ArticleAngewandte Chemie (International ed. in English)2019
A Peptide-Induced Self-Cleavage Reaction Initiates the Activation of Tyrosinase.
Article in Angewandte Chemie (International ed. in English), 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 45 citations in OpenAlex.
- In silico and in vitro exploration of a tyrosinase for biocatalytic production of catechols.FEBS open bio · 2026Article
- Investigation and characterization of the GhPPO gene family and its expression in response to fibre cell growth and biotic stress in Gossypium hirsutum L.BMC genomics · 2025Article
- Simultaneous Monitoring of Tyrosinase and ATP in Thick Brain Tissues Using a Single Two-Photon Fluorescent Probe.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Classification of polyphenol oxidases shows ancient gene duplication leading to two distinct enzyme types.iScience · 2025Article
- Characterization of two bacterial tyrosinases from the halophilic bacterium Hahella sp. CCB MM4 relevant for phenolic compounds oxidation in wetlands.FEBS open bio · 2024Article
- Biosynthesis of Piceatannol from Resveratrol in Grapevine Can Be Mediated by Cresolase-DependentPlants (Basel, Switzerland) · 2024Article
- Tyrosinases: a family of copper-containing metalloenzymes.Chemtexts · 2024Article
- Biochemical Investigations of Five Recombinantly Expressed Tyrosinases Reveal Two Novel Mechanisms Impacting Carbon Storage in Wetland Ecosystems.Environmental science & technology · 2023Article
- The Crystal Structure of Tyrosinase fromBiomolecules · 2023Article
- Metabolic Pathway Reconstruction Indicates the Presence of Important Medicinal Compounds inInternational journal of molecular sciences · 2023Article
- Biochemical characterization of Dimocarpus longan polyphenol oxidase provides insights into its catalytic efficiency.Scientific reports · 2022Article
- The Novel Role of Tyrosinase Enzymes in the Storage of Globally Significant Amounts of Carbon in Wetland Ecosystems.Environmental science & technology · 2022Review
- 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
- Polyphenol oxidases exhibit promiscuous proteolytic activity.Communications chemistry · 2020Article
- Conversion of walnut tyrosinase into a catechol oxidase by site directed mutagenesis.Scientific reports · 2020Article
- Inhibition of apricot polyphenol oxidase by combinations of plant proteases and ascorbic acid.Food chemistry: X · 2019Article
- A Peptide-Induced Self-Cleavage Reaction Initiates the Activation of Tyrosinase.Angewandte Chemie (International ed. in English) · 2019Article
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Authors and funding
4 authors at 1 institution in 1 country.
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Abstract
The conversion of inactive pro-polyphenol oxidases (pro-PPOs) into the active enzyme results from the proteolytic cleavage of its C-terminal domain. Herein, a peptide-mediated cleavage process that activates pro-MdPPO1 (Malus domestica) is reported. Mass spectrometry, mutagenesis studies, and X-ray crystal-structure analysis of pro-MdPPO1 (1.35 Å) and two separated C-terminal domains, one obtained upon self-cleavage of pro-MdPPO1 and the other one produced independently, were applied to study the observed self-cleavage. The sequence Lys 355-Val 370 located in the linker between the active and the C-terminal domain is indispensable for the self-cleavage. Partial introduction (Lys 352-Ala 360) of this peptide into the sequence of two other PPOs, MdPPO2 and aurone synthase (CgAUS1), triggered self-cleavage in the resulting mutants. This is the first experimental proof of a self-cleavage-inducing peptide in PPOs, unveiling a new mode of activation for this enzyme class that is independent of any external protease.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.