| Primary Identifier | IPR001447 | Type | Family |
| Short Name | Arylamine_N-AcTrfase |
| description | Arylamine N-acetyltransferase (NAT) facilitates the transfer of an acetyl group from acetyl coenzyme A on to a wide range of arylamine, N-hydroxyarylamines and hydrazines. Acetylation of these compounds generally results in inactivation. NAT is found in many species from Mycobacteria (Mycobacterium tuberculosis, Mycobacterium smegmatis etc) to Homo sapiens (Human). It was the first enzyme to be observed to have polymorphic activity amongst human individuals. NAT is also responsible for the inactivation of Isoniazid (a drug used to treat tuberculosis) in humans [, ]. NAT catalyses the reaction:Acetyl-coA + arylamine = coA + N-acetylarylamineNAT is the target of a common genetic polymorphism of clinical relevance in humans. The N-acetylation polymorphism is determined by low or high NAT activity in liver. NAT has been implicated in the action and toxicity of amine-containing drugs, and in the susceptibility to cancer and systematic lupus erythematosus [, , , ]. Two highly similar human genes for NAT, termed NAT1 and NAT2, encode genetically invariant and variant NAT proteins, respectively. The structure of both proteins is similar to each other and to their prokaryotic orthologues, showing three domains: the N-terminal domain is mostly α-helical, the central domain consists of nine β-strands and the C-terminal has has four anti-parallel β-strands and one α-helix. However, in the human central domain there is a specific insertion []. N-malonyltransferase FDB2 from the fungal fitopathogen Fusarium pseudograminearum also belongs to this family. It is involved in the degradation of benzoxazolinones produced by the host plant [, , ]. |
