Isolation and characterization of an arylalkylamine N-acetyltransferase from Drosophila melanogaster

35Citations
Citations of this article
17Readers
Mendeley users who have this article in their library.

Abstract

The enzyme arylalkylamine N-acetyltransferase (aaNAT) catalyzes the rate-limiting step in melatonin formation in the vertebrate pineal gland. Numerous attempts to purify this highly unstable enzyme from vertebrates have been unsuccessful. Here, we report the purification of an aaNAT enzyme from Drosophila melanogaster, using a radioenzymatic activity assay and column chromatography. The isolated 29.5-kDa protein acetylates tryptamine, dopamine and serotonin with affinities of 0.89 to 0.97 mM, respectively. This suggests that the identified aaNAT may be involved in melatonin synthesis and sclerotization as well as in neurotransmitter catabolism in insects. © 1995.

Cite

CITATION STYLE

APA

Hintermann, E., Jenö, P., & Meyer, U. A. (1995). Isolation and characterization of an arylalkylamine N-acetyltransferase from Drosophila melanogaster. FEBS Letters, 375(1–2), 148–150. https://doi.org/10.1016/0014-5793(95)01198-N

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free