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Information on EC 1.11.1.23 - (S)-2-hydroxypropylphosphonic acid epoxidase
for references in articles please use BRENDA:EC1.11.1.23
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EC Tree 1 Oxidoreductases
1.11 Acting on a peroxide as acceptor
1.11.1 Peroxidases
1.11.1.23 (S)-2-hydroxypropylphosphonic acid epoxidase
IUBMB Comments
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 .
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Reaction Schemes
showSynonyms
(s)-2-hydroxypropylphosphonic acid epoxidase, hpp epoxidase, ps-hppe, 2-hydroxypropylphosphonic acid epoxidase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
2-hydroxypropylphosphonic acid epoxidase
EC 1.14.19.7
-
-
formerly
-
HPP epoxidase
HppE
HppE
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(S)-2-hydroxypropylphosphonate + H2O2 = (1R,2S)-1,2-epoxypropylphosphonate + 2 H2O
-
-
-
-
(S)-2-hydroxypropylphosphonate + H2O2 = (1R,2S)-1,2-epoxypropylphosphonate + 2 H2O
a straightforward epoxidase mechanism is proposed that depends on the Lewis acid properties of divalent cations and the redox properties of FMN
(S)-2-hydroxypropylphosphonate + H2O2 = (1R,2S)-1,2-epoxypropylphosphonate + 2 H2O
an iron-redox mechanism is proposed in which the active site bound Fe2+ serves as a Lewis acid to activate the 2-OH group of (S)-2-hydroxypropylphosphonic acid, and the epoxide ring is formed by the attack of the 2-OH group at C-1 coupled with the transfer of the C-1 hydrogen as a hydride ion to the bound FMN
(S)-2-hydroxypropylphosphonate + H2O2 = (1R,2S)-1,2-epoxypropylphosphonate + 2 H2O
electron transfer is presumed to be the predominant rate-limiting step. Proposed mechanism: the reaction likely begins with hydrogen atom abstraction from the C-1 position by an activated oxygen species. The C-1 centered radical intermediate can then cyclize to form fosfomycin and the reduced iron center
-
(S)-2-hydroxypropylphosphonate + H2O2 = (1R,2S)-1,2-epoxypropylphosphonate + 2 H2O
Tyr105 is a key residue, which plays a role in the activation of dioxygen required for the enzymatic activity of HppE
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PATHWAY SOURCE
PATHWAYS
MetaCyc
fosfomycin biosynthesis
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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].
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CAS REGISTRY NUMBER
COMMENTARY
261769-38-4
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(1-fluoro-3-oxopropan-2-yl)phosphonate + H2O2
?
Substrates: -
Products: -
Products: -
?
(1-methoxy-3-oxopropan-2-yl)phosphonate + H2O2
?
Substrates: -
Products: -
Products: -
?
(1-oxobutan-2-yl)phosphonate + H2O2
?
Substrates: -
Products: -
Products: -
?
(1-oxopropan-2-yl)phosphonate + H2O2
?
Substrates: -
Products: -
Products: -
?
(2-methyl-1-oxopropan-2-yl)phosphonate + H2O2
?
Substrates: -
Products: -
Products: -
?
(2-methylpropanoyl)phosphonate + H2O2
?
Substrates: -
Products: -
Products: -
?
(3,3,3-trifluoro-1-hydroxypropyl)phosphonic acid + H2O2
?
Substrates: -
Products: -
Products: -
?
(3-cyclopropyloxiran-2-yl)phosphonate + H2O2
?
Substrates: -
Products: -
Products: -
?
(R)-2-hydroxypropylphosphonate + H2O2
2-oxo-propylphosphonic acid + H2O
-
Substrates: -
Products: -
Products: -
?
(R)-2-hydroxypropylphosphonate + H2O2
2-oxopropylphosphonic acid + H2O
Substrates: -
Products: -
Products: -
?
(R)-2-hydroxypropylphosphonate + H2O2
?
Substrates: -
Products: -
Products: -
?
