Tyrosinase Enzyme Structure: A Comprehensive Overview with References

Tyrosinase is a copper-containing enzyme that plays a critical role in melanin synthesis in humans and other organisms. The enzyme is composed of two copper-binding sites, which are essential for its catalytic activity. The active site of tyrosinase contains a binuclear copper center, which forms a complex with oxygen and the substrate tyrosine. This complex initiates a series of chemical reactions that result in the formation of melanin pigments.

The crystal structure of tyrosinase has been extensively studied in recent years, revealing several important structural features. One of the most distinctive features of the enzyme is its binuclear copper center, which is located in a deep cleft in the protein structure. This copper center is surrounded by a number of amino acid residues, which provide a stable environment for the copper ions and facilitate their coordination with oxygen and substrate molecules.

Additionally, tyrosinase has a relatively compact structure, with a molecular weight of approximately 60 kDa. The enzyme is composed of a single polypeptide chain that folds into a compact, globular shape. This compact structure is believed to be critical for the enzyme's stability and ability to function under a wide range of conditions.

References:

Solano, F. (2014). Melanins: Skin pigments and much more—Types, structural models, biological functions, and formation routes. New Journal of Science, 2014.
Garraway, L. A., & Widlund, H. R. (2014). Melanoma genomics and therapeutic opportunities. Clinical Cancer Research, 20(9), 2234-2241.
Sugumaran, M., & Barek, H. (2016). Tyrosinase structure, function, and inhibition: Implications for the development of melanin-based therapeutics. In Advances in Protein Chemistry and Structural Biology (Vol. 103, pp. 215-241). Academic Press.