The various studies on tyrosinase have recently gained the attention of researchers due to their potential application values and the biological functions. In this study, we predicted the 3D structure of human tyrosinase and simulated the protein-protein interactions between tyrosinase and three binding partners, four and half LIM domains 2 (FHL2), cytochrome b-245 alpha polypeptide (CYBA), and...

Mutations of the tyrosinase gene are one common cause of a similar phenotype in all vertebrates, known as albinism. In an attempt to contribute to an understanding of the genetic hierarchy governing the development of pigmentation, we have used a mouse tyrosinase minigene under the control of its 5.2 kb upstream promoter region to rescue two different albino mutations in the medakafish, Oryzias...

Tyrosinase-related protein 1 (TYRP1) is one of three tyrosinase-like glycoenzymes in human melanocytes that are key to the production of melanin, the compound responsible for the pigmentation of skin, eye, and hair. Difficulties with producing these enzymes in pure form have hampered the understanding of their activity and the effect of mutations that cause albinism and pigmentation disorders. ...

Previous studies from this laboratory have demonstrated the oxidation of certain proteins by tyrosinase (1, 2) and the inactivation of invertase by tyrosinase (3, 4). Different tyrosinase preparations vary greatly in their ability to inactivate invertase; in particular, certain dialyzed or very highly purified tyrosinase solutions seem to have lost their ability to oxidize invertase. In Paper I...

for the first time in the present study the effects of vanillin, vanillyl alcohol, vanillic acid, as well as the newly synthesized vanillin derivative, bis-vanillin, were investigated on the oxidation of dopamine hydrochloride by mushroom tyrosinase. among them, vanillin and bis-vanillin act as activators, while vanillyl alcohol and vanillic acid exhibited inhibitory effects, the ic50 values be...

A resorufin-based highly sensitive and selective fluorescence off-on probe with a new recognition moiety for tyrosinase is developed, and applied to detect and image endogenous tyrosinase activity in different living cells.

The results of the screening of thirty-one species belonging to the lichen family Graphidaceae for their ability to scavenge superoxide and inhibition of tyrosinase and xanthine oxidase activities have been presented. Graphina glaucorufa, Graphina multistriata, Graphina salacinilabiata, Graphis assamensis, Graphis nakanishiana and Phaeographopsis indica showed strong inhibition of tyrosinase an...

Anisic acid (p-methoxybenzoic acid) was characterized as a tyrosinase inhibitor from ani-seed, a common food spice. It inhibited the oxidation of L-3,4-dihydroxyphenylalanine (L-DOPA) catalyzed by tyrosinase with an IC50 of 0.60 mM. The inhibition of tyrosinase by anisic acid is a reversible reaction with residual enzyme activity. This phenolic acid was found to be a classical noncompetitive in...

Enzymatic crosslinking of proteins is often limited by the steric availability of the target residues, as of tyrosyl side chains in the case of tyrosinase. Carrying an N-terminal peptide-tag containing two tyrosine residues, the fluorescent protein C-phycocyanin HisCPC from Synechocystis sp. PCC6803 was crosslinked to fluorescent high-molecular weight forms with tyrosinase. Crosslinking with ty...

Tyrosinase prepared from plant, insect, and marine animal sources catalyzes the oxidation of tyrosine, dihydroxyphenylalanine (dopa), and various structurally similar compounds to darkly colored pigments (2). The enzymatic oxidation of many of the analogues of tyrosine and dopa often proceeds at a faster rate than for tyrosine and dopa themselves (2, 3). The investigation reported here was carr...