = 86.44, c = 221.56 A, gamma = 120°
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichi coli
expression in Escherichia coli
expression in Escherichia coli BL21(DE3)
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E142A
-
complete loss of enzymatic activity in vivo and in vitro, 2.1% of the active site iron as compared to wild-type enzyme, no self-hydroxylation at Tyr105
H138A
-
inactive in vivo, but in vitro it retains 27% of the active site iron and nearly 20% of the wild-type activity, limited self-hydroxylation (at Tyr105)
H180A
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complete loss of enzymatic activity in vivo and in vitro, 5.8% of the active site iron as compared to wild-type enzyme, no self-hydroxylation at Tyr105
Y102F
-
mutant maintains 60% of the activity of the wild-type enzyme
Y103F
-
mutant maintains 60% of the activity of the wild-type enzyme
Y105F
-
mutant enzyme is inactive
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine