Microbial Tyrosinase: Biochemical, Molecular Properties and Pharmaceutical Applications

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.

Reductase-catalyzed tetrahydrobiopterin regeneration alleviates the anti-competitive inhibition of tyrosine hydroxylation by 7,8-dihydrobiopterin

l-Tyrosine hydroxylation by tyrosine hydroxylase is a significant reaction for preparing many nutraceutical and pharmaceutical chemicals.

Expression of the Tyrosine Hydroxylase Gene from Rat Leads to Oxidative Stress in Potato Plants

Catecholamines are biogenic aromatic amines common among both animals and plants. In animals, they are synthesized via tyrosine hydroxylation, while both hydroxylation or decarboxylation of tyrosine are possible in plants, depending on the species, though no tyrosine hydroxylase—a counterpart of the animal enzyme—has been identified yet. It is known that in potato plants, it is the decarboxylation of tyrosine that leads to catecholamine production. In this paper, we present the effects of the induction of an alternative route of catecholamine production by introducing the tyrosine hydroxylase gene from rat. We demonstrate that an animal system can be used by the plant. However, it does not function to synthesize catecholamines. Instead, it leads to elevated reactive oxygen species content and a constant stress condition in the plant, which responds with elevated antioxidant levels and improved resistance to infection.

Expression of tyrosine hydroxylase gene from rat leads to oxidative stress in potato plants

Catecholamines are biogenic aromatic amines common among both animals and plants. In animals they are synthesized via tyrosine hydroxylation, while in plants, both hydroxylation or decarboxylation of tyrosine are possible, depending on the species, though no tyrosine hydroxylase – a counterpart of animal enzyme has been identified yet. It is known that in potato plants it is the decarboxylation of tyrosine that leads to catecholamine production. In this paper we present the effects of induction of an alternative route of catecholamine production by introducing tyrosine hydroxylase gene from rat. We demonstrate that an animal system can be used by the plant, however, it does not function to synthesize catecholamines. Instead it leads to elevated reactive oxygen species content and constant stress condition to the plant which responds with elevated antioxidant level and further with improved resistance to infection.One sentence summaryIntroduction of rat tyrosine hydroxylase gene to potato disturbs catecholamine synthesis, causes oxidative stress and activates antioxidant response.