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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Gasparetti, Chiara Nordlund, Emilia Jänis, Janne Kruus, Kristiina Buchert, Johanna |
| Description | Author Affiliation: Gasparetti C ( VTT Technical Research Centre of Finland, Espoo, Finland. ext-Chiara.Gasparetti@vtt.fi) |
| Abstract | Tyrosinase (EC 1.14.18.1) is a widely distributed type 3 copper enzyme participating in essential biological functions. Tyrosinases are potential biotools as biosensors or protein crosslinkers. Understanding the reaction mechanism of tyrosinases is fundamental for developing tyrosinase-based applications. The reaction mechanisms of tyrosinases from Trichoderma reesei (TrT) and Agaricus bisporus (AbT) were analyzed using three diphenolic substrates: caffeic acid, L-DOPA (3,4-dihydroxy- l -phenylalanine), and catechol. With caffeic acid the oxidation rates of TrT and AbT were comparable; whereas with L-DOPA or catechol a fast decrease in the oxidation rates was observed in the TrT-catalyzed reactions only, suggesting end product inhibition of TrT. Dopachrome was the only reaction end product formed by TrT- or AbT-catalyzed oxidation of L-DOPA. We produced dopachrome by AbT-catalyzed oxidation of L-DOPA and analyzed the TrT end product (i.e. dopachrome) inhibition by oxygen consumption measurement. In the presence of 1.5 mM dopachrome the oxygen consumption rate of TrT on 8 mM L-DOPA was halved. The type of inhibition of potential inhibitors for TrT was studied using p -coumaric acid (monophenol) and caffeic acid (diphenol) as substrates. The strongest inhibitors were potassium cyanide for the TrT-monophenolase activity, and kojic acid for the TrT-diphenolase activity. The lag period related to the TrT-catalyzed oxidation of monophenol was prolonged by kojic acid, sodium azide and arbutin; contrary it was reduced by potassium cyanide. Furthermore, sodium azide slowed down the initial oxidation rate of TrT- and AbT-catalyzed oxidation of L-DOPA or catechol, but it also formed adducts with the reaction end products, i.e., dopachrome and o -benzoquinone. |
| ISSN | 00063002 |
| Journal | Biochimica et Biophysica Acta (BBA) - Reviews on Cancer |
| Issue Number | 4 |
| Volume Number | 1824 |
| Language | English |
| Publisher | Elsevier |
| Publisher Date | 2012-04-01 |
| Publisher Place | Netherlands |
| Access Restriction | Open |
| Subject Keyword | Agaricus Enzymology Fungal Proteins Chemistry Monophenol Monooxygenase Trichoderma Caffeic Acids Catechols Coumaric Acids Enzyme Inhibitors Antagonists & Inhibitors Indolequinones Intracellular Fluid Kinetics Levodopa Oxidation-Reduction Potassium Cyanide Pyrones Sodium Azide Spectrophotometry, Ultraviolet Research Support, Non-U.S. Gov't Biochemistry |
| Content Type | Text |
| Resource Type | Article |
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