ArticleMolecular microbiology2016
Structural and biochemical characterization of EDTA monooxygenase and its physical interaction with a partner flavin reductase.
Article in Molecular microbiology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Structural, biophysical, and biochemical insights into C-S bond cleavage by dimethylsulfone monooxygenase.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- In silico screening and heterologous expression of soluble dimethyl sulfide monooxygenases of microbial origin in Escherichia coli.Applied microbiology and biotechnology · 2022Article
- Structures of the alkanesulfonate monooxygenase MsuD provide insight into C-S bond cleavage, substrate scope, and an unexpected role for the tetramer.The Journal of biological chemistry · 2021Article
- A [6+4]-cycloaddition adduct is the biosynthetic intermediate in streptoseomycin biosynthesis.Nature communications · 2021Article
- Formicamycin biosynthesis involves a unique reductive ring contraction.Chemical science · 2020Article
- Microbial Degradation of Pyridine: a Complete Pathway inApplied and environmental microbiology · 2020Article
- The Structural Basis of the Binding of Various Aminopolycarboxylates by the Periplasmic EDTA-Binding Protein EppA fromInternational journal of molecular sciences · 2020Article
- Bacterial non-specific nucleases of the phospholipase D superfamily and their biotechnological potential.Applied microbiology and biotechnology · 2020Review
- A Novel Aerobic Degradation Pathway for Thiobencarb Is Initiated by the TmoAB Two-Component Flavin Mononucleotide-Dependent Monooxygenase System in Acidovorax sp. Strain T1.Applied and environmental microbiology · 2017Article
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Authors and funding
5 authors.
Funding
Abstract
Ethylenediaminetetraacetate (EDTA) is currently the most abundant organic pollutant due to its recalcitrance and extensive use. Only a few bacteria can degrade it, using EDTA monooxygenase (EmoA) to initiate the degradation. EmoA is an FMNH2 -dependent monooxygenase that requires an NADH:FMN oxidoreductase (EmoB) to provide FMNH2 as a cosubstrate. Although EmoA has been identified from Chelativorans (ex. Mesorhizobium) sp. BNC1, its catalytic mechanism is unknown. Crystal structures of EmoA revealed a domain-like insertion into a TIM-barrel, which might serve as a flexible lid for the active site. Docking of MgEDTA(2-) into EmoA identified an intricate hydrogen bond network connected to Tyr(71) , which should potentially lower its pKa. Tyr(71) , along with nearby Glu(70) and a peroxy flavin, facilitates a keto-enol transition of the leaving acetyl group of EDTA. Further, for the first time, the physical interaction between EmoA and EmoB was observed by ITC, molecular docking and enzyme kinetic assay, which enhanced both EmoA and EmoB activities probably through coupled channelling of FMNH2 .
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