ArticleJournal of the American Chemical Society2018
Use of a Tyrosine Analogue To Modulate the Two Activities of a Nonheme Iron Enzyme OvoA in Ovothiol Biosynthesis, Cysteine Oxidation versus Oxidative C-S Bond Formation.
Article in Journal of the American Chemical Society, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 54 citations in OpenAlex.
- Recent discoveries in mono- and dinuclear nonheme iron enzymes: Emerging mechanisms and catalytic strategies.Archives of biochemistry and biophysics · 2026Review
- Genetic Code Expansion: Recent Developments and Emerging Applications.Chemical reviews · 2025Review
- Structural insights into the convergent evolution of sulfoxide synthase EgtB-IV, an ergothioneine-biosynthetic homolog of ovothiol synthase OvoA.Structure (London, England : 1993) · 2024Article
- Discovery of the selenium-containing antioxidant ovoselenol derived from convergent evolution.Nature chemistry · 2024Article
- Noncanonical Amino Acids: Bringing New-to-Nature Functionalities to Biocatalysis.Chemical reviews · 2024Review
- Noncanonical Amino Acids in Biocatalysis.Chemical reviews · 2024Review
- Ovoselenol, a Selenium-containing Antioxidant Derived from Convergent Evolution.bioRxiv : the preprint server for biology · 2024Article
- Unusual cysteine modifications in natural product biosynthesis.RSC chemical biology · 2024Review
- Ergothioneine and its congeners: anti-ageing mechanisms and pharmacophore biosynthesis.Protein & cell · 2024Review
- Biochemical and Structural Characterization of OvoAACS catalysis · 2023Article
- An S=1 Iron(IV) Intermediate Revealed in a Non-Heme Iron Enzyme-Catalyzed Oxidative C-S Bond Formation.Angewandte Chemie (International ed. in English) · 2023Article
- Ergothioneine, Ovothiol A, and Selenoneine-Histidine-Derived, Biologically Significant, Trace Global Alkaloids.Molecules (Basel, Switzerland) · 2022Review
- OvoAChemical science · 2022Article
- Metabolic Adaptations to Marine Environments: Molecular Diversity and Evolution of Ovothiol Biosynthesis in Bacteria.Genome biology and evolution · 2021Article
- Proton-Coupled Electron-Transfer Reactivity Controls Iron versus Sulfur Oxidation in Nonheme Iron-Thiolate Complexes.Inorganic chemistry · 2021Article
- Implications for an imidazol-2-yl carbene intermediate in the rhodanase-catalyzed C-S bond formation reaction of anaerobic ergothioneine biosynthesis.ACS catalysis · 2021Article
- Chemical modifications of proteins and their applications in metalloenzyme studies.Synthetic and systems biotechnology · 2021Review
- Nonheme iron-thiolate complexes as structural models of sulfoxide synthase active sites.Dalton transactions (Cambridge, England : 2003) · 2020Article
- The complex evolutionary history of sulfoxide synthase in ovothiol biosynthesis.Proceedings. Biological sciences · 2019Article
- Crystal Structure of the Ergothioneine Sulfoxide Synthase fromACS catalysis · 2019Article
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Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
Abstract
Ovothiol is a histidine thiol derivative. The biosynthesis of ovothiol involves an extremely efficient trans-sulfuration strategy. The nonheme iron enzyme OvoA catalyzed oxidative coupling between cysteine and histidine is one of the key steps. Besides catalyzing the oxidative coupling between cysteine and histidine, OvoA also catalyzes the oxidation of cysteine to cysteine sulfinic acid (cysteine dioxygenase activity). Thus far, very little mechanistic information is available for OvoA-catalysis. In this report, we measured the kinetic isotope effect (KIE) in OvoA-catalysis using the isotopically sensitive branching method. In addition, by replacing an active site tyrosine (Tyr417) with 2-amino-3-(4-hydroxy-3-(methylthio)phenyl)propanoic acid (MtTyr) through the amber suppressor mediated unnatural amino acid incorporation method, the two OvoA activities (oxidative coupling between cysteine and histidine, and cysteine dioxygenase activity) can be modulated. These results suggest that the two OvoA activities branch out from a common intermediate and that the active site tyrosine residue plays some key roles in controlling the partitioning between these two pathways.
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