ArticleAngewandte Chemie (International ed. in English)2015
The Structure of a Plant Tyrosinase from Walnut Leaves Reveals the Importance of "Substrate-Guiding Residues" for Enzymatic Specificity.
Article in Angewandte Chemie (International ed. in English), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.
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45 citing papers in PubMed, 121 citations in OpenAlex.
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- Historical Insights Into the Purification of Polyphenol Oxidase From Plants.Food science & nutrition · 2025Review
- Biochemical Analysis of Recombinant Pea Seed Coat-Specific Polyphenol Oxidase (Journal of agricultural and food chemistry · 2025Article
- Classification of polyphenol oxidases shows ancient gene duplication leading to two distinct enzyme types.iScience · 2025Article
- Coupled Binuclear Copper Sites in Biology: An Experimentally-Calibrated Computational Perspective.Coordination chemistry reviews · 2025Article
- Genetic Linkage betweenInternational journal of molecular sciences · 2024Article
- Tyrosinases: a family of copper-containing metalloenzymes.Chemtexts · 2024Article
- Synthesis,Journal of enzyme inhibition and medicinal chemistry · 2023Article
- The Crystal Structure of Tyrosinase fromBiomolecules · 2023Article
- Genome-Wide Analysis of the Polyphenol Oxidase Gene Family inAntioxidants (Basel, Switzerland) · 2023Article
- High-quality genome assembly and multi-omics analysis of pigment synthesis pathway inFrontiers in microbiology · 2023Article
- Biochemical characterization of Dimocarpus longan polyphenol oxidase provides insights into its catalytic efficiency.Scientific reports · 2022Article
- Computational Analysis of Triazole-Based Kojic Acid Analogs as Tyrosinase Inhibitors by Molecular Dynamics and Free Energy Calculations.Molecules (Basel, Switzerland) · 2022Article
- Evidence for H-bonding interactions to the μ-ηChemical communications (Cambridge, England) · 2022Article
- Identification of genomic regions associated with soybean responses to off-target dicamba exposure.Frontiers in plant science · 2022Article
- Synthesis of Multi-Protein Complexes through Charge-Directed Sequential Activation of Tyrosine Residues.Journal of the American Chemical Society · 2021Article
- Review
- Considerations Regarding Activity Determinants of Fungal Polyphenol Oxidases Based on Mutational and Structural Studies.Applied and environmental microbiology · 2021Article
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5 authors at 1 institution in 1 country.
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Abstract
Tyrosinases and catechol oxidases are members of the class of type III copper enzymes. While tyrosinases accept both mono- and o-diphenols as substrates, only the latter substrate is converted by catechol oxidases. Researchers have been working for decades to elucidate the monophenolase/diphenolase specificity on a structural level and have introduced an early hypothesis that states that the reason for the lack of monophenolase activity in catechol oxidases may be its structurally restricted active site. However, recent structural and biochemical studies of this enzyme class have raised doubts about this theory. Herein, the first crystal structure of a plant tyrosinase (from Juglans regia) is presented. The structure reveals that the distinction between mono- and diphenolase activity does not depend on the degree of restriction of the active site, and thus a more important role for amino acid residues located at the entrance to and in the second shell of the active site is proposed.
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