The American Cancer Society estimates that skin cancer is the most prevalent of all cancers with over 2 million cases of non-melanoma skin cancer each year and 75,000 melanoma cases in 2012**. Melanoma is one of themost serious consequences of skin cancer where melanocytesproliferate actively with enhanced accumulation of melaninpigment leading to hyperpigmentation and tumor formation. Up-regulated levels oftyrosinase enzyme appear to be correlated to with greater production and accumulation of melanin which induces skin cancer.
Tyrosinase (EC 1.14.18.1) is an oxygen oxidoreductase enzyme involved in vertebrate cutaneous pigmentation, browning of fruits and vegetables, and morphogenesis and fruiting body formation in fungi. It catalyzses the o-hydroxylation of monophenols and aerobic oxidation of o-diphenols to o-quinones, leading to the …show more content…
Tyrosinase is found virtually every organism commonly found as tetramer made up of two heavy and two light subunits. The heavy subunit containing the active site contains a conserved pair of copper-binding sites referred to as Cu(A) and Cu(B) which are coordinately bonded to a distinct set of 3 histidine residues His87, His108, His117 and His239, His243, His273 respectively. The identified tyro isoezymes α, β, γ, and δ, have different amino acid sequences but the same binuclear three copper center. Tyrosinase can exist latent state known as zymogen and can be activated by a curtain treatment or an agent like the detergent Sodium dodecyl sulfate (SDS) at low concentration. Low SDS concentration is found to activate Tyr but high SDS concentration is known to denature the enzyme. Inibitors can bind reversebly or irreversibly depending on the kinetic mechanism, or can block
Tyrosinase (EC 1.14.18.1) is an oxygen oxidoreductase enzyme involved in vertebrate cutaneous pigmentation, browning of fruits and vegetables, and morphogenesis and fruiting body formation in fungi. It catalyzses the o-hydroxylation of monophenols and aerobic oxidation of o-diphenols to o-quinones, leading to the …show more content…
Tyrosinase is found virtually every organism commonly found as tetramer made up of two heavy and two light subunits. The heavy subunit containing the active site contains a conserved pair of copper-binding sites referred to as Cu(A) and Cu(B) which are coordinately bonded to a distinct set of 3 histidine residues His87, His108, His117 and His239, His243, His273 respectively. The identified tyro isoezymes α, β, γ, and δ, have different amino acid sequences but the same binuclear three copper center. Tyrosinase can exist latent state known as zymogen and can be activated by a curtain treatment or an agent like the detergent Sodium dodecyl sulfate (SDS) at low concentration. Low SDS concentration is found to activate Tyr but high SDS concentration is known to denature the enzyme. Inibitors can bind reversebly or irreversibly depending on the kinetic mechanism, or can block