title: Arylamine N-acetyltransferases.
abstract: Arylamine N-acetyltransferases (NATs), known as drug- and carcinogen-metabolising enzymes, have had historic roles in cellular metabolism, carcinogenesis and pharmacogenetics, including epidemiological studies of disease susceptibility. NAT research in the past 5 years builds on that history and additionally paves the way for establishing the following new concepts in biology and opportunities in drug discovery: i) NAT polymorphisms can be used as tools in molecular anthropology to study human evolution; ii) tracing NAT protein synthesis and degradation within cells is providing insight into protein folding in cell biology; iii) studies on control of NAT gene expression may help to understand the increase in the human NAT isoenzyme, NAT1, in breast cancer; iv) a NAT homologue in mycobacteria plays an essential role in cell-wall synthesis and mycobacterial survival inside host macrophage, thus identifying a novel biochemical pathway; v) transgenic mice, with genetic modifications of all Nat genes, provide in vivo tools for drug metabolism; and vi) structures of NAT isoenzymes provide essential in silico tools for drug discovery.
authors.affiliation: University of Oxford, Department of Pharmacology, Mansfield Road, Oxford, UK. edith.sim@pharm.ox.ac.uk
authors.forename: Edith
authors.initials: E
authors.lastname: Sim
authors.forename: Isaac
authors.initials: I
authors.lastname: Westwood
authors.forename: Elizabeth
authors.initials: E
authors.lastname: Fullam
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001191:Arylamine N-Acetyltransferase / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism*; D002384:Catalysis; D019143:Evolution, Molecular; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011110:Polymorphism, Genetic; D017433:Protein Structure, Secondary
chemical_list: D001191:Arylamine N-Acetyltransferase