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Cloning and characterization of insect arylalkylamine N-acetyltransferase from Bombyx mori.

Comp. Biochem. Physiol. B, Biochem. Mol. Biol.2007 Jul;147(3):358-66. Epub 2007 Feb 07
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摘要


Arylalkylamine N-acetyltransferase (AANAT) catalyzes N-acetylation of arylarkylamines. A cDNA of Bombyx mori insect AANAT (Bm-iAANAT) was found by searching an expressed-sequence tag (EST) database of B. mori (SilkBase). The cDNA encoded a 261 amino acid protein. The mRNA of Bm-iAANAT was expressed in eggs, larvae, adults and various tissues. Recombinant Bm-iAANAT protein was expressed in Sf9 cells by a baculovirus expression system. The AANAT activity of Bm-iAANAT was inhibited by high concentrations (over 0.01 mM) of tryptamine used as a substrate. The Bm-iAANAT acetylated tryptamine, serotonin, dopamine, octopamine, tyramine and norepinephrine. This is the first report of a cloned AANAT that acetylated norepinephrine. These results suggest that Bm-iAANAT is a novel member of insect AANAT family with unique kinetic properties and a broad substrate range.

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