ReviewApplied and environmental microbiology2012
Ring-cleaving dioxygenases with a cupin fold.
Review in Applied and environmental microbiology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 72 papers.
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Who cites it
72 citing papers in PubMed, 192 citations in OpenAlex.
- Genome-wide association studies builds a predictive model and reveals novel resistance features for macrolide-resistant Bordetella pertussis.The Journal of antimicrobial chemotherapy · 2026Article
- Microbial-mediated degradation of benzyl paraben: isolation, characterization, and mechanistic insights.World journal of microbiology & biotechnology · 2026Article
- Article
- Molecular basis for adaptive evolution of aromatic degradation enzymes in bacteria revealed by metagenomics.Frontiers in microbiology · 2026Review
- Biodegradation of Diesel by Free and ImmobilizedACS omega · 2025Article
- Effects of Pirin-like proteins on PAT biosynthesis and stress resilience in postharvest apple pathogen Penicillium expansum.Archives of microbiology · 2025Article
- Draft genome sequence of benzo[a]pyrene degradingMicrobiology resource announcements · 2025Article
- Characterization of the substrate specificity and regioselectivity of ring-cleavage of Pseudomonas putida DLL-E4 hydroquinone 1,2-dioxygenase (PnpC1C2).Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2025Article
- Bioremediation of Polycyclic Aromatic Hydrocarbons by Means of Bacteria and Bacterial Enzymes.Microorganisms · 2024Review
- Novel enzymes for biodegradation of polycyclic aromatic hydrocarbons identified by metagenomics and functional analysis in short-term soil microcosm experiments.Scientific reports · 2024Article
- Biosynthesis of Cytosporones in Leotiomycetous Filamentous Fungi.Journal of the American Chemical Society · 2024Article
- Observing extradiol dioxygenases in action through a crystalline lens.Methods in enzymology · 2024Article
- Transcriptional Reprogramming ofJournal of fungi (Basel, Switzerland) · 2023Article
- Crystal structure of the monocupin ring-cleaving dioxygenase 5-nitrosalicylate 1,2-dioxygenase from Bradyrhizobium sp.Acta crystallographica. Section D, Structural biology · 2023Article
- Bioconversion of 4-hydroxyestradiol by extradiol ring-cleavage dioxygenases from Novosphingobium sp. PP1Y.Scientific reports · 2023Article
- Polyphenols as Drivers of a Homeostatic Gut Microecology and Immuno-Metabolic Traits ofInternational journal of molecular sciences · 2022Review
- Review
- Intradiol ring cleavage dioxygenases from herbivorous spider mites as a new detoxification enzyme family in animals.BMC biology · 2022Article
- Charge Maintenance during Catalysis in Nonheme Iron Oxygenases.ACS catalysis · 2022Article
- Article
12 more citing papers are in PubMed but not listed here.
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Authors and funding
1 author at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Ring-cleaving dioxygenases catalyze key reactions in the aerobic microbial degradation of aromatic compounds. Many pathways converge to catecholic intermediates, which are subject to ortho or meta cleavage by intradiol or extradiol dioxygenases, respectively. However, a number of degradation pathways proceed via noncatecholic hydroxy-substituted aromatic carboxylic acids like gentisate, salicylate, 1-hydroxy-2-naphthoate, or aminohydroxybenzoates. The ring-cleaving dioxygenases active toward these compounds belong to the cupin superfamily, which is characterized by a six-stranded β-barrel fold and conserved amino acid motifs that provide the 3His or 2- or 3His-1Glu ligand environment of a divalent metal ion. Most cupin-type ring cleavage dioxygenases use an Fe(II) center for catalysis, and the proposed mechanism is very similar to that of the canonical (type I) extradiol dioxygenases. The metal ion is presumed to act as an electron conduit for single electron transfer from the metal-bound substrate anion to O(2), resulting in activation of both substrates to radical species. The family of cupin-type dioxygenases also involves quercetinase (flavonol 2,4-dioxygenase), which opens up two C-C bonds of the heterocyclic ring of quercetin, a wide-spread plant flavonol. Remarkably, bacterial quercetinases are capable of using different divalent metal ions for catalysis, suggesting that the redox properties of the metal are relatively unimportant for the catalytic reaction. The major role of the active-site metal ion could be to correctly position the substrate and to stabilize transition states and intermediates rather than to mediate electron transfer. The tentative hypothesis that quercetinase catalysis involves direct electron transfer from metal-bound flavonolate to O(2) is supported by model chemistry.
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