Information on EC 1.14.14.33 - ethylenediaminetetraacetate monooxygenase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.14.14.33
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RECOMMENDED NAME
GeneOntology No.
ethylenediaminetetraacetate monooxygenase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ethylenediaminetetraacetate + 2 FMNH2 + 2 O2 = ethylenediamine-N,N'-diacetate + 2 glyoxylate + 2 FMN + 2 H2O
show the reaction diagram
overall reaction
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ethylenediaminetetraacetate + FMNH2 + O2 = ethylenediaminetriacetate + glyoxylate + FMN + H2O
show the reaction diagram
(1a)
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ethylenediaminetriacetate + FMNH2 + O2 = ethylenediamine-N,N'-diacetate + glyoxylate + FMN + H2O
show the reaction diagram
(1b)
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SYSTEMATIC NAME
IUBMB Comments
ethylenediaminetetraacetate,FMNH2:O2 oxidoreductase (glyoxylate-forming)
The enzyme is part of a two component system that also includes EC 1.5.1.42, FMN reductase (NADH), which provides reduced flavin mononucleotide for this enzyme. It acts on EDTA only when it is complexed with divalent cations such as Mg2+, Zn2+, Mn2+, Co2+, or Cu2+. While the enzyme has a substrate overlap with EC 1.14.14.10, nitrilotriacetate monooxygenase, it has a much wider substrate range, which includes nitrilotriacetate (NTA) and diethylenetriaminepentaacetate (DTPA) in addition to EDTA.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
diethylenetriaminepentaacetate + FMNH2 + O2
diethylenetriaminetetraacetate + glyoxylate + FMN + H2O
show the reaction diagram
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-
-
?
ethylenediaminetetraacetate + 2 FADH2 + 2 O2
ethylenediamine-N,N'-diacetate + 2 glyoxylate + 2 FAD + 2 H2O
show the reaction diagram
ethylenediaminetetraacetate + 2 FMNH2 + 2 O2
ethylenediamine-N,N'-diacetate + 2 glyoxylate + 2 FMN + 2 H2O
show the reaction diagram
ethylenediaminetetraacetate + FMNH2 + O2
ethylenediaminetriacetate + glyoxylate + FMN + H2O
show the reaction diagram
ethylenediaminetriacetate + FMNH2 + O2
ethylenediamine-N,N'-diacetate + glyoxylate + FMN + H2O
show the reaction diagram
nitrilotriacetate + FMNH2 + O2
nitrilodiacetate + glyoxylate + FMN + H2O
show the reaction diagram
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?
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
ethylenediaminetetraacetate + 2 FMNH2 + 2 O2
ethylenediamine-N,N'-diacetate + 2 glyoxylate + 2 FMN + 2 H2O
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
FMNH2
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
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MgEDTA2- is the best substrate
additional information
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the enzyme is able to release glyoxylate from EDTA complexed with any of the cations tested (Mg2+, Mn2+, Ni2+, Co2+, Zn2+, Fe2+, Ca2+, Cu2+, Cr2+, Sn2+, Ba2+, Cd2+, Sr2+, Pd2+, Al3+, Cr3+, K+, or Na+). MgEDTA2- is the best substrate
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0085 - 0.521
ethylenediaminetetraacetate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.8 - 47.1
ethylenediaminetetraacetate
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
20 - 430
ethylenediaminetetraacetate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1.6
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pH 8.0, 30°C
16
presence of NADH2, pH 8.0, 30°C
17
presence of NADH2 and FMNH2, pH 8.0, 30°C
29
presence of NADH2 and FADH2, pH 8.0, 30°C
30
presence of NADH, pH 8.0, 30°C
70
presence of NADH and FADH2, pH 8.0, 30°C
80
presence of NADH, pH 8.0, 30°C
81
presence of NADH and FADH2, pH 8.0, 30°C
107
presence of NADH and FMNH2, pH 8.0, 30°C
156
presence of NADH and FMNH2, pH 8.0, 30°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.9
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75% of maximum activity
8.1
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70% of maximum activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
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75% of maximum activity
40
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96% of maximum activity
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
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light scattering experiments
monomer
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1 * 45000, SDS-PAGE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
to 2.15 A resolution. The structure shows a domain-like insertion into a TIM-barrel, which might serve as a flexible lid for the active site. Docking of MgEDTA2- into EmoA identifies an intricate hydrogen bond network connected to Tyr71, which should lower its pKa. Tyr71, along with nearby Glu70 and a peroxy flavin, facilitates a keto-enol transition of the leaving acetyl group of EDTA. The interaction between EmoA and oxidoreductase EmoB enhances both EmoA and EmoB activities probably through coupled channelling of FMNH2
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the emoA and emoB genes are cotranscribed when BNC1 cells are grown on EDTA
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E70A
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complete loss of activtiy
P291A
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74.4% of wild-type activity
Q294A
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85.6% of wild-type activity
Q58A
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51.3% of wild-type activity
R68A
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85.3% of wild-type activity
W11A
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26.4% of wild-type activity
Y71A
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complete loss of activtiy
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis