Abstract
Publisher Summary This chapter provides an overview of assays and the properties of tryptophan 5-hydroxylase. The search for an enzymatic system responsible for the formation of 5-hydroxytryptophan (5-HTP)—the direct precursor of 5-hydroxytryptamine (5-HT)—was first directed toward a microorganism called Chromobaoterium violaeeum. It was because chemical analysis of violacein—a purple pigment produced by this organism—had revealed the existence of a 5-hydroxyindole moiety. Hydroxylation of tryptophan in a cell-free system was reported in mammalian intestinal mucosa. The assay of brain tryptophan hydroxylase requires a radioisotopic method. Several rapid and sensitive assays for brain tryptophan hydroxylase are now available that have partially unraveled several intriguing properties of tryptophan 5-hydroxylase. The complexity of the regulation of hepatic phenylalanine hydroxylase—another enzyme using tetrahydrobiopterin as an electron donor source—illustrates and provides a model to pursue the purification of tryptophan hydroxylase to elucidate its regulatory properties.
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