ArticleAngewandte Chemie (International ed. in English)2020
Identification of Amino Acid Residues Responsible for C-H Activation in Type-III Copper Enzymes by Generating Tyrosinase Activity in a Catechol Oxidase.
Article in Angewandte Chemie (International ed. in English), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 42 citations in OpenAlex.
- In silico and in vitro exploration of a tyrosinase for biocatalytic production of catechols.FEBS open bio · 2026Article
- Structural insights intoInorganic chemistry frontiers · 2026Article
- Article
- Biochemical Analysis of Recombinant Pea Seed Coat-Specific Polyphenol Oxidase (Journal of agricultural and food chemistry · 2025Article
- Identification of an Activity Selector for the Nitroso-Forming Activity in Bacterial Type-III Copper Enzymes.Angewandte Chemie (International ed. in English) · 2025Article
- Endohedral Coordination of Bulky Substrates in Metalloenzyme-Like Organometallic Nanotubes.Chemistry (Weinheim an der Bergstrasse, Germany) · 2025Article
- Coupled Binuclear Copper Sites in Biology: An Experimentally-Calibrated Computational Perspective.Coordination chemistry reviews · 2025Article
- Tyrosinases: a family of copper-containing metalloenzymes.Chemtexts · 2024Article
- Experimental Evidence and Mechanistic Description of the Phenolic H-Transfer to the CuJournal of the American Chemical Society · 2023Article
- The Crystal Structure of Tyrosinase fromBiomolecules · 2023Article
- Genome-Wide Analysis of the Polyphenol Oxidase Gene Family inAntioxidants (Basel, Switzerland) · 2023Article
- New mechanistic insights into coupled binuclear copper monooxygenases from the recent elucidation of the ternary intermediate of tyrosinase.FEBS letters · 2023Review
- Biochemical characterization of Dimocarpus longan polyphenol oxidase provides insights into its catalytic efficiency.Scientific reports · 2022Article
- The Relationship between the ICMolecules (Basel, Switzerland) · 2022Article
- Considerations Regarding Activity Determinants of Fungal Polyphenol Oxidases Based on Mutational and Structural Studies.Applied and environmental microbiology · 2021Article
- Similar but Still Different: Which Amino Acid Residues Are Responsible for Varying Activities in Type-III Copper Enzymes?Chembiochem : a European journal of chemical biology · 2021Review
- Plant Copper Metalloenzymes As Prospects for New Metabolism Involving Aromatic Compounds.Frontiers in plant science · 2021Review
- Identification of Amino Acid Residues Responsible for C-H Activation in Type-III Copper Enzymes by Generating Tyrosinase Activity in a Catechol Oxidase.Angewandte Chemie (International ed. in English) · 2020Article
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3 authors at 1 institution in 1 country.
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Abstract
Tyrosinases (TYRs) catalyze the hydroxylation of phenols and the oxidation of the resulting o-diphenols to o-quinones, while catechol oxidases (COs) exhibit only the latter activity. Aurone synthase (AUS) is not able to react with classical tyrosinase substrates, such as tyramine and l-tyrosine, while it can hydroxylate its natural substrate isoliquiritigenin. The structural difference of TYRs, COs, and AUS at the heart of their divergent catalytic activities is still a puzzle. Therefore, a library of 39 mutants of AUS from Coreopsis grandiflora (CgAUS) was generated and the activity studies showed that the reactivity of the three conserved histidines (HisA
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