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Information on EC 1.14.14.33 - ethylenediaminetetraacetate monooxygenase
for references in articles please use BRENDA:EC1.14.14.33
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EC Tree 1 Oxidoreductases
1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
1.14.14 With reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen into the other donor
1.14.14.33 ethylenediaminetetraacetate monooxygenase
IUBMB Comments
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.
The enzyme appears in viruses and cellular organisms
Reaction Schemes
show+
2
+
2
=
+
2
+
2
+
2
Synonyms
EmoA, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
EmoA
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ethylenediaminetetraacetate + 2 FMNH2 + 2 O2 = ethylenediamine-N,N'-diacetate + 2 glyoxylate + 2 FMN + 2 H2O
overall reaction
-
-
-
ethylenediaminetetraacetate + FMNH2 + O2 = ethylenediaminetriacetate + glyoxylate + FMN + H2O
(1a)
-
-
-
ethylenediaminetriacetate + FMNH2 + O2 = ethylenediamine-N,N'-diacetate + glyoxylate + FMN + H2O
(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.
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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
diethylenetriaminepentaacetate + FMNH2 + O2
diethylenetriaminetetraacetate + glyoxylate + FMN + H2O
Substrates: -
Products: -
Products: -
?
ethylenediaminetetraacetate + 2 FADH2 + 2 O2
ethylenediamine-N,N'-diacetate + 2 glyoxylate + 2 FAD + 2 H2O
ethylenediaminetetraacetate + 2 FMNH2 + 2 O2
ethylenediamine-N,N'-diacetate + 2 glyoxylate + 2 FMN + 2 H2O
ethylenediaminetetraacetate + FMNH2 + O2
ethylenediaminetriacetate + glyoxylate + FMN + H2O
ethylenediaminetriacetate + FMNH2 + O2
ethylenediamine-N,N'-diacetate + glyoxylate + FMN + H2O
nitrilotriacetate + FMNH2 + O2
nitrilodiacetate + glyoxylate + FMN + H2O
Substrates: -
Products: -
Products: -
?
ethylenediaminetetraacetate + 2 FADH2 + 2 O2
ethylenediamine-N,N'-diacetate + 2 glyoxylate + 2 FAD + 2 H2O
Substrates: -
Products: overall reaction
Products: overall reaction
?
ethylenediaminetetraacetate + 2 FADH2 + 2 O2
ethylenediamine-N,N'-diacetate + 2 glyoxylate + 2 FAD + 2 H2O
Substrates: -
Products: overall reaction
Products: overall reaction
?
ethylenediaminetetraacetate + 2 FADH2 + 2 O2
ethylenediamine-N,N'-diacetate + 2 glyoxylate + 2 FAD + 2 H2O
Substrates: -
Products: overall reaction
Products: overall reaction
?
ethylenediaminetetraacetate + 2 FADH2 + 2 O2
ethylenediamine-N,N'-diacetate + 2 glyoxylate + 2 FAD + 2 H2O
Substrates: -
Products: overall reaction
Products: overall reaction
?
ethylenediaminetetraacetate + 2 FMNH2 + 2 O2
ethylenediamine-N,N'-diacetate + 2 glyoxylate + 2 FMN + 2 H2O
Substrates: -
Products: overall reaction
Products: overall reaction
?
ethylenediaminetetraacetate + 2 FMNH2 + 2 O2
ethylenediamine-N,N'-diacetate + 2 glyoxylate + 2 FMN + 2 H2O
Substrates: -
Products: overall reaction
Products: overall reaction
?
ethylenediaminetetraacetate + 2 FMNH2 + 2 O2
ethylenediamine-N,N'-diacetate + 2 glyoxylate + 2 FMN + 2 H2O
Substrates: 100% activity in presence of Mg2+, 53% in presence of Zn2+, 35% in presence of Mn2+, 19% in presence of Co2+, 11% in presence of Cu2+
Products: -
Products: -
?
ethylenediaminetetraacetate + 2 FMNH2 + 2 O2
ethylenediamine-N,N'-diacetate + 2 glyoxylate + 2 FMN + 2 H2O
Substrates: -
Products: overall reaction
Products: overall reaction
?
ethylenediaminetetraacetate + 2 FMNH2 + 2 O2
ethylenediamine-N,N'-diacetate + 2 glyoxylate + 2 FMN + 2 H2O
Substrates: 100% activity in presence of Mg2+, 53% in presence of Zn2+, 35% in presence of Mn2+, 19% in presence of Co2+, 11% in presence of Cu2+
Products: -
Products: -
?
ethylenediaminetetraacetate + 2 FMNH2 + 2 O2
ethylenediamine-N,N'-diacetate + 2 glyoxylate + 2 FMN + 2 H2O
Substrates: -
Products: overall reaction
Products: overall reaction
?