(R)-2-hydroxypropylphosphonate + NADH + H+ + O2
2-oxopropylphosphonic acid + NAD+ + H2O
-
Substrates: -
Products: -
Products: -
?
(R)-2-hydroxypropylphosphonic acid + H2O2
2-oxo-propylphosphonic acid + H2O
Substrates: -
Products: -
Products: -
?
(S)-2-hydroxybutylphosphonic acid + 2 NADH + O2
cis-(1R,2S)-epoxybutylphosphonic acid + 2 H2O + 2 NAD+
Substrates: -
Products: -
Products: -
?
(S)-2-hydroxypropyl-1-phosphonate + H2O2
(1R,2S)-1,2-epoxypropylphosphonate + H2O
-
Substrates: -
Products: i.e. fosfomycin
Products: i.e. fosfomycin
?
(S)-2-hydroxypropylphosphonate + H2O2
cis-fosfomycin + trans-fosfomycin + 2 H2O
Substrates: -
Products: -
Products: -
?
(S)-2-hydroxypropylphosphonate + NADH + H+ + O2
(1R,2S)-epoxypropylphosphonate + NAD+ + H2O
-
Substrates: -
Products: i.e. fosfomycin
Products: i.e. fosfomycin
?
(S)-2-hydroxypropylphosphonic acid + 2 NADH + O2
cis-(1R,2S)-epoxypropylphosphonic acid + 2 H2O + 2 NAD+
[(1R)-1-hydroxy-2-methylpropyl]phosphonate + H2O2
?
Substrates: -
Products: -
Products: -
?
[(1R)-1-hydroxy-3-methoxypropyl]phosphonate + H2O2
?
Substrates: -
Products: -
Products: -
?
[(1R)-1-hydroxybutyl]phosphonate + H2O2
?
Substrates: -
Products: -
Products: -
?
[(1R)-1-hydroxyethyl]phosphonate + H2O2
?
Substrates: -
Products: -
Products: -
?
[(1R)-3,3,3-trifluoro-1-hydroxypropyl]phosphonate + H2O2
?
Substrates: -
Products: -
Products: -
?
[(1R)-3-fluoro-1-hydroxypropyl]phosphonate + H2O2
?
Substrates: -
Products: -
Products: -
?
[(1S)-1-hydroxy-2-methylpropyl]phosphonate + H2O2
?
Substrates: -
Products: -
Products: -
?
[(2R)-2-hydroxy-2-[(1R)-2-methylidenecyclopropyl]ethyl]phosphonate + H2O2
?
-
Substrates: -
Products: -
Products: -
?
[(2R)-2-hydroxy-2-[(1S)-2-methylidenecyclopropyl]ethyl]phosphonate + H2O2
?
-
Substrates: -
Products: -
Products: -
?
[(2R)-3-cyclopropyloxiran-2-yl]phosphonate + H2O2
?
-
Substrates: -
Products: -
Products: -
?
[(2R,3S)-3-[(1R)-2-methylidenecyclopropyl]oxiran-2-yl]phosphonate + H2O2
?
-
Substrates: -
Products: -
Products: -
?
[(2R,3S)-3-[(1S)-2-methylidenecyclopropyl]oxiran-2-yl]phosphonate + H2O2
?
-
Substrates: -
Products: -
Products: -
?
[(2S)-2-hydroxy-2-(2-methylidenecyclopropyl)ethyl]phosphonate + H2O2
?
Substrates: -
Products: -
Products: -
?
[(2S)-2-hydroxy-2-[(1R)-2-methylidenecyclopropyl]ethyl]phosphonic acid + H2O2
?
-
Substrates: -
Products: -
Products: -
?
[2-[(1S)-2-methylidenecyclopropyl]-2-oxoethyl]phosphonate + H2O2
?
-
Substrates: -
Products: -
Products: -
?
[3-(2-methylidenecyclopropyl)oxiran-2-yl]phosphonate + H2O2
?
Substrates: -
Products: -
Products: -
?
(2-cyclopropyl-2-oxoethyl)phosphonate + H2O2
?
