ArticleScientific reports2018
Structural Studies based on two Lysine Dioxygenases with Distinct Regioselectivity Brings Insights Into Enzyme Specificity within the Clavaminate Synthase-Like Family.
Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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10 citing papers in PubMed, 7 citations in OpenAlex.
- Article
- Lid loop-mediated proton transfer revealed in the Fe/αKG-dependent decarboxylase TraH.Communications chemistry · 2026Article
- ASMC: investigating the amino acid diversity of enzyme active sites.Bioinformatics (Oxford, England) · 2025Article
- Sequential oxidation of L-lysine by a non-heme iron hydroxylase.bioRxiv : the preprint server for biology · 2025Article
- An Active Site Tyr Residue Guides the Regioselectivity of Lysine Hydroxylation by Nonheme Iron Lysine-4-hydroxylase Enzymes through Proton-Coupled Electron Transfer.Journal of the American Chemical Society · 2024Article
- Biocatalytic control of site-selectivity and chain length-selectivity in radical amino acid halogenases.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Enhancing regioselectivity of sucrose phosphorylase by loop engineering for glycosylation of L-ascorbic acid.Applied microbiology and biotechnology · 2022Article
- Review
- Harnessing the biocatalytic potential of iron- and α-ketoglutarate-dependent dioxygenases in natural product total synthesis.Natural product reports · 2020Review
- Novel halo- and thermo-tolerant Cohnella sp. A01 L-glutaminase: heterologous expression and biochemical characterization.Scientific reports · 2019Article
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5 authors at 3 institutions in 1 country.
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Abstract
Iron(II)/α-ketoacid-dependent oxygenases (αKAOs) are enzymes that catalyze the oxidation of unactivated C-H bonds, mainly through hydroxylation. Among these, those that are active towards amino-acids and their derivatives are grouped in the Clavaminate Synthase Like (CSL) family. CSL enzymes exhibit high regio- and stereoselectivities with strict substrate specificity. This study reports the structural elucidation of two new regiodivergent members, KDO1 and KDO5, active towards lysine, and the structural and computational analysis of the whole family through modelling and classification of active sites. The structures of KDO1 and KDO5 in complex with their ligands show that one exact position in the active site controls the regioselectivity of the reaction. Our results suggest that the substrate specificity and high stereoselectivity typical of this family is linked to a lid that closes up in order to form a sub-pocket around the side chain of the substrate. This dynamic lid is found throughout the family with varying sequence and length and is associated with a conserved stable dimeric interface. Results from this study could be a starting-point for exploring the functional diversity of the CSL family and direct in vitro screening in the search for new enzymatic activities.
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