The Structure of a Plant Tyrosinase from Walnut Leaves Reveals the Importance of “Substrate‐Guiding Residues” for Enzymatic Specificity
Author:
Affiliation:
1. Institut für Biophysikalische Chemie, Fakultät für Chemie, Universität Wien, Althanstraße 14, 1090 Wien (Austria) http://www.bpc.univie.ac.at
Funder
Funded Access
Austrian Science Fund
FWF
Publisher
Wiley
Subject
General Chemistry,Catalysis
Link
https://onlinelibrary.wiley.com/doi/pdf/10.1002/anie.201506994
Reference24 articles.
1. Structure-function correlations in tyrosinases
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3. Tyrosinase: The four oxidation states of the active site and their relevance to enzymatic activation, oxidation and inactivation
4. Novel Roles for the Polyphenol Oxidase Enzyme in Secondary Metabolism and the Regulation of Cell Death in Walnut
5. Crystal structure of a plant catechol oxidase containing a dicopper center
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