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Updated: Aug 8, 2025

Preparation and In Vivo Use of an Activity-based Probe for N-acylethanolamine Acid Amidase
Published on: November 23, 2016
Function, structure, evolution, regulation of a potent drug target, arylalkylamine N-acetyltransferase
Lei Zhang1, Yu Tang1, David J Merkler2
1Laboratory of Tropical Veterinary Medicine and Vector Biology, School of Life Sciences, Hainan University, Haikou, Hainan, P.R. China; One Health Institute, Hainan University, Haikou, Hainan, P.R. China.
Abstract:
Arylalkylamine N-acetyltransferase (aaNAT) catalyzes the transacetylation of acetyl coenzyme A to arylamines and arylalkylamines. Based on three-dimensional structural information, aaNAT belongs to the GCN5-related N-acetyltransferases superfamily with a conserved acetyl-CoA binding domain (Dyda et al., 2000). By comparison of sequence similarity, aaNAT is usually divided into vertebrate aaNAT (VT-aaNAT) and non-vertebrate aaNAT (NV-aaNAT) (Cazaméa-Catalan et al., 2014). Insects have evolved multiple aaNATs in comparison to mammals, thus more diverse functions are also reflected in insects. This chapter will summarize previous studies on the function, regulation, structure and evolution of aaNAT, and provide insight into future pest management.
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