title: Recombinant Tyrosinase from Polyporus arcularius: Overproduction in Escherichia coli, Characterization, and Use in a Study of Aurones as Tyrosinase Effectors.
abstract: Tyrosinases act in the development of organoleptic properties of tea, raisins, etc., but also cause unwanted browning of fruits, vegetables, and mushrooms. The tyrosinase from Agaricus bisporus has been used as a model to study tyrosinase inhibitors, which are also indispensable in the treatment of skin pigmentation disorders. However, this model has disadvantages such as side enzyme activities and the presence of multiple isoenzymes. Therefore, we aimed to introduce a new tyrosinase model. The pro-tyrosinase from Polyporus arcularius was overproduced in Escherichia coli. Trypsin digestion led to a cleavage after R388 and hence enzyme activation. The tyrosinase was a homodimer and transformed L-DOPA and tert-butylcatechol preferentially. Various aurons were examined as effectors of this enzyme. 2'- and 3'-hydroxyaurones acted as its activators and 2',4'-dihydroxyaurone as an inhibitor, whereas 4'-hydroxyaurones were its substrates. The enzyme is a promising model for tyrosinase effector studies, being a single isoenzyme and void of side enzyme activities.
authors.affiliation: Institute of Microbiology, Czech Academy of Sciences , Vídeňská 1083, 142 20 Prague, Czech Republic.|Department of Biochemistry and Microbiology, Faculty of Food and Biochemical Technology, University of Chemistry and Technology Prague , Technická 3, 166 28 Prague, Czech Republic.
authors.forename: Eva
authors.initials: E
authors.lastname: Marková
authors.affiliation: Institute of Microbiology, Czech Academy of Sciences , Vídeňská 1083, 142 20 Prague, Czech Republic.
authors.forename: Michael
authors.initials: M
authors.lastname: Kotik
authors.affiliation: Institute of Microbiology, Czech Academy of Sciences , Vídeňská 1083, 142 20 Prague, Czech Republic.
authors.forename: Alena
authors.initials: A
authors.lastname: Křenková
authors.affiliation: Institute of Microbiology, Czech Academy of Sciences , Vídeňská 1083, 142 20 Prague, Czech Republic.
authors.forename: Petr
authors.initials: P
authors.lastname: Man
authors.affiliation: Université Grenoble Alpes, CNRS, DPM UMR 5063 , 38041 Grenoble, France.
authors.forename: Romain
authors.initials: R
authors.lastname: Haudecoeur
authors.affiliation: Université Grenoble Alpes, CNRS, DPM UMR 5063 , 38041 Grenoble, France.
authors.forename: Ahcène
authors.initials: A
authors.lastname: Boumendjel
authors.affiliation: Aix Marseille Université, Centrale Marseille, CNRS, ISm2 UMR 7313 , 13397 Marseille, France.
authors.forename: Renaud
authors.initials: R
authors.lastname: Hardré
authors.affiliation: Aix Marseille Université, Centrale Marseille, CNRS, ISm2 UMR 7313 , 13397 Marseille, France.
authors.forename: Yasmina
authors.initials: Y
authors.lastname: Mekmouche
authors.affiliation: Aix Marseille Université, Centrale Marseille, CNRS, ISm2 UMR 7313 , 13397 Marseille, France.
authors.forename: Elise
authors.initials: E
authors.lastname: Courvoisier-Dezord
authors.affiliation: Aix Marseille Université, Centrale Marseille, CNRS, ISm2 UMR 7313 , 13397 Marseille, France.
authors.forename: Marius
authors.initials: M
authors.lastname: Réglier
authors.affiliation: Institute of Microbiology, Czech Academy of Sciences , Vídeňská 1083, 142 20 Prague, Czech Republic.
authors.forename: Ludmila
authors.initials: L
authors.lastname: Martínková
mesh_terms: D001572:Benzofurans / Q000378:metabolism*; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism; D005656:Fungal Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D015870:Gene Expression; D007700:Kinetics; D014442:Monophenol Monooxygenase / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D055492:Polyporus / Q000201:enzymology*; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism
chemical_list: D001572:Benzofurans; D005656:Fungal Proteins; D011994:Recombinant Proteins; C486837:aurone; D014442:Monophenol Monooxygenase
keywords: Escherichia coli; Polyporus arcularius; aurones; trypsin digestion; tyrosinase