ArticlePlant molecular biology2018
A specific amino acid residue in the catalytic site of dandelion polyphenol oxidases acts as 'selector' for substrate specificity.
Article in Plant molecular biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 16 citations in OpenAlex.
- Structural insights intoInorganic chemistry frontiers · 2026Article
- 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
- Phenoloxidases: catechol oxidase - the temporary employer and laccase - the rising star of vascular plants.Horticulture research · 2023Article
- Enzymatic browning: The role of substrates in polyphenol oxidase mediated browning.Current research in food science · 2023Review
- 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
- Conversion of walnut tyrosinase into a catechol oxidase by site directed mutagenesis.Scientific reports · 2020Article
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Authors and funding
4 authors at 1 institution in 2 countries.
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No grant is acknowledged in the PubMed record.
Abstract
key messageSuccessful site-directed mutagenesis combined with in silico modeling and docking studies for the first time offers experimental proof of the role of the 'substrate selector' residue in plant polyphenol oxidases. The plant and fungi enzymes responsible for tissue browning are called polyphenol oxidases (PPOs). In plants, PPOs often occur as families of isoenzymes which are differentially expressed, but little is known about their physiological roles or natural substrates. In a recent study that explored these structure-function relationships, the eleven known dandelion (Taraxacum officinale) PPOs were shown to separate into two different phylogenetic groups differing in catalytic cavity architecture, kinetic parameters, and substrate range. The same study proposed that the PPOs' substrate specificity is controlled by one specific amino acid residue positioned at the entrance to the catalytic site: whereas group 1 dandelion PPOs possess a hydrophobic isoleucine (I) at position H
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