-
Substrates: -
Products: -
Products: -
?
(2-cyclopropyl-2-oxoethyl)phosphonate + H2O2
?
Substrates: -
Products: -
Products: -
?
(S)-2-hydroxypropylphosphonate + H2O2
(1R,2S)-1,2-epoxypropylphosphonate + H2O
-
Substrates: -
Products: -
Products: -
?
(S)-2-hydroxypropylphosphonate + H2O2
(1R,2S)-1,2-epoxypropylphosphonate + H2O
Substrates: -
Products: -
Products: -
?
(S)-2-hydroxypropylphosphonic acid + 2 NADH + O2
cis-(1R,2S)-epoxypropylphosphonic acid + 2 H2O + 2 NAD+
-
Substrates: -
Products: i.e. fosfomycin
Products: i.e. fosfomycin
?
(S)-2-hydroxypropylphosphonic acid + 2 NADH + O2
cis-(1R,2S)-epoxypropylphosphonic acid + 2 H2O + 2 NAD+
-
Substrates: if either iron, FMN, or NADH is omitted from the reaction mixture, no product formation is detected
Products: i.e. fosfomycin
Products: i.e. fosfomycin
?
(S)-2-hydroxypropylphosphonic acid + 2 NADH + O2
cis-(1R,2S)-epoxypropylphosphonic acid + 2 H2O + 2 NAD+
Substrates: -
Products: i.e. fosfomycin
Products: i.e. fosfomycin
?
(S)-2-hydroxypropylphosphonic acid + 2 NADH + O2
cis-(1R,2S)-epoxypropylphosphonic acid + 2 H2O + 2 NAD+
Substrates: -
Products: i.e. fosfomycin
Products: i.e. fosfomycin
?
(S)-2-hydroxypropylphosphonic acid + 2 NADH + O2
cis-(1R,2S)-epoxypropylphosphonic acid + 2 H2O + 2 NAD+
-
Substrates: -
Products: i.e. fosfomycin
Products: i.e. fosfomycin
?
(S)-2-hydroxypropylphosphonic acid + 2 NADH + O2
cis-(1R,2S)-epoxypropylphosphonic acid + 2 H2O + 2 NAD+
Substrates: -
Products: i.e. fosfomycin
Products: i.e. fosfomycin
?
(S)-2-hydroxypropylphosphonic acid + 2 NADH + O2
cis-(1R,2S)-epoxypropylphosphonic acid + 2 H2O + 2 NAD+
Substrates: bidentate mode of substrate binding to the active site iron in the solution state is established. The binding of the hydroxyl group of the substrates determines the site of oxidation. Use of (R)-2-hydroxypropylphosphonic acid yields the 2-keto-adduct rather than the epoxide
Products: i.e. fosfomycin
Products: i.e. fosfomycin
?
[(2R)-2-cyclopropyl-2-hydroxyethyl]phosphonate + H2O2
?
-
Substrates: -
Products: -
Products: -
?
[(2R)-2-cyclopropyl-2-hydroxyethyl]phosphonate + H2O2
?
Substrates: -
Products: -
Products: -
?
[(2S)-2-cyclopropyl-2-hydroxyethyl]phosphonate + H2O2
?
-
Substrates: -
Products: -
Products: -
?
[(2S)-2-cyclopropyl-2-hydroxyethyl]phosphonate + H2O2
?
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme also forms 2-oxopropylphosphonic acid from (R)-2-hydroxypropylphosphonic acid, the rate of this reaction is 1.9times faster than the reaction with (S)-2-hydroxypropylphosphonic acid
Products: -
Products: -
?
additional information
?
-
Substrates: no activity with 2-hydroxyethyl phosphonic acid
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme also forms 2-oxopropylphosphonic acid from (R)-2-hydroxypropylphosphonic acid. HPP epoxidase is not selective with regard to substrate recognition, but can stereospecifically convert each enantiomer into a unique product with similar efficiency
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(R)-2-hydroxypropylphosphonate + H2O2
2-oxo-propylphosphonic acid + H2O
-
Substrates: -
Products: -
Products: -
?
