Serotonin N-acetyltransferase: Mechanism and Inhibition

Authors: Zheng W.; Cole P.A.

Source: Current Medicinal Chemistry, Volume 9, Number 12, June 2002 , pp. 1187-1199(13)

Publisher: Bentham Science Publishers

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Abstract:

Serotonin N-acetyltransferase (arylalkylamine N-acetyltransferase, AANAT) catalyzes the rate-limiting step in the biosynthesis of the circadian hormone melatonin from serotonin. Although melatonin was identified 40 years ago, relatively little is known about its (patho)physiological roles, and a solid scientific foundation is still lacking for most therapeutic applications currently claimed for melatonin. The development of potent, specific, and cell permeable inhibitors for AANAT should constitute an important strategy to address these issues. These inhibitors are also potential therapeutics for various sleep / mood disorders. This review will focus on the efforts toward developing in vitro and in vivo AANAT inhibitors, including basic mechanistic studies on AANAT, which have played an important role in design.

Keywords: aanat; serotonin n-acefyltransferase; sleep disorder; mood disorder; aanat inhibitor

Language: English

Document Type: Review article

DOI: http://dx.doi.org/10.2174/0929867023370013

Publication date: 2002-06-01

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Current Medicinal Chemistry covers all the latest and outstanding developments in medicinal chemistry and rational drug design. Each issue contains a series of timely in-depth reviews written by leaders in the field covering a range of the current topics in medicinal chemistry. Current Medicinal Chemistry is an essential journal for every medicinal chemist who wishes to be kept informed and up-to-date with the latest and most important developments.