کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
1977362 1061484 2013 10 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Characterization of arylalkylamine N-acetyltransferase from silkmoth (Antheraea pernyi) and pesticidal drug design based on the baculovirus-expressed enzyme
موضوعات مرتبط
علوم زیستی و بیوفناوری بیوشیمی، ژنتیک و زیست شناسی مولکولی زیست شیمی
پیش نمایش صفحه اول مقاله
Characterization of arylalkylamine N-acetyltransferase from silkmoth (Antheraea pernyi) and pesticidal drug design based on the baculovirus-expressed enzyme
چکیده انگلیسی

Arylalkylamine N-acetyltransferase (AANAT; EC 2.3.1.87) catalyzes the N-acetylation of arylalkylamines. A cDNA encoding AANAT (ApAANAT) was cloned from Antheraea pernyi by PCR. The cDNA of 1966 bp encodes a 261 amino acid protein. The amino acid sequence was found to have a high homology with Bombyx mori AANAT (BmNAT) but had very low homology with vertebrate AANATs. Amino acid sequence analysis revealed that four insect AANATs cloned from three species including ApAANAT formed a distinct cluster from the vertebrate group. A recombinant ApAANAT protein was expressed in Sf9 cells using a baculovirus expression system, having AANAT activity. The transformed cell extract acetylated tryptamine, serotonin, dopamine, tyramine, octopamine and norepinephrine. The AANAT activity was inhibited at over 0.03 mM tryptamine. Although insect AANATs have been considered as a target of insecticide, this type of insecticide has never been developed. Screening a chemical library of Otsuka Chemical Co., Ltd., we found a novel compound and its derivatives that inhibited the AANAT activity of ApAANAT. This may facilitate investigation of the monoamine metabolic pathway in insects and the development of new types of insecticides and inhibitors of AANATs.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Comparative Biochemistry and Physiology Part C: Toxicology & Pharmacology - Volume 157, Issue 1, January 2013, Pages 93–102
نویسندگان
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