Microbial Tyrosinase: Biochemical, Molecular Properties and Pharmaceutical Applications
Ashraf S.A. El-Sayed1*
, Hanaa Salah Maamoun1 , Gamal H. Rabie1, Ibrahim Shaker2, Bothaina A. Alaidaroos3, Mostafa G. Ali4 and Amgad M. Rady51Enzymology and Fungal Biotechnology lab, Botany and Microbiology Department, Faculty of Science, Zagazig University, Zagazig, 44519, Egypt
2Limnology Department, Central Laboratory of Aquaculture Research
3Biology Department, Faculty of Science, King Abdulaziz University, Jeddah 21955, Saudi Arabia
4Botany and Microbiology Department, Faculty of Science, Benha University, Benha, 13518, Egypt
5Faculty of Biotechnology, October University for Modern Science and Arts, Cairo 12566, Egypt
Corresponding Author E-mail: ash.elsayed@gmail.com
Abstract: Tyrosinase is a copper-containing monooxygenase involved in thecatalysis of the hydroxylation and oxidation reaction of monophenols and diphenols, respectively, into O-quinones intermediates. Tyrosinase is mainly involved in melanogenesis via two reactions. Firstly, 3,4-dihydroxyphenylalanine is produced through tyrosine hydroxylation the nit oxidized into dopaquinone, and finally gives melanin. However, dopaquinones can results in neuronal damage and cell death through the excessive production, suggesting that tyrosinase may be implanted in the formation human brain’s neuromelanin and association with Parkinson’s diseases. Thus, down regulating the melanin pigments and its intermediates by inhibiting tyrosinase activity is the major pharmaceutical challenge to prevent hyperpigmentation, in addition to therapy of neuromelanin disorders. Thus, this review has been focused on exploring the biochemical and molecular properties of tyrosinase from different sources and its potential inhibition with different natural and synthetic compounds.
Keywords: Anticancer; Biochemical Properties; Inhibitors; Melanin Biosynthesis; Tyrosinase Back to TOC