Abstract
Tyrosine hydroxylase (TH, EC 1.14.16.2) catalyzes the hydroxylation of L-Tyr to L-DOPA, which is the rate limiting reaction in the biosynthesis of catecholamines. The enzyme is mainly expressed in noradrenergic neurons in the brain, in the peripheral sympathetic nervous system, and in chromaffin cells in the adrenal medulla (1). In brain, TH seems to exist in two distinct forms, a soluble and a membrane-bound form (2). The distribution of both forms seems to be region-specific with the soluble form predominating in the substantia nigra and locus coeruleus, while in nerve endings or axons the enzyme seems to be associated to neurotubules and membranes (1). In adrenal chromaffin cells TH is mostly found as a soluble enzyme in the cytoplasm, but considerable evidence has also been presented on its association with membranes of the chromaffin granule (1, 3, 4). Although the physico-chemical basis and physiological significance of the association of TH with membranes is not understood, it has been proposed that binding of TH to the storage secretory granules might play a role in coordinating TH activity and catecholamine release (5).
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Thórólfsson, M., Muga, A., Martinez, A. (2002). The N-Terminus of Human Tyrosine Hydroxylase is Responsible for its Association with Phospholipid Bilayers. In: Milstien, S., Kapatos, G., Levine, R.A., Shane, B. (eds) Chemistry and Biology of Pteridines and Folates. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-0945-5_19
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DOI: https://doi.org/10.1007/978-1-4615-0945-5_19
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