New Insight into the Interactions of Arbutin with Mushroom Tyrosinase.

Autor: Ghofrani NS; National Institute for Genetic Engineering and Biotechnology, P.O. Box: 14965/161, Tehran, Iran., Sheikhi M; National Institute for Genetic Engineering and Biotechnology, P.O. Box: 14965/161, Tehran, Iran., Amirzakaria JZ; National Institute for Genetic Engineering and Biotechnology, P.O. Box: 14965/161, Tehran, Iran., Hassani S; National Institute for Genetic Engineering and Biotechnology, P.O. Box: 14965/161, Tehran, Iran., Aminzadeh S; National Institute for Genetic Engineering and Biotechnology, P.O. Box: 14965/161, Tehran, Iran., Haghbeen K; National Institute for Genetic Engineering and Biotechnology, P.O. Box: 14965/161, Tehran, Iran. Kamahl@nigeb.ac.ir.
Jazyk: angličtina
Zdroj: The protein journal [Protein J] 2021 Oct; Vol. 40 (5), pp. 689-698. Date of Electronic Publication: 2021 May 28.
DOI: 10.1007/s10930-021-10004-x
Abstrakt: As a safe substitute for hydroquinone, β-arbutin, a natural plant substance, and its synthetic counterpart, α-arbutin, are used in depigmentation formulations. However, there are debatable points regarding the impact of arbutin on tyrosinase and the pigmentation process. To shed light on this issue, the effects of Pyrus biossieriana leaves extract (PbLE) and β-arbutin, extracted from PbLE, on mushroom tyrosinase (MT) were comprehensively examined. The study was focused on cresolase activity as the characteristic reaction of a tyrosinase. Kinetics studies disclosed that β-arbutin can modulate MT monophenolase activity from inhibition to activation or vice versa. β-Arbutin inhibited L-tyrosine (LTy) oxidation at concentrations < 0.3 mM but it increased (more than 400%) the enzymatic oxidation of L-tyrosine at the concentrations > 0.3 mM. An opposite pattern (activation then inhibition) was observed when a synthetic substrate was used instead of LTy. Computational studies, focused on the heavy chain of MT, indicated that β-arbutin effect could be overruled by the enzyme's ability to provide the ligand with a non-specific binding site (MTPc). A plausible mechanism was presented to show the influence of MTPc on the substrate pose in the active site. The possible determinant correlation between the findings of this research and the current studies on human tyrosinase role in the pigmentation process has been presented.
(© 2021. The Author(s), under exclusive licence to Springer Science+Business Media, LLC, part of Springer Nature.)
Databáze: MEDLINE
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