ReviewChembiochem : a European journal of chemical biology2021
Similar but Still Different: Which Amino Acid Residues Are Responsible for Varying Activities in Type-III Copper Enzymes?
Review in Chembiochem : a European journal of chemical biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 53 citations in OpenAlex.
- Rational design of triazole tyrosinase inhibitors via integrated free energy calculations.Molecular diversity · 2026Article
- In silico and in vitro exploration of a tyrosinase for biocatalytic production of catechols.FEBS open bio · 2026Article
- Structural insights intoInorganic chemistry frontiers · 2026Article
- Structural insights into the catalytic mechanism of ammonia monooxygenase.Nature communications · 2025Article
- Biochemical Analysis of Recombinant Pea Seed Coat-Specific Polyphenol Oxidase (Journal of agricultural and food chemistry · 2025Article
- Identification of an Activity Selector for the Nitroso-Forming Activity in Bacterial Type-III Copper Enzymes.Angewandte Chemie (International ed. in English) · 2025Article
- The small molecule ML233 is a direct inhibitor of tyrosinase function.Communications biology · 2025Article
- Classification of polyphenol oxidases shows ancient gene duplication leading to two distinct enzyme types.iScience · 2025Article
- The small molecule ML233 is a direct inhibitor of tyrosinase function.bioRxiv : the preprint server for biology · 2025Article
- Characterization of two bacterial tyrosinases from the halophilic bacterium Hahella sp. CCB MM4 relevant for phenolic compounds oxidation in wetlands.FEBS open bio · 2024Article
- Tyrosinases: a family of copper-containing metalloenzymes.Chemtexts · 2024Article
- Experimental Evidence and Mechanistic Description of the Phenolic H-Transfer to the CuJournal of the American Chemical Society · 2023Article
- Biochemical Investigations of Five Recombinantly Expressed Tyrosinases Reveal Two Novel Mechanisms Impacting Carbon Storage in Wetland Ecosystems.Environmental science & technology · 2023Article
- The Crystal Structure of Tyrosinase fromBiomolecules · 2023Article
- Phenoloxidases: catechol oxidase - the temporary employer and laccase - the rising star of vascular plants.Horticulture research · 2023Article
- Structural insight into polyphenol oxidation during black tea fermentation.Food chemistry: X · 2023Article
- New mechanistic insights into coupled binuclear copper monooxygenases from the recent elucidation of the ternary intermediate of tyrosinase.FEBS letters · 2023Review
- The Novel Role of Tyrosinase Enzymes in the Storage of Globally Significant Amounts of Carbon in Wetland Ecosystems.Environmental science & technology · 2022Review
- Evidence for H-bonding interactions to the μ-ηChemical communications (Cambridge, England) · 2022Article
- Wells-Dawson phosphotungstates as mushroom tyrosinase inhibitors: a speciation study.Scientific reports · 2021Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Type-III copper enzymes like polyphenol oxidases (PPOs) are ubiquitous among organisms and play a significant role in the formation of pigments. PPOs comprise different enzyme groups, including tyrosinases (TYRs) and catechol oxidases (COs). TYRs catalyze the o-hydroxylation of monophenols and the oxidation of o-diphenols to the corresponding o-quinones (EC 1.14.18.1). In contrast, COs only catalyze the oxidation of o-diphenols to the corresponding o-quinones (EC 1.10.3.1). To date (August 2020), 102 PDB entries encompassing 18 different proteins from 16 organisms and several mutants have been reported, identifying key residues for tyrosinase activity. The structural similarity between TYRs and COs, especially within and around the active center, complicates the elucidation of their modes of action on a structural basis. However, mutagenesis studies illuminate residues that influence the two activities and show that crystallography on its own cannot elucidate the enzymatic activity mode. Several amino acid residues around the dicopper active center have been proposed to play an essential role in the two different activities. Herein, we critically review the role of all residues identified so far that putatively affect the two activities of PPOs.
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