ArticleActa crystallographica. Section D, Biological crystallography2014
Latent and active abPPO4 mushroom tyrosinase cocrystallized with hexatungstotellurate(VI) in a single crystal.
Article in Acta crystallographica. Section D, Biological crystallography, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
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42 citing papers in PubMed, 126 citations in OpenAlex.
- Design, synthesis, and anticancer activity of novel isocryptolepine 'aza' type acyl thiourea derivatives via combined experimental and computational approach.Bioscience reports · 2026Article
- Tyrosinases: a family of copper-containing metalloenzymes.Chemtexts · 2024Article
- The Crystal Structure of Tyrosinase fromBiomolecules · 2023Article
- Speciation atlas of polyoxometalates in aqueous solutions.Science advances · 2023Article
- Exploring the Reactivity of Polyoxometalates toward Proteins: From Interactions to Mechanistic Insights.JACS Au · 2023Review
- Biochemical characterization of Dimocarpus longan polyphenol oxidase provides insights into its catalytic efficiency.Scientific reports · 2022Article
- Synthesis and characterization of the `Japanese rice-ball'-shaped Molybdenum Blue NaActa crystallographica. Section C, Structural chemistry · 2022Article
- Speciation of Transition-Metal-Substituted Keggin-Type Silicotungstates Affected by the Co-crystallization Conditions with Proteinase K.Inorganic chemistry · 2021Article
- Wells-Dawson phosphotungstates as mushroom tyrosinase inhibitors: a speciation study.Scientific reports · 2021Article
- A Novel Tyrosinase fromApplied and environmental microbiology · 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
- Polyphenol oxidases exhibit promiscuous proteolytic activity.Communications chemistry · 2020Article
- Conversion of walnut tyrosinase into a catechol oxidase by site directed mutagenesis.Scientific reports · 2020Article
- Biochemical and structural characterization of tomato polyphenol oxidases provide novel insights into their substrate specificity.Scientific reports · 2019Article
- Exploring Wells-Dawson Clusters Associated With the Small Ribosomal Subunit.Frontiers in chemistry · 2019Article
- Catalytic mechanism of the tyrosinase reaction toward the Tyr98 residue in the caddie protein.PLoS biology · 2018Article
- Total Synthesis, Stereochemical Assignment, and Divergent Enantioselective Enzymatic Recognition of Larreatricin.Chemistry (Weinheim an der Bergstrasse, Germany) · 2018Article
- The P-type ATPase inhibiting potential of polyoxotungstates.Metallomics : integrated biometal science · 2018Article
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5 authors at 2 institutions in 2 countries.
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Abstract
Tyrosinases, bifunctional metalloenzymes, catalyze the oxidation of monophenols and o-diphenols to o-quinones, the precursor compounds of the brown-coloured pigment melanin. In eukaryotic organisms, tyrosinases are expressed as latent zymogens that have to be proteolytically cleaved in order to form highly active enzymes. This activation mechanism, known as the tyrosinase maturation process, has scientific and industrial significance with respect to biochemical and technical applications of the enzyme. Here, not only the first crystal structure of the mushroom tyrosinase abPPO4 is presented in its active form (Ser2-Ser383) and in its 21 kDa heavier latent form (Ser2-Thr545), but furthermore the simultaneous presence of both forms within one single-crystal structure is shown. This allows for a simple approach to investigate the transition between these two forms. Isoform abPPO4 was isolated and extensively purified from the natural source (Agaricus bisporus), which contains a total of six polyphenol oxidases (PPOs). The enzyme formed crystals (diffracting to a resolution of 2.76 Å) owing to the employment of the 6-tungstotellurate(VI) salt (Na6[TeW6O24]·22H2O) as a cocrystallization agent. Two of these disc-shaped Anderson-type polyoxoanions [TeW6O24](6-) separate two asymmetric units comprising one crystallographic heterodimer of abPPO4, thus resulting in very interesting crystal packing.
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