ethylenediaminetetraacetate + 2 FMNH2 + 2 O2
ethylenediamine-N,N'-diacetate + 2 glyoxylate + 2 FMN + 2 H2O
Substrates: -
Products: overall reaction
Products: overall reaction
?
ethylenediaminetetraacetate + 2 FMNH2 + 2 O2
ethylenediamine-N,N'-diacetate + 2 glyoxylate + 2 FMN + 2 H2O
Substrates: -
Products: -
Products: -
?
ethylenediaminetetraacetate + 2 FMNH2 + 2 O2
ethylenediamine-N,N'-diacetate + 2 glyoxylate + 2 FMN + 2 H2O
Substrates: -
Products: overall reaction
Products: overall reaction
?
ethylenediaminetetraacetate + 2 FMNH2 + 2 O2
ethylenediamine-N,N'-diacetate + 2 glyoxylate + 2 FMN + 2 H2O
Substrates: -
Products: overall reaction
Products: overall reaction
?
ethylenediaminetetraacetate + FMNH2 + O2
ethylenediaminetriacetate + glyoxylate + FMN + H2O
Substrates: -
Products: -
Products: -
?
ethylenediaminetetraacetate + FMNH2 + O2
ethylenediaminetriacetate + glyoxylate + FMN + H2O
Substrates: -
Products: -
Products: -
?
ethylenediaminetetraacetate + FMNH2 + O2
ethylenediaminetriacetate + glyoxylate + FMN + H2O
Substrates: -
Products: -
Products: -
?
ethylenediaminetriacetate + FMNH2 + O2
ethylenediamine-N,N'-diacetate + glyoxylate + FMN + H2O
Substrates: -
Products: -
Products: -
?
ethylenediaminetriacetate + FMNH2 + O2
ethylenediamine-N,N'-diacetate + glyoxylate + FMN + H2O
Substrates: -
Products: -
Products: -
?
ethylenediaminetriacetate + FMNH2 + O2
ethylenediamine-N,N'-diacetate + glyoxylate + FMN + H2O
Substrates: -
Products: -
Products: -
?
additional information
?
-
Substrates: the EDTA-oxidizing enzyme complex accepts EDTA as a substrate only when it is complexed with Mg2+, Zn2+, Mn2+, Co2+, or Cu2+. It catalyzes the removal of acetyl groups from several other aminopolycarboxylic acids that possess three or more acetyl groups
Products: -
Products: -
?
additional information
?
-
Substrates: the EDTA-oxidizing enzyme complex accepts EDTA as a substrate only when it is complexed with Mg2+, Zn2+, Mn2+, Co2+, or Cu2+. It catalyzes the removal of acetyl groups from several other aminopolycarboxylic acids that possess three or more acetyl groups
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme oxidizes both EDTA complexed with various metal ions and uncomplexed EDTA
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
ethylenediaminetetraacetate + 2 FMNH2 + 2 O2
ethylenediamine-N,N'-diacetate + 2 glyoxylate + 2 FMN + 2 H2O
ethylenediaminetetraacetate + 2 FMNH2 + 2 O2
ethylenediamine-N,N'-diacetate + 2 glyoxylate + 2 FMN + 2 H2O
Substrates: -
Products: overall reaction
Products: overall reaction
?
ethylenediaminetetraacetate + 2 FMNH2 + 2 O2
ethylenediamine-N,N'-diacetate + 2 glyoxylate + 2 FMN + 2 H2O
Substrates: -
Products: overall reaction
Products: overall reaction
?
ethylenediaminetetraacetate + 2 FMNH2 + 2 O2
ethylenediamine-N,N'-diacetate + 2 glyoxylate + 2 FMN + 2 H2O
Substrates: -
Products: overall reaction
Products: overall reaction
?
