Catechol Oxidase (Tyrosinase) Highly Pure

<strong>Catechol Oxidase (Tyrosinase)</strong>_x000D_ <strong>Catalog number:</strong> B2010450_x000D_ <strong>Lot number:</strong> Batch Dependent_x000D_ <strong>Expiration Date:</strong> Batch dependent_x000D_ <strong>Amount:</strong> 25 kU_x000D_ <strong>Molecular Weight or Concentration:</strong> 119.5 kDa_x000D_ <strong>Supplied as:</strong> Lyophilized powder_x000D_ <strong>Appearance:</strong> Powder_x000D_ <strong>Applications:</strong> highly pure, high specific activity (≥1000 unit/mg solid) Catechol Oxidase purified from mushroom._x000D_ <strong>Storage:</strong> −20°C_x000D_ <strong>Keywords:</strong> Monophenol Monooxygenase, Catechol Oxidase, Monophenol, dihydroxyphenylalanine:oxygen oxidoreductase, Polyphenol Oxidase_x000D_ <strong>Grade:</strong> Biotechnology grade. All solid components are highly pure (minimum 95%). All solutions are made with Type I ultrapure water (resistivity &gt;18 MΩ-cm) and are filtered through 0.22 um._x000D_ _x000D_ <strong>References:</strong>_x000D_ 1: Prexler SM, Frassek M, Moerschbacher BM, Dirks-Hofmeister ME. Catechol_x000D_ Oxidase versus Tyrosinase Classification Revisited by Site-Directed Mutagenesis_x000D_ Studies. Angew Chem Int Ed Engl. 2019 Jun 24;58(26):8757-8761._x000D_ _x000D_ 2: Eicken C, Krebs B, Sacchettini JC. Catechol oxidase - structure and activity._x000D_ Curr Opin Struct Biol. 1999 Dec;9(6):677-83._x000D_ _x000D_ 3: Benaceur F, Gouzi H, Meddah B, Neifar A, Guergouri A. Purification and_x000D_ characterization of catechol oxidase from Tadela (Phoenix dactylifera L.) date_x000D_ fruit. Int J Biol Macromol. 2019 Mar 15;125:1248-1256._x000D_ _x000D_ 4: Terán A, Jaafar A, Sánchez-Peláez AE, Torralba MC, Gutiérrez Á. Design and_x000D_ catalytic studies of structural and functional models of the catechol_oxidase_x000D_ enzyme. J Biol Inorg Chem. 2020 Jun;25(4):671-683._x000D_ _x000D_ 5: Koval IA, Gamez P, Belle C, Selmeczi K, Reedijk J. Synthetic models of the_x000D_ active site of catechol_oxidase: mechanistic studies. Chem Soc Rev. 2006_x000D_ Sep;35(9):814-40._x000D_ _x000D_ 6: Penttinen L, Rutanen C, Jänis J, Rouvinen J, Hakulinen N. Unraveling_x000D_ Substrate Specificity and Catalytic Promiscuity of Aspergillus oryzae Catechol_x000D_ Oxidase. Chembiochem. 2018 Nov 16;19(22):2348-2352._x000D_ _x000D_ 7: Gerdemann C, Eicken C, Krebs B. The crystal structure of catechol_oxidase:_x000D_ new insight into the function of type-3 copper proteins. Acc Chem Res. 2002_x000D_ Mar;35(3):183-91._x000D_ _x000D_ 8: Moon KM, Kwon EB, Lee B, Kim CY. Recent Trends in Controlling the Enzymatic_x000D_ Browning of Fruit and Vegetable Products. Molecules. 2020 Jun 15;25(12):2754._x000D_ _x000D_ 9: Solem E, Tuczek F, Decker H. Tyrosinase versus Catechol_Oxidase: One_x000D_ Asparagine Makes the Difference. Angew Chem Int Ed Engl. 2016 Feb_x000D_ 18;55(8):2884-8._x000D_ <a href="https://pubmed.ncbi.nlm.nih.gov/15185133/">10: Siegbahn PE. The catalytic cycle of catechol oxidase. J Biol Inorg Chem._x000D_ 2004 Jul;9(5):577-90. </a>_x000D_ _x000D_ <strong>Products Related to Catechol Oxidase (Tyrosinase) </strong> <a href="https://moleculardepot.com/product-category/Enzymes/">: Enzymes</a>