ArticleActa crystallographica. Section F, Structural biology communications2017
In crystallo activity tests with latent apple tyrosinase and two mutants reveal the importance of the mutated sites for polyphenol oxidase activity.
Article in Acta crystallographica. Section F, Structural biology communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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9 citing papers in PubMed, 16 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
- Molecular and Enzymatic Characterization of Flavonoid 3'-Hydroxylase ofPlants (Basel, Switzerland) · 2021Article
- 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
- 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
- Conversion of walnut tyrosinase into a catechol oxidase by site directed mutagenesis.Scientific reports · 2020Article
- A Peptide-Induced Self-Cleavage Reaction Initiates the Activation of Tyrosinase.Angewandte Chemie (International ed. in English) · 2019Article
- Biochemical and structural characterization of tomato polyphenol oxidases provide novel insights into their substrate specificity.Scientific reports · 2019Article
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4 authors at 1 institution in 1 country.
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Abstract
Tyrosinases are type 3 copper enzymes that belong to the polyphenol oxidase (PPO) family and are able to catalyze both the ortho-hydroxylation of monophenols and their subsequent oxidation to o-quinones, which are precursors for the biosynthesis of colouring substances such as melanin. The first plant pro-tyrosinase from Malus domestica (MdPPO1) was recombinantly expressed in its latent form (56.4 kDa) and mutated at four positions around the catalytic pocket which are believed to influence the activity of the enzyme. Mutating the amino acids, which are known as activity controllers, yielded the mutants MdPPO1-Ala239Thr and MdPPO1-Leu243Arg, whereas mutation of the so-called water-keeper and gatekeeper residues resulted in the mutants MdPPO1-Glu234Ala and MdPPO1-Phe259Ala, respectively. The wild-type enzyme and two of the mutants, MdPPO1-Ala239Thr and MdPPO1-Phe259Ala, were successfully crystallized, leading to single crystals that diffracted to 1.35, 1.55 and 1.70 Å resolution, respectively. All crystals belonged to space group P2
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