ethylenediaminetetraacetate + 2 FMNH2 + 2 O2
ethylenediamine-N,N'-diacetate + 2 glyoxylate + 2 FMN + 2 H2O
Substrates: -
Products: overall reaction
Products: overall reaction
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0085
ethylenediaminetetraacetate
presence of Mg2+, pH 7.8, 35Ā°C
0.034
ethylenediaminetetraacetate
no addition of divalent ions, pH 7.8, 35Ā°C
0.0461
ethylenediaminetetraacetate
wild-type, presence of Mg2+ and oxidoreductase EmoB, pH 7.6, temperature not specified in the publication
0.047
ethylenediaminetetraacetate
mutant R68A, presence of Mg2+, pH 7.6, temperature not specified in the publication
0.0492
ethylenediaminetetraacetate
wild-type, presence of Mg2+, pH 7.6, temperature not specified in the publication
0.0615
ethylenediaminetetraacetate
wild-type, presence of Mg2+ and flavin reductase from Escherichia coli, pH 7.6, temperature not specified in the publication
0.069
ethylenediaminetetraacetate
mutant Q294A, presence of Mg2+, pH 7.6, temperature not specified in the publication
0.198
ethylenediaminetetraacetate
mutant W11A, presence of Mg2+, pH 7.6, temperature not specified in the publication
0.49
ethylenediaminetetraacetate
mutant Q58A, presence of Mg2+, pH 7.6, temperature not specified in the publication
0.521
ethylenediaminetetraacetate
mutant P291A, presence of Mg2+, pH 7.6, temperature not specified in the publication
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2.8
ethylenediaminetetraacetate
no addition of divalent ions, pH 7.8, 35Ā°C
3.6
ethylenediaminetetraacetate
presence of Mg2+, pH 7.8, 35Ā°C
4.5
ethylenediaminetetraacetate
mutant W11A, presence of Mg2+, pH 7.6, temperature not specified in the publication
8.8
ethylenediaminetetraacetate
mutant Q58A, presence of Mg2+, pH 7.6, temperature not specified in the publication
12.8
ethylenediaminetetraacetate
mutant P291A, presence of Mg2+, pH 7.6, temperature not specified in the publication
13.2
ethylenediaminetetraacetate
wild-type, presence of Mg2+ and flavin reductase from Escherichia coli, pH 7.6, temperature not specified in the publication
14.7
ethylenediaminetetraacetate
mutant Q294A, presence of Mg2+, pH 7.6, temperature not specified in the publication
14.7
ethylenediaminetetraacetate
mutant R68A, presence of Mg2+, pH 7.6, temperature not specified in the publication
17.2
ethylenediaminetetraacetate
wild-type, presence of Mg2+, pH 7.6, temperature not specified in the publication
47.1
ethylenediaminetetraacetate
wild-type, presence of Mg2+ and oxidoreductase EmoB, pH 7.6, temperature not specified in the publication
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
20
ethylenediaminetetraacetate
mutant P291A, presence of Mg2+, pH 7.6, temperature not specified in the publication
20
ethylenediaminetetraacetate
mutant Q58A, presence of Mg2+, pH 7.6, temperature not specified in the publication
20
ethylenediaminetetraacetate
mutant W11A, presence of Mg2+, pH 7.6, temperature not specified in the publication
31
ethylenediaminetetraacetate
mutant R68A, presence of Mg2+, pH 7.6, temperature not specified in the publication
80
ethylenediaminetetraacetate
no addition of divalent ions, pH 7.8, 35Ā°C
210
ethylenediaminetetraacetate
mutant Q294A, presence of Mg2+, pH 7.6, temperature not specified in the publication
350
ethylenediaminetetraacetate
wild-type, presence of Mg2+, pH 7.6, temperature not specified in the publication
430
ethylenediaminetetraacetate
presence of Mg2+, pH 7.8, 35Ā°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3.8
3.8
pH 7.8, temperature not specified in the publication
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE RANGE
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.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
EmoA is a reduced flavin mononucleotide-utilizing monooxygenase and EmoB is an NADH:flavin mononucleotide oxidoreductase. The two-enzyme system oxidizes EDTA to ethylenediaminediacetate (EDDA) and nitrilotriacetate (NTA) to iminodiacetate (IDA) with the production of glyoxylate
physiological function
EmoA is a reduced flavin mononucleotide-utilizing monooxygenase and EmoB is an NADH:flavin mononucleotide oxidoreductase. The two-enzyme system oxidizes EDTA to ethylenediaminediacetate (EDDA) and nitrilotriacetate (NTA) to iminodiacetate (IDA) with the production of glyoxylate
physiological function
enzyme catalyzes the first reaction of EDTA decomposition by cell extracts, an NADH-dependent process that is accompanied by O2 uptake
physiological function
enzyme catalyzes the first reaction of EDTA decomposition by cell extracts, an NADH-dependent process that is accompanied by O2 uptake
physiological function
enzyme catalyzes the first reaction of EDTA decomposition by cell extracts, an NADH2-dependent process that is accompanied by O2 uptake
physiological function
