Abstract
Tyrosine hydroxylase catalyzes the rate-limiting step in the biosynthesis of the catecholamine neurotransmitters, the hydroxylation of tyrosine to dihydroxyphenylalanine1. The other substrates for the reaction are molecular oxygen and a tetrahydropterin. In addition, tyrosine hydroxylase requires one atom of ferrous iron per active site for activity2,3; the role of the iron atom is unknown. While the central position of tyrosine hydroxylase in the function of the central nervous system has resulted in a great deal of interest in the enzyme over the years, very little is known about the actual mechanism of catalysis. This report describes recent studies towards elucidating the mechanism of this important monooxygenase.
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© 1993 Springer Science+Business Media New York
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Fitzpatrick, P.F. (1993). Mechanistic Studies of Tyrosine Hydroxylase. In: Ayling, J.E., Nair, M.G., Baugh, C.M. (eds) Chemistry and Biology of Pteridines and Folates. Advances in Experimental Medicine and Biology, vol 338. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-2960-6_16
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DOI: https://doi.org/10.1007/978-1-4615-2960-6_16
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