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- W2418506247 abstract "Tyrosine hydroxylase (EC 1.14.16.2) catalyzes the first step in catecholamine biosynthesis, and plays an important role in the regulation of this biosynthetic pathway. Accordingly, there has been a great deal of interest in understanding the control of tyrosine hydroxylase activity. Two major hypotheses for the acute regulation of tyrosine hydroxylase activity have been proposed. Both of these hypotheses are based upon the properties of tyrosine hydroxylase in vitro. First, tyrosine hydroxylase is inhibited by catecholamines in vitro tro (Nagatsu et al., 1964). Tyrosine hydroxylase in intact tissues may normally be restrained by feedback inhibition, and changes in enzyme activity may be produced by changes in the degree of this inhibition (Weiner, 1970). Secondly, tyrosine hydroxylase is a substrate for both cAMP-dependent (Vulliet et al., 1980) and cAMP-independent (Raese et al., 1979) protein kinases in vitro; tyrosine hydroxylase activity is increased by phosphorylation. The activity of tyrosine hydroxylase in vivo may also be regulated by phosphorylation and dephosphorylation.KeywordsTyrosine HydroxylaseCholera ToxinChromaffin CellFeedback InhibitionAdenosine DeaminaseThese keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves." @default.
- W2418506247 created "2016-06-24" @default.
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- W2418506247 date "1981-01-01" @default.
- W2418506247 modified "2023-09-26" @default.
- W2418506247 title "The control of tyrosine hydroxylase activity: enzyme activation versus feedback inhibition" @default.
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- W2418506247 doi "https://doi.org/10.1007/978-1-349-06276-8_5" @default.
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