the first two steps of the catabolic pathway for EDTA consist of the sequential oxidative removal of two acetyl groups, resulting in the formation of glyoxylate. Ethylenediaminetriacetate (ED3A) is formed as an intermediate and N,N'-ethylenediaminediacetate is the end product. The enzyme complex consists of a monooxygenase, which catalyzes the cleavage of EDTA and ED3A while consuming oxygen and reduced flavin mononucleotide FMNH2, and an NADH2:FMN oxidoreductase that provides FMNH2 for the monooxygenase. The oxidoreductase can be replaced by other NADH2:FMN oxidoreductases
physiological function
-
EmoA is a reduced flavin mononucleotide-utilizing monooxygenase and EmoB is an NADH:flavin mononucleotide oxidoreductase. The two-enzyme system oxidizes EDTA to ethylenediaminediacetate (EDDA) and nitrilotriacetate (NTA) to iminodiacetate (IDA) with the production of glyoxylate
-
physiological function
-
the first two steps of the catabolic pathway for EDTA consist of the sequential oxidative removal of two acetyl groups, resulting in the formation of glyoxylate. Ethylenediaminetriacetate (ED3A) is formed as an intermediate and N,N'-ethylenediaminediacetate is the end product. The enzyme complex consists of a monooxygenase, which catalyzes the cleavage of EDTA and ED3A while consuming oxygen and reduced flavin mononucleotide FMNH2, and an NADH2:FMN oxidoreductase that provides FMNH2 for the monooxygenase. The oxidoreductase can be replaced by other NADH2:FMN oxidoreductases
-
physiological function
-
enzyme catalyzes the first reaction of EDTA decomposition by cell extracts, an NADH-dependent process that is accompanied by O2 uptake
-
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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). A7LIY3_9HYPH
204
0
22403
TrEMBL
Mitochondrion (Reliability: 3)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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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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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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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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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the emoA and emoB genes are cotranscribed when BNC1 cells are grown on EDTA
the emoA and emoB genes are cotranscribed when BNC1 cells are grown on EDTA
the emoA and emoB genes are cotranscribed when BNC1 cells are grown on EDTA
the emoA and emoB genes are cotranscribed when BNC1 cells are grown on EDTA
-
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
analysis
design of a system of primers to obtain emoA gene fragments approximately 750 bp long for bacterial destructors of EDTA. The system can be effectively used for detecting the emoA gene in representatives of Alpha- and Gammaproteobacteria
analysis
design of a system of primers to obtain emoA gene fragments approximately 750 bp long for bacterial destructors of EDTA. The system can be effectively used for detecting the emoA gene in representatives of Alpha- and Gammaproteobacteria
analysis
design of a system of primers to obtain emoA gene fragments approximately 750 bp long for bacterial destructors of EDTA. The system can be effectively used for detecting the emoA gene in representatives of Alpha- and Gammaproteobacteria
analysis
-
design of a system of primers to obtain emoA gene fragments approximately 750 bp long for bacterial destructors of EDTA. The system can be effectively used for detecting the emoA gene in representatives of Alpha- and Gammaproteobacteria
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Payne, J.W.; Bolton, H.; Campbell, J.A.; Xun, L.
Purification and characterization of EDTA monooxygenase from the EDTA-degrading bacterium BNC1
J. Bacteriol.
180
3823-3827
1998
EDTA-degrading bacterium BNC1 (Q9F9T3)
brenda
Kaparullina, E.; Fedorov, D.; Doronina, N.; Trotsenko, Y.
System of oligonucleotide primers for detection and amplification of the emoA gene encoding bacterial ethylenediaminetetraacetate monooxygenase
Appl. Biochem. Microbiol.
44
361-365
2008
Chelativorans multitrophicus (A7LKG7), Chelativorans oligotrophicus (A7LIY3), Chelativorans oligotrophicus LPM-4 (A7LIY3), Stenotrophomonas chelatiphaga (A7LKG8)
-
brenda
Bohuslavek, J.; Payne, J.; Liu, Y.; Bolton H., J.; Xun, L.
Cloning, sequencing, and characterization of a gene cluster involved in EDTA degradation from the bacterium BNC1
Appl. Environ. Microbiol.
67
688-695
2001
Chelativorans multitrophicus (A7LKG9), Chelativorans multitrophicus DSM 9103 (A7LKG9), EDTA-degrading bacterium BNC1 (Q9F9T3)
brenda
Witschel, M.; Nagel, S.; Egli, T.
Identification and characterization of the two-enzyme system catalyzing oxidation of EDTA in the EDTA-degrading bacterial strain DSM 9103
J. Bacteriol.
179
6937-6943
1997
Chelativorans multitrophicus (A7LKG9), Chelativorans multitrophicus DSM 9103 (A7LKG9)
brenda
Jun, S.Y.; Lewis, K.M.; Youn, B.; Xun, L.; Kang, C.
Structural and biochemical characterization of EDTA monooxygenase and its physical interaction with a partner flavin reductase
Mol. Microbiol.
100
989-1003
2016
EDTA-degrading bacterium BNC1 (Q9F9T3)
brenda
EXTERNAL LINKS (specific for EC-Number 1.14.14.33)
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