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

Comp Biochem Physiol B Biochem Mol Biol. 2007 Jul;147(3):358-66. doi: 10.1016/j.cbpb.2006.10.112. Epub 2007 Feb 7.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Arylalkylamine N-Acetyltransferase / biosynthesis
  • Arylalkylamine N-Acetyltransferase / chemistry*
  • Arylalkylamine N-Acetyltransferase / genetics*
  • Baculoviridae
  • Base Sequence
  • Bombyx / enzymology*
  • Bombyx / genetics*
  • Cloning, Molecular
  • DNA, Complementary / genetics
  • Gene Expression
  • Insect Proteins / biosynthesis
  • Insect Proteins / chemistry*
  • Insect Proteins / genetics*
  • Molecular Sequence Data
  • Recombinant Proteins / biosynthesis
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / genetics
  • Substrate Specificity

Substances

  • DNA, Complementary
  • Insect Proteins
  • Recombinant Proteins
  • Arylalkylamine N-Acetyltransferase