The Structure of a Plant Tyrosinase from Walnut Leaves Reveals the Importance of “Substrate-Guiding Residues” for Enzymatic Specificity
M. Sc. Aleksandar Bijelic, Dipl.-Ing. Matthias Pretzler, Dipl.-Chem. Christian Molitor, M. Sc. Florime Zekiri and Prof. Dr. Annette Rompel * Institut für Biophysikalische Chemie, Fakultät für Chemie Universität Wien, Althanstraße 14, 1090 Wien (Austria) Angew. Chem. Int. Ed . 2015 , 54 , 1 DOI: 10.1002/anie.201506994 Abstract Tyrosinases and catechol oxidases are members of the class of type III copper enzymes. While tyrosinases accept both mono- and o -diphenols as substrates, only the latter substrate is converted by catechol oxidases. Researchers have been working for decades to elucidate the monophenolase/diphenolase specificity on a structural level and have introduced an early hypothesis that states that the reason for the lack of monophenolase activity in catechol oxidases may be its structurally restricted active site. However, recent structural and biochemical studies of this enzyme c...