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.
Tyrosinase, tyrosinase inhibitors, terrestrial and marine resource, discovery, plants, animals, microorganisms, macrofungi.
Ocean College, Zhejiang University, Hangzhou 310058, China.