Mechanistic and Structural Analysis of a Drosophila melanogaster Enzyme, Arylalkylamine N-Acetyltransferase Like 7, an Enzyme That Catalyzes the Formation of N-Acetylarylalkylamides and N-Acetylhistamine.

@article{Dempsey2015MechanisticAS,
  title={Mechanistic and Structural Analysis of a Drosophila melanogaster Enzyme, Arylalkylamine N-Acetyltransferase Like 7, an Enzyme That Catalyzes the Formation of N-Acetylarylalkylamides and N-Acetylhistamine.},
  author={Daniel R. Dempsey and K. A. Jeffries and S. Handa and Anne-Marie Carpenter and Santiago Rodriguez-Ospina and L. Breydo and D. Merkler},
  journal={Biochemistry},
  year={2015},
  volume={54 16},
  pages={
          2644-58
        }
}
Arylalkylamine N-acetyltransferase like 7 (AANATL7) catalyzes the formation of N-acetylarylalkylamides and N-acetylhistamine from acetyl-CoA and the corresponding amine substrate. AANATL7 is a member of the GNAT superfamily of >10000 GCN5-related N-acetyltransferases, many members being linked to important roles in both human metabolism and disease. Drosophila melanogaster utilizes the N-acetylation of biogenic amines for the inactivation of neurotransmitters, the biosynthesis of melatonin, and… Expand
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A combination of pH–activity profiling and site-directed mutagenesis to study prospective residues believed to function in AANATA catalysis led to an assignment of Glu-47 as the general base in catalysis with an apparent pKa of 7.0. Expand
Purification, cloning, and characterization of a second arylalkylamine N-acetyltransferase from Drosophila melanogaster.
TLDR
These findings demonstrate the presence of a second expressed gene encoding an AANAT in D. melanogaster, and reveal no diurnal variation of aaNAT2 transcription, similar to the results obtained for aa NAT1a and aa NATO1b. Expand
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