ArticleScientific reports2019
Structural Insights into Catalytic Versatility of the Flavin-dependent Hydroxylase (HpaB) from Escherichia coli.
Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed.
- Efficient synthesis of l-DOPA inSynthetic and systems biotechnology · 2026Article
- Engineering non-P450 3-hydroxylase forSynthetic and systems biotechnology · 2025Article
- Elucidating the metabolic pathway and initial degradation gene forApplied and environmental microbiology · 2025Article
- Biosynthesis of Biphenomycin-like Macrocyclic Peptides by Formation and Cross-Linking ofJournal of the American Chemical Society · 2025Article
- Directed evolution of L-DOPA sensing and production enables efficient incorporation of an expanded genetic code into proteins.bioRxiv : the preprint server for biology · 2025Article
- Biodegradation of p-nitrophenol by Rhodococcus sp. 21391 unveils a two-component p-nitrophenol monooxygenase with broad substrate specificity.Microbial cell factories · 2025Article
- Biosynthesis of Macrocyclic Peptides by Formation and Crosslinking ofbioRxiv : the preprint server for biology · 2025Article
- Novel enzymatic route to the synthesis of C-8 hydroxyflavonoids including flavonols and isoflavones.Scientific reports · 2024Article
- Exploring the role of flavin-dependent monooxygenases in the biosynthesis of aromatic compounds.Biotechnology for biofuels and bioproducts · 2024Review
- 4-Hydroxyphenylacetate 3-Hydroxylase (4HPA3H): A Vigorous Monooxygenase for VersatileInternational journal of molecular sciences · 2024Review
- Unifying and versatile features of flavin-dependent monooxygenases: Diverse catalysis by a common C4a-(hydro)peroxyflavin.The Journal of biological chemistry · 2023Review
- Advances in 4-Hydroxyphenylacetate-3-hydroxylase Monooxygenase.Molecules (Basel, Switzerland) · 2023Review
- Modification of the 4-Hydroxyphenylacetate-3-hydroxylase Substrate Pocket to Increase Activity towards Resveratrol.Molecules (Basel, Switzerland) · 2023Article
- Oxygenating Biocatalysts for Hydroxyl Functionalisation in Drug Discovery and Development.ChemMedChem · 2022Review
- Engineered Bacterial Flavin-Dependent Monooxygenases for the Regiospecific Hydroxylation of Polycyclic Phenols.Chembiochem : a European journal of chemical biology · 2022Article
- A single amino acid substitution in aromatic hydroxylase (HpaB) of Escherichia coli alters substrate specificity of the structural isomers of hydroxyphenylacetate.BMC microbiology · 2020Article
- Developing a highly efficient hydroxytyrosol whole-cell catalyst by de-bottlenecking rate-limiting steps.Nature communications · 2020Article
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12 authors.
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No grant is acknowledged in the PubMed record.
Abstract
4-Hydroxyphenylacetate 3-hydroxylase (EcHpaB) from Escherichia coli is capable of efficient ortho-hydroxylation of a wide range of phenolic compounds and demonstrates great potential for broad chemoenzymatic applications. To understand the structural and mechanistic basis of its catalytic versatility, we elucidated the crystal structure of EcHpaB by X-ray crystallography, which revealed a unique loop structure covering the active site. We further performed mutagenesis studies of this loop to probe its role in substrate specificity and catalytic activity. Our results not only showed the loop has great plasticity and strong tolerance towards extensive mutagenesis, but also suggested a flexible loop that enables the entrance and stable binding of substrates into the active site is the key factor to the enzyme catalytic versatility. These findings lay the groundwork for editing the loop sequence and structure for generation of EcHpaB mutants with improved performance for broader laboratory and industrial use.
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