ArticleFEBS letters2015
Site-directed mutagenesis around the CuA site of a polyphenol oxidase from Coreopsis grandiflora (cgAUS1).
Article in FEBS letters, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 23 citations in OpenAlex.
- Historical Insights Into the Purification of Polyphenol Oxidase From Plants.Food science & nutrition · 2025Review
- Tyrosinases: a family of copper-containing metalloenzymes.Chemtexts · 2024Article
- The Crystal Structure of Tyrosinase fromBiomolecules · 2023Article
- Biochemical characterization of Dimocarpus longan polyphenol oxidase provides insights into its catalytic efficiency.Scientific reports · 2022Article
- 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
- Histidine residues at the copper-binding site in human tyrosinase are essential for its catalytic activities.Journal of enzyme inhibition and medicinal chemistry · 2020Article
- Conversion of walnut tyrosinase into a catechol oxidase by site directed mutagenesis.Scientific reports · 2020Article
- Three recombinantly expressed apple tyrosinases suggest the amino acids responsible for mono- versus diphenolase activity in plant polyphenol oxidases.Scientific reports · 2017Article
- In crystallo activity tests with latent apple tyrosinase and two mutants reveal the importance of the mutated sites for polyphenol oxidase activity.Acta crystallographica. Section F, Structural biology communications · 2017Article
- Ten Good Reasons for the Use of the Tellurium-Centered Anderson-Evans Polyoxotungstate in Protein Crystallography.Accounts of chemical research · 2017Review
- The Structure of a Plant Tyrosinase from Walnut Leaves Reveals the Importance of "Substrate-Guiding Residues" for Enzymatic Specificity.Angewandte Chemie (International ed. in English) · 2015Article
- Structure-function correlations in tyrosinases.Protein science : a publication of the Protein Society · 2015Review
- Crystallization and preliminary crystallographic analysis of latent, active and recombinantly expressed aurone synthase, a polyphenol oxidase, from Coreopsis grandiflora.Acta crystallographica. Section F, Structural biology communications · 2015Article
- Multi-Omics Unveils the Dual-Life of the Aquatic Plant Potamogeton nodosus.Physiologia plantarumArticle
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Aurone synthase from Coreopsis grandiflora (cgAUS1), catalyzing conversion of butein to sulfuretin in a type-3 copper center, is a rare example of a polyphenol oxidase involved in anabolism. Site-directed mutagenesis around the CuA site of AUS1 was performed, and recombinant enzymes were analyzed by mass spectrometry. Replacement of the coordinating CuA histidines with alanine resulted in the presence of a single copper and loss of diphenolase activity. The thioether bridge-building cysteine and a phenylalanine over the CuA site, exchanged to alanine, have no influence on copper content but appear to play an important role in substrate binding.
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