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. 2020 May 15;3:62. doi: 10.1038/s42004-020-0305-2

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© The Author(s) 2020

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 1 — Tyrosinases catalyse reactions from monophenols to o-quinones through monophenolase (a) and diphenolase (b) activity. Incubation of the commercial tyrosinase from A. bisporus (AbT) with the carboxylesterase EstA led to a cleavage of the latter into a big (ΔEstA) and a small subunit (c). EstA was cleaved at a specific site between Ser71 and Ile72. The 71 amino acids cleaved off form an α-helix and a loop on the surface of EstA (PDB 5AH1) (released N-terminal part in red; ΔEstA in blue, cleavage site in orange, catalytic triad of the active site in yellow sticks) (d).