ReviewProtein science : a publication of the Protein Society2019
Monooxygenation of aromatic compounds by flavin-dependent monooxygenases.
Review in Protein science : a publication of the Protein Society, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed, 99 citations in OpenAlex.
- Dual cytosine modification through hydroxylation and arabinofuranosylation in phages.Nature chemical biology · 2026Article
- The Flexible Peripheral Segments Modulate the Catalytic Activity of the FAD-Containing Monooxygenase EthA fromBiomolecules · 2026Article
- Structural basis for oxidative decarboxylation of lignin-derived aromatics by the fungal flavoprotein monooxygenase PcMNX1.The Journal of biological chemistry · 2026Article
- Fungal endophyte-enhanced phytoremediation of persistent organic pollutants: mechanisms, advances, and future prospects.World journal of microbiology & biotechnology · 2026Review
- Integrative genomic and transcriptomic insights into the biocontrol activity ofFrontiers in microbiology · 2026Article
- Multiscale metabolic engineering in biological lignin valorization.Innovation (Cambridge (Mass.)) · 2025Review
- Investigations of the Flavin-Dependent Monooxygenase PhzO Involved in Phenazine Biosynthesis.Microbial biotechnology · 2025Article
- Biodegradation of p-nitrophenol by Rhodococcus sp. 21391 unveils a two-component p-nitrophenol monooxygenase with broad substrate specificity.Microbial cell factories · 2025Article
- Characterization of the Flavin-Dependent Monooxygenase Involved in the Biosynthesis of the Nocardiosis-Associated Polyketide†.Biochemistry · 2024Article
- Exploring the role of flavin-dependent monooxygenases in the biosynthesis of aromatic compounds.Biotechnology for biofuels and bioproducts · 2024Review
- Ligand bound structure of a 6-hydroxynicotinic acid 3-monooxygenase provides mechanistic insights.Archives of biochemistry and biophysics · 2024Article
- 4-Hydroxyphenylacetate 3-Hydroxylase (4HPA3H): A Vigorous Monooxygenase for VersatileInternational journal of molecular sciences · 2024Review
- Elucidation of 4-Hydroxybenzoic Acid Catabolic Pathways inInternational journal of molecular sciences · 2024Article
- Unifying and versatile features of flavin-dependent monooxygenases: Diverse catalysis by a common C4a-(hydro)peroxyflavin.The Journal of biological chemistry · 2023Review
- Mechanism UnderlyingToxins · 2023Article
- Non-Native Site-Selective Enzyme Catalysis.Chemical reviews · 2023Review
- Gut microbiome of mealworms (Tenebrio molitor Larvae) show similar responses to polystyrene and corn straw diets.Microbiome · 2023Article
- Semi-Rational Design of L-Isoleucine Dioxygenase Generated Its Activity for Aromatic Amino Acid Hydroxylation.Molecules (Basel, Switzerland) · 2023Article
- Oxygenating Biocatalysts for Hydroxyl Functionalisation in Drug Discovery and Development.ChemMedChem · 2022Review
- Genome mining of Burkholderia ambifaria strain T16, a rhizobacterium able to produce antimicrobial compounds and degrade the mycotoxin fusaric acid.World journal of microbiology & biotechnology · 2022Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Many flavoenzymes catalyze hydroxylation of aromatic compounds especially phenolic compounds have been isolated and characterized. These enzymes can be classified as either single-component or two-component flavin-dependent hydroxylases (monooxygenases). The hydroxylation reactions catalyzed by the enzymes in this group are useful for modifying the biological properties of phenolic compounds. This review aims to provide an in-depth discussion of the current mechanistic understanding of representative flavin-dependent monooxygenases including 3-hydroxy-benzoate 4-hydroxylase (PHBH, a single-component hydroxylase), 3-hydroxyphenylacetate 4-hydroxylase (HPAH, a two-component hydroxylase), and other monooxygenases which catalyze reactions in addition to hydroxylation, including 2-methyl-3-hydroxypyridine-5-carboxylate oxygenase (MHPCO, a single-component enzyme that catalyzes aromatic-ring cleavage), and HadA monooxygenase (a two-component enzyme that catalyzes additional group elimination reaction). These enzymes have different unique structural features which dictate their reactivity toward various substrates and influence their ability to stabilize flavin intermediates such as C4a-hydroperoxyflavin. Understanding the key catalytic residues and the active site environments important for governing enzyme reactivity will undoubtedly facilitate future work in enzyme engineering or enzyme redesign for the development of biocatalytic methods for the synthesis of valuable compounds.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.