(R)-2-hydroxypropylphosphonate + H2O2
2-oxopropylphosphonic acid + H2O
Substrates: -
Products: -
Products: -
?
(R)-2-hydroxypropylphosphonate + NADH + H+ + O2
2-oxopropylphosphonic acid + NAD+ + H2O
-
Substrates: -
Products: -
Products: -
?
(R)-2-hydroxypropylphosphonic acid + H2O2
2-oxo-propylphosphonic acid + H2O
Substrates: -
Products: -
Products: -
?
(S)-2-hydroxypropyl-1-phosphonate + H2O2
(1R,2S)-1,2-epoxypropylphosphonate + H2O
-
Substrates: -
Products: i.e. fosfomycin
Products: i.e. fosfomycin
?
(S)-2-hydroxypropylphosphonate + H2O2
cis-fosfomycin + trans-fosfomycin + 2 H2O
Substrates: -
Products: -
Products: -
?
(S)-2-hydroxypropylphosphonate + NADH + H+ + O2
(1R,2S)-epoxypropylphosphonate + NAD+ + H2O
-
Substrates: -
Products: i.e. fosfomycin
Products: i.e. fosfomycin
?
(S)-2-hydroxypropylphosphonic acid + 2 NADH + O2
cis-(1R,2S)-epoxypropylphosphonic acid + 2 H2O + 2 NAD+
(S)-2-hydroxypropylphosphonate + H2O2
(1R,2S)-1,2-epoxypropylphosphonate + H2O
-
Substrates: -
Products: -
Products: -
?
(S)-2-hydroxypropylphosphonate + H2O2
(1R,2S)-1,2-epoxypropylphosphonate + H2O
Substrates: -
Products: -
Products: -
?
(S)-2-hydroxypropylphosphonic acid + 2 NADH + O2
cis-(1R,2S)-epoxypropylphosphonic acid + 2 H2O + 2 NAD+
-
Substrates: -
Products: i.e. fosfomycin
Products: i.e. fosfomycin
?
(S)-2-hydroxypropylphosphonic acid + 2 NADH + O2
cis-(1R,2S)-epoxypropylphosphonic acid + 2 H2O + 2 NAD+
Substrates: -
Products: i.e. fosfomycin
Products: i.e. fosfomycin
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FAD
FMN and FAD greatly enhance production of fosfomycin. The flavin coenzyme is unlikely an integral part of the epoxidase
FAD
FMN or FAD increase level of fosfomycin production. The effect of FMN is slightly better than that of FAD. The flavin coenzyme is not likely to be an integral part of the epoxidase itself, but it may serve as a surrogate for the putative electron mediator in the in vitro assay
FMN
a straightforward epoxidase mechanism is proposed that depends on the Lewis acid properties of divalent cations and the redox properties of FMN
FMN
FMN and FAD greatly enhance production of fosfomycin. The flavin coenzyme is unlikely an integral part of the epoxidase
FMN
FMN is an artificial electron mediator for the in vitro HppE activity. It accepts a hydride from NADH and then passes electrons on to reduce the iron center of HppE. Several non-flavin electron mediators can replace FMN
FMN
FMN or FAD increase level of fosfomycin production. The effect of FMN is slightly better than that of FAD. The flavin coenzyme is not likely to be an integral part of the epoxidase itself, but it may serve as a surrogate for the putative electron mediator in the in vitro assay
FMN
-
if either iron, FMN, or NADH is omitted from the reaction mixture, no product formation is detected. Due to the fact that the reduction of iron requires single electron transfer and NADH is an obligate two-electron donor, FMN is required to mediate the transfer of reducing equivalents from NADH to the active site iron
NADH
NADH is a necessary component for (S)-2-hydroxypropylphosphonic acid epoxidation and the overall catalysis is a four-electron redox reaction
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
Iron
Zn2+
the recombinant enzyme is active, when reconstituted with Zn2+ or Fe2+
Fe2+
Fe2+ is the only metal ion that is effective to reconstitute HppE activity. Zn2+ cannot replace Fe2+ in the HppE reaction
Fe2+
the recombinant enzyme is active, when reconstituted with Zn2+ or Fe2+
Iron
-
mononuclear non-heme iron-containing enzyme. Contains about one iron per monomer. Substrate and NO can bind to the ferrous center of the reduced HppE enzyme to form a stable complex
