Abstract
Tryptophan hydroxylase is the initial and rate-limiting enzyme in the biosynthesis of the neurotransmitter serotonin (5-HT). Knowledge about how the activity of this important brain enzyme is regulated has emerged at a slow rate, primarily as a result of the extreme instability of tryptophan hydroxylase to storage and purification. The present chapter will present some of our past and recent research on tryptophan hydroxylase which has concentrated roughly on two different aspects of the control or determination of its level of activity. First, we have attempted to delineate which factor(s) contribute to the in vitro lability of tryptophan hydroxylase and second, the activation of tryptophan hydroxylase by a calmodulin-dependent phosphorylation reaction has been described.
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Kuhn, D.M. (1981). The regulation of tryptophan hydroxylase activity. In: Usdin, E., Weiner, N., Youdim, M.B.H. (eds) Function and Regulation of Monoamine Enzymes: Basic and Clinical Aspects. Palgrave Macmillan, London. https://doi.org/10.1007/978-1-349-06276-8_20
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DOI: https://doi.org/10.1007/978-1-349-06276-8_20
Publisher Name: Palgrave Macmillan, London
Print ISBN: 978-1-349-06278-2
Online ISBN: 978-1-349-06276-8
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