1995
DOI: 10.1016/0014-5793(95)01198-n
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Isolation and characterization of an arylalkylamine N‐acetyltransferase from Drosophila melanogaster

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. Thi… Show more

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Cited by 48 publications
(34 citation statements)
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“…2, lane B*), consistent with the presence of related genes. During our purification of aaNAT1 based on tryptamine acetylation activity (20), fractions with biphasic enzyme kinetics, separation of two activity peaks on hydroxylapatite columns, and evidence for two additional protein spots after two-dimensional SDS/ PAGE also suggested the presence of additional aaNAT enzymes (data not shown).…”
Section: Resultsmentioning
confidence: 88%
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“…2, lane B*), consistent with the presence of related genes. During our purification of aaNAT1 based on tryptamine acetylation activity (20), fractions with biphasic enzyme kinetics, separation of two activity peaks on hydroxylapatite columns, and evidence for two additional protein spots after two-dimensional SDS/ PAGE also suggested the presence of additional aaNAT enzymes (data not shown).…”
Section: Resultsmentioning
confidence: 88%
“…With the primer combination sp2O/apG, a PCR product was isolated that was 298-bp long and contained the sequences coding for all four internal peptides identified in aaNAT1 (Fig. IA) (20). Surprisingly, this DNA fragment contained no poly(A) tail, presumably due to amplification by only one primer (26).…”
Section: Resultsmentioning
confidence: 99%
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