Abstract
Tryptophan hydroxylase (L-tryptophan 5-monooxygenase, EC 1.14. 16.4), the enzyme catalyzing the rate limiting step in the biosynthesis of serotonin (5-HT) in brain, exhibits several characteristics which strongly suggest that it plays a key role in the in vivo control of 5-HT synthesis. Regulatory properties of tryptophan hydroxylase have been mainly revealed in vitro on the soluble enzyme either in crude extracts (35,000 g supernatant of homogenates) or in semi-purified preparations (Hamon et al., 1977b). Thus, the partial proteolysis of tryptophan hydroxylase by trypsin or by the endogenous Ca2+-dependent neutral proteinase significantly augments its activity (Hamon et al., 1977a). Kinetic analyses have indicated that this activation is associated with marked increases in the Vmax and the affinities of tryptophan hydroxylase for both tryptophan and its pterin cofactor (6-methyl-5,6,7,8-tetrahydropterin, 6-MPH4).
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Mestikawy, S.E., Bourgoin, S., Artaud, F., Hamon, M. (1981). In vitro and in vivo activation of tryptophan hydroxylase in the rat brain. 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_19
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DOI: https://doi.org/10.1007/978-1-349-06276-8_19
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