Iron
mononuclear non-heme iron enzyme. Substrate binds near, and perhaps to, the active site Fe2+ and in doing so organizes the center so that effectively one species is present
Iron
O2 binds to the iron, and substrates bind in a single orientation that strongly perturbs the iron environment. Both functional groups of (S)-2-hydroxypropylphosphonic acid bind to Fe(II) ion at the same time as NO, suggesting that the chelated substrate binding mode dominates in solution. The Fe(II)-substrate chelate structure is important to active fosfomycin formation. This fixed orientation may align the substrate next to the iron-bound activated oxygen species thought to mediate hydrogen atom abstraction from the nearest substrate carbon
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
[(2R)-2-hydroxy-2-(2-methylidenecyclopropyl)ethyl]phosphonate
-
[(2R)-2-hydroxy-2-[(1S)-2-methylidenecyclopropyl]ethyl]phosphonate
-
highly effective inhibitor
[(2S)-1,1-difluoro-2-hydroxypropyl]phosphonic acid
tight binding inhibitor
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). A0A5J4PX85_9ZZZZ
191
0
21368
TrEMBL
other Location (Reliability: 2)
A0A5J4R943_9ZZZZ
191
0
21198
TrEMBL
other Location (Reliability: 1)
A0A1Q2HMK7_9BACT
191
0
21271
TrEMBL
-
A0A5J4SD61_9ZZZZ
191
0
21690
TrEMBL
other Location (Reliability: 1)
A0A644T769_9ZZZZ
191
0
21312
TrEMBL
other Location (Reliability: 1)
A0A5J4RED8_9ZZZZ
175
0
19541
TrEMBL
other Location (Reliability: 2)
A0A1V6JAY2_9BACT
191
0
21138
TrEMBL
-
A0A1V5IWV6_9BACT
191
0
21239
TrEMBL
-
A0A5J4P9N5_9ZZZZ
118
0
13336
TrEMBL
other Location (Reliability: 3)
A0A1V6EGH0_9FIRM
194
0
22343
TrEMBL
-
A0A1V5YZ90_9BACT
191
0
20770
TrEMBL
-
A0A5J4R108_9ZZZZ
191
0
21339
TrEMBL
other Location (Reliability: 1)
A0A5J4RTE7_9ZZZZ
191
0
21427
TrEMBL
other Location (Reliability: 1)
A0A166DI89_9EURY
191
0
21261
TrEMBL
-
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
21000
21400
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
tetramer
trimer
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
side-chain modification
side-chain modification
-
posttranslationally modified by the hydroxylation of Tyr95
side-chain modification
DOPA formation, probably at Tyr105, is a self-hydroxylation reaction
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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
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
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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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
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
F182A
the variant favors trans-fosfomycin production from (S)-2-hydroxypropylphosphonate
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
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
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
medicine
-
fosfomycin is a clinically useful antibiotic for the treatment of limb-threatening diabetic foot infections and lower urinary tract infections. It is effective against ciprofloxacin-resistant Escherichia coli, as well as methicillin-resistant and vancomycin-resistant strains of Staphylococcus aureus. The antimicrobial activity of fosfomycin is due to the inactivation of UDP-GlcNAc-3-O-enolpyruvyltransferase, which catalyzes the first committed step in the biosynthesis of peptidoglycan, the main component of the bacterial cell wall
medicine
fosfomycin is a clinically utilized antibiotic of low toxicity, blocking bacterial cell wall biosynthesis by acting as an analogue of phosphoenolpyruvate
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Cameron, S.; McLuskey, K.; Chamberlayne, R.; Hallyburton, I.; Hunter, W.N.
