| Arylamine N-acetyltransferase 2 | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 A 3d cartoon depiction of human N-acetyltransferase 2 | |||||||||
| Identifiers | |||||||||
| EC no. | 2.3.1.5 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
N-acetyltransferase (NAT) is an enzyme that catalyzes the transfer of acetyl groups from acetyl-CoA to arