ArticleCommunications chemistry2020
Polyphenol oxidases exhibit promiscuous proteolytic activity.
Article in Communications chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
What it found
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Who cites it
12 citing papers in PubMed, 35 citations in OpenAlex.
- Biochemical Analysis of Recombinant Pea Seed Coat-Specific Polyphenol Oxidase (Journal of agricultural and food chemistry · 2025Article
- Standardization guidelines and future trends for PET hydrolase research.Nature communications · 2025Review
- Classification of polyphenol oxidases shows ancient gene duplication leading to two distinct enzyme types.iScience · 2025Article
- Article
- Tyrosinases: a family of copper-containing metalloenzymes.Chemtexts · 2024Article
- Tyrosinase enzyme purification and immobilization from Pseudomonas sp. EG22 using cellulose coated magnetic nanoparticles: characterization and application in melanin production.World journal of microbiology & biotechnology · 2023Article
- Biochemical Investigations of Five Recombinantly Expressed Tyrosinases Reveal Two Novel Mechanisms Impacting Carbon Storage in Wetland Ecosystems.Environmental science & technology · 2023Article
- Biochemical characterization of Dimocarpus longan polyphenol oxidase provides insights into its catalytic efficiency.Scientific reports · 2022Article
- Desiccation Tolerance inPlants (Basel, Switzerland) · 2022Article
- Current Advances in the Biodegradation and Bioconversion of Polyethylene Terephthalate.Microorganisms · 2021Review
- Considerations Regarding Activity Determinants of Fungal Polyphenol Oxidases Based on Mutational and Structural Studies.Applied and environmental microbiology · 2021Article
- "Clicking" an Ionic Liquid to a Potent Antimicrobial Peptide: On the Route towards Improved Stability.International journal of molecular sciences · 2020Article
Corrections and comments
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Authors and funding
9 authors at 5 institutions in 2 countries.
Funding
Abstract
Tyrosinases catalyse both the cresolase and catecholase reactions for the formation of reactive compounds which are very important for industrial applications. In this study, we describe a proteolytic activity of tyrosinases. Two different tyrosinases originating from mushroom and apple are able to cleave the carboxylesterase EstA. The cleavage reaction correlates with the integrity of the active site of tyrosinase and is independent of other possible influencing factors, which could be present in the reaction. Therefore, the cleavage of EstA represents a novel functionality of tyrosinases. EstA was previously reported to degrade synthetic polyesters, albeit slowly. However, the EstA truncated by tyrosinase shows higher degradation activity on the non-biodegradable polyester polyethylene terephthalate (PET), which is a well-established environmental threat.
Identifiers
What OpenQuestion holds
Registered trials
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.