5M6B
structure of recombinant mushroom tyrosinase (abPPO4)
Summary for 5M6B
| Entry DOI | 10.2210/pdb5m6b/pdb |
| Descriptor | Polyphenol oxidase 4, COPPER (II) ION, OXYGEN ATOM (3 entities in total) |
| Functional Keywords | heterologous expression, polyphenol oxidase, tyrosinase activity, agaricus bisporus, oxidoreductase |
| Biological source | Agaricus bisporus (White button mushroom) |
| Total number of polymer chains | 4 |
| Total formula weight | 261260.68 |
| Authors | Pretzler, M.,Bijelic, A.,Rompel, A. (deposition date: 2016-10-24, release date: 2017-05-17, Last modification date: 2024-01-17) |
| Primary citation | Pretzler, M.,Bijelic, A.,Rompel, A. Heterologous expression and characterization of functional mushroom tyrosinase (AbPPO4). Sci Rep, 7:1810-1810, 2017 Cited by PubMed Abstract: Tyrosinases are an ubiquitous group of copper containing metalloenzymes that hydroxylate and oxidize phenolic molecules. In an application context the term 'tyrosinase' usually refers to 'mushroom tyrosinase' consisting of a mixture of isoenzymes and containing a number of enzymatic side-activities. We describe a protocol for the efficient heterologous production of tyrosinase 4 from Agaricus bisporus in Escherichia coli. Applying this procedure a pure preparation of a single isoform of latent tyrosinase can be achieved at a yield of 140 mg per liter of autoinducing culture medium. This recombinant protein possesses the same fold as the enzyme purified from the natural source as evidenced by single crystal X-ray diffraction. The latent enzyme can be activated by limited proteolysis with proteinase K which cleaves the polypeptide chain after K382, only one The latent enzyme can amino acid before the main in-vivo activation site. Latent tyrosinase can be used as obtained and enzymatic activity may be induced in the reaction mixture by the addition of an ionic detergent (e.g. 2 mM SDS). The proteolytically activated mushroom tyrosinase shows >50% of its maximal activity in the range of pH 5 to 10 and accepts a wide range of substrates including mono- and diphenols, flavonols and chalcones. PubMed: 28500345DOI: 10.1038/s41598-017-01813-1 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.25 Å) |
Structure validation
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