ReviewEngineering microbiology2023
Oxidative modification of free-standing amino acids by Fe(II)/αKG-dependent oxygenases.
Review in Engineering microbiology, 2023. 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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Who cites it
10 citing papers in PubMed.
- Active-site recognition enables hydroxylation of a fluorine-deactivated C-H bond in 6,6,6-trifluoro-L-norleucine.Chemical communications (Cambridge, England) · 2026Article
- Protein Structuromics Reveals a Loop-Controlled Half-Open Active Pocket Conformation Throughout Fe(II)/α-ketoglutarate-Dependent Dioxygenase Catalytic Cycle.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Discovery and Biosynthesis of the Novel Glycotetrapeptide Antibiotic Biffamycin A.Angewandte Chemie (International ed. in English) · 2026Article
- Molecular Basis of α-Glycine C-H Activation by a Nonheme Fe(II)/2-Oxoglutarate Dioxygenase.Biochemistry · 2026Article
- Review
- Mechanistic Divergence in Sulfur-Ligated Iron(III)-Alkylperoxo Reactivity: Aldehyde Oxidation Prevails over Deformylation.Angewandte Chemie (International ed. in English) · 2025Article
- Substrate Epoxidation Catalyzed by the Nonheme Iron Dioxygenase Dapdiamide Biosynthesis Enzyme C. Why Is the Substrate Tethered?Chemistry (Weinheim an der Bergstrasse, Germany) · 2025Article
- C-C Bond Cleavage in the Late-Stage Biosynthesis of Huperzine Alkaloids Occurs via Enzymatic Retro-Aza-Prins Reaction.Journal of the American Chemical Society · 2025Article
- Discovery and substrate specificity engineering of nucleotide halogenases.Nature communications · 2024Article
- Semi-Rational Design of L-Isoleucine Dioxygenase Generated Its Activity for Aromatic Amino Acid Hydroxylation.Molecules (Basel, Switzerland) · 2023Article
Corrections and comments
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Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Fe(II)/α-ketoglutarate (αKG)-dependent oxygenases catalyze the oxidative modification of various molecules, from DNA, RNA, and proteins to primary and secondary metabolites. They also catalyze a variety of biochemical reactions, including hydroxylation, halogenation, desaturation, epoxidation, cyclization, peroxidation, epimerization, and rearrangement. Given the versatile catalytic capability of such oxygenases, numerous studies have been conducted to characterize their functions and elucidate their structure-function relationships over the past few decades. Amino acids, particularly nonproteinogenic amino acids, are considered as important building blocks for chemical synthesis and components for natural product biosynthesis. In addition, the Fe(II)/αKG-dependent oxygenase superfamily includes important enzymes for generating amino acid derivatives, as they efficiently modify various free-standing amino acids. The recent discovery of new Fe(II)/αKG-dependent oxygenases and the repurposing of known enzymes in this superfamily have promoted the generation of useful amino acid derivatives. Therefore, this study will focus on the recent progress achieved from 2019 to 2022 to provide a clear view of the mechanism by which these enzymes have expanded the repertoire of free amino acid oxidative modifications.
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