Information on EC 1.13.11.78 - 2-amino-1-hydroxyethylphosphonate dioxygenase (glycine-forming)

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.13.11.78
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RECOMMENDED NAME
GeneOntology No.
2-amino-1-hydroxyethylphosphonate dioxygenase (glycine-forming)
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(2-amino-1-hydroxyethyl)phosphonate + O2 = glycine + phosphate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
O-O heterolytic cleavage
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mechanism, detailed overview
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
2-aminoethylphosphonate degradation III
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Phosphonate and phosphinate metabolism
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SYSTEMATIC NAME
IUBMB Comments
2-amino-1-hydroxyethylphosphonate:oxygen 1-oxidoreductase (glycine-forming)
Requires Fe2+. The enzyme, characterized from a marine bacterium, is involved in a 2-aminoethylphosphonate degradation pathway.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
metabolism
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combined with PhnY, which is a nonheme mononuclear 2-oxoglutarate-dependent dioxygenase to effect typical hydroxylation transformation of 2-amino-ethylphosphonic acid (2-AEP) to (R)-OH-AEP, the PhnY-PhnZ relay pathway affords aquatic and marine bacteria in Pi limited environments to utilize 2-AEP, the most abundant environmental 2-AEP, as the source of phosphate
physiological function
additional information
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enzyme PhnZ has an active site containing two Fe ions coordinated by four histidines and two aspartates that is strikingly similar to the carbon-carbon bond cleaving enzyme, myo-inositol-oxygenase. The exception is residue Y24, which forms a transient ligand interaction at the dioxygen binding site of the second Fe2+. Structure comparisons and substrate binding structures, active site structure, detailed overview
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(+/-)-(2-amino-1-hydroxyethyl)phosphonate + O2
?
show the reaction diagram
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50% conversion
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-
?
(2-amino-1-hydroxyethyl)phosphonate + O2
glycine + phosphate
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
(2-amino-1-hydroxyethyl)phosphonate + O2
glycine + phosphate
show the reaction diagram
additional information
?
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D0E8I5
the enzyme uses a di-iron oxygenase mechanism for catabolism of organophosphonates, overview
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
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partial activation compared to Fe2+
Co2+
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partial activation compared to Fe2+
Cu2+
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partial activation compared to Fe2+
Fe3+
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partial activation compared to Fe2+
Iron
the enzyme contains 1.2 Fe per monomer, contains a dinuclear iron cluster. The mixed-valent FeII/FeIII state is the catalytically active cofactor form
Mn2+
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partial activation compared to Fe2+
Ni2+
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partial activation compared to Fe2+
Zn2+
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partial activation compared to Fe2+
additional information
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not influenced by Mg2+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.017 - 1.1
(2-amino-1-hydroxyethyl)phosphonate
additional information
additional information
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kinetic analysis with substrate analogues, Michaelis-Menten kinetics
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2 - 11
(2-amino-1-hydroxyethyl)phosphonate
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.72 - 423.1
(2-amino-1-hydroxyethyl)phosphonate
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purified enzyme in complex with substrate (R)-2-amino-1-hydroxyethylphosphonate or with L-tartrate, derived from the crystallization buffer, hanging drop vapour diffusion method, mixing 0.005 ml of 16 mg/ml selenomethionine-labeled protein of enzyme in complex with L-tartrate in a solution containing 5% n-octyl-beta-D-glucoside with 0.005 ml of reservoir solution containing 2.4 M ammonium sulfate and 0.15 M potassium sodium L-tartrate, 5-7 days at room temperature, the substrate-complexed enzyme is crystallized by sitting drop vapour diffusion method by mixing of 0.001 ml of protein solution with 0.001 ml of reservoir solution containing 0.1 M Bis-Tris, pH 6.5 and 20% w/v PEG 5000 monomethyl ether, X-ray diffraction structure determination and analysis at 2.1 and 1.7 A resolution, respectively, molecular replacement and modeling
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Ni2+-affinity chromatography
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
gene phnZ, DNA and amino acid sequence determination and analysis, sequence comparisons, recombinant expression of wild-type and mutant C-terminally His-tagged enzymes in Escherichia coli strain DL41(DE3)
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D161A
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site-directed mutagenesis, the mutant is inactive
D59A
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site-directed mutagenesis, the mutant is unstable
H104A
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site-directed mutagenesis, the mutant is inactive
H34A
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site-directed mutagenesis, the mutant is inactive
H58A
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site-directed mutagenesis, the mutant is inactive
H80A
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site-directed mutagenesis, the mutant shows 10fold reduced activity compared to the wild-type enzyme, reduced Fe-enzyme molar ratios exist in the variants H80A