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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The enzyme appears in viruses and cellular organisms
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 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
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
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
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
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
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
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
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
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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
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
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
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
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