5CE9

structure of tyrosinase from walnut (Juglans regia)

Summary for 5CE9

• Entry DOI: 10.2210/pdb5ce9/pdb
• Descriptor: Polyphenol oxidase, COPPER (II) ION, OXYGEN ATOM, ... (5 entities in total)
• Functional Keywords: polyphenol oxidase, tyrosinase, monophenolase activtiy, diphenolase activity, oxidoreductase
• Biological source: Juglans regia (English walnut)
• Total number of polymer chains: 2
• Total formula weight: 77267.21

Authors

Bijelic, A.,Pretzler, M.,Zekiri, F.,Rompel, A. (deposition date: 2015-07-06, release date: 2015-10-28, Last modification date: 2024-11-06)

Primary citation

Bijelic, A.,Pretzler, M.,Molitor, C.,Zekiri, F.,Rompel, A.
The Structure of a Plant Tyrosinase from Walnut Leaves Reveals the Importance of """"Substrate-Guiding Residues"""" for Enzymatic Specificity.
Angew.Chem.Int.Ed.Engl., 54:14677-14680, 2015

PubMed 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 class have raised doubts about this theory. Herein, the first crystal structure of a plant tyrosinase (from Juglans regia) is presented. The structure reveals that the distinction between mono- and diphenolase activity does not depend on the degree of restriction of the active site, and thus a more important role for amino acid residues located at the entrance to and in the second shell of the active site is proposed.

PubMed: 26473311
DOI: 10.1002/anie.201506994

Experimental method

X-RAY DIFFRACTION (1.8 Å)