Literature DB >> 24853564

Tyrosinase inhibitors from terrestrial and marine resources.

Bin Wu1.   

Abstract

Tyrosinase is a multifunctional copper-containing enzyme widely distributed in plants and animals, which catalyzes both the hydroxylation of tyrosine into o-diphenols and the oxidation of o-diphenols into o-quinones. Tyrosinase is known to be a key enzyme for melanin biosynthesis in plants and animals. Tyrosinase inhibitors, therefore, can be clinically useful for the treatment of some dermatological disorders associated with melanin hyperpigmentation. They also find uses in cosmetics for whitening and depigmentation after sunburn. This review describes 236 compounds obtained from terrestrial and marine plants, animals, microorganisms and macrofungi which have been shown to inhibit tyrosinase. The mechanism of action of tyrosinase, together with the mode of action of inhibitors is described. The relative activities of the different compounds are recorded. The literature on plant-origin inhibitors is extensive, and their chemistry and biological activity have been intensively reviewed. This review will therefore be deliberately cover new classes of inhibitors from terrestrial and marine plants, animals, microorganisms and macrofungi, as well as the traditional classes. The present paper summarizes and discusses the scientific results on the discovery of natural tyrosinase inhibitors.

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Year:  2014        PMID: 24853564     DOI: 10.2174/1568026614666140523115357

Source DB:  PubMed          Journal:  Curr Top Med Chem        ISSN: 1568-0266            Impact factor:   3.295


  3 in total

1.  Tyrosinase and catechol oxidase activity of copper(I) complexes supported by imidazole-based ligands: structure-reactivity correlations.

Authors:  Franziska Wendt; Christian Näther; Felix Tuczek
Journal:  J Biol Inorg Chem       Date:  2016-06-22       Impact factor: 3.358

Review 2.  A comprehensive review on tyrosinase inhibitors.

Authors:  Samaneh Zolghadri; Asieh Bahrami; Mahmud Tareq Hassan Khan; J Munoz-Munoz; F Garcia-Molina; F Garcia-Canovas; Ali Akbar Saboury
Journal:  J Enzyme Inhib Med Chem       Date:  2019-12       Impact factor: 5.051

3.  UV-B-activated B16 melanoma cells or HaCaT keratinocytes accelerate signaling pathways associated with melanogenesis via ANGPTL 2 induction, an activity antagonized by Chrysanthemum extract.

Authors:  Gaku Satou; Daisuke Maji; Takayuki Isamoto; Yuichi Oike; Motoyoshi Endo
Journal:  Exp Dermatol       Date:  2019-01-14       Impact factor: 3.960

  3 in total

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