Initiating a crystallographic analysis of recombinant (S)-2-hydroxypropylphosphonic acid epoxidase from Streptomyces wedmorensis
Acta Crystallogr. Sect. F
61
534-536
2005
Streptomyces wedmorensis (Q56185), Streptomyces wedmorensis
brenda
Zhao, Z.; Liu, P.; Murakami, K.; Kuzuyama, T.; Seto, H.; Liu, H.W.
Mechanistic studies of HPP epoxidase: configuration of the substrate governs its enzymatic fate
Angew. Chem. Int. Ed. Engl.
41
4529-4532
2002
Streptomyces wedmorensis (Q56185)
brenda
Watanabe, M.; Sumida, N.; Murakami, S.; Anzai, H.; Thompson, C.J.; Tateno, Y.; Murakami, T.
A phosphonate-induced gene which promotes Penicillium-mediated bioconversion of cis-propenylphosphonic acid to fosfomycin
Appl. Environ. Microbiol.
65
1036-1044
1999
Penicillium decumbens
brenda
Yan, F.; Li, T.; Lipscomb, J.D.; Liu, A.; Liu, H.W.
Site-directed mutagenesis and spectroscopic studies of the iron-binding site of (S)-2-hydroxypropylphosphonic acid epoxidase
Arch. Biochem. Biophys.
442
82-91
2005
Streptomyces wedmorensis (Q56185), Streptomyces wedmorensis
brenda
Liu, P.; Liu, A.; Yan, F.; Wolfe, M.D.; Lipscomb, J.D.; Liu, H.W.
Biochemical and spectroscopic studies on (S)-2-hydroxypropylphosphonic acid epoxidase: a novel mononuclear non-heme iron enzyme
Biochemistry
42
11577-11586
2003
Streptomyces wedmorensis (Q56185)
brenda
Yan, F.; Munos, J.W.; Liu, P.; Liu, H.W.
Biosynthesis of fosfomycin, re-examination and re-confirmation of a unique Fe(II)- and NAD(P)H-dependent epoxidation reaction
Biochemistry
45
11473-11481
2006
Streptomyces wedmorensis (Q56185)
brenda
Yan, F.; Moon, S.J.; Liu, P.; Zhao, Z.; Lipscomb, J.D.; Liu, A.; Liu, H.W.
Determination of the substrate binding mode to the active site iron of (S)-2-hydroxypropylphosphonic acid epoxidase using 17O-enriched substrates and substrate analogues
Biochemistry
46
12628-12638
2007
Streptomyces wedmorensis (Q56185)
brenda
Munos, J.W.; Moon, S.J.; Mansoorabadi, S.O.; Chang, W.; Hong, L.; Yan, F.; Liu, A.; Liu, H.W.
Purification and characterization of the epoxidase catalyzing the formation of fosfomycin from Pseudomonas syringae
Biochemistry
47
8726-8735
2008
Pseudomonas syringae
brenda
Schweifer, A.; Hammerschmidt, F.
On the conversion of structural analogues of (S)-2-hydroxypropylphosphonic acid to epoxides by the final enzyme of fosfomycin biosynthesis in S. fradiae
Bioorg. Med. Chem. Lett.
18
3056-3059
2008
Streptomyces fradiae (D2SNF6)
brenda
Kuzuyama, T.; Seki, T.; Kobayashi, S.; Hidaka, T.; Seto, H.
Cloning and expression in Escherichia coli of 2-hydroxypropylphosphonic acid epoxidase from the fosfomycin-producing organism, Pseudomonas syringae PB-5123
Biosci. Biotechnol. Biochem.
63
2222-2224
1999
Pseudomonas syringae (Q9JN69), Pseudomonas syringae PB-5123 (Q9JN69), Pseudomonas syringae PB-5123
brenda
Liu, P.; Murakami, K.; Seki, T.; He, X.; Yeung, S.M.; Kuzuyama, T.; Seto, H.; Liu, H.
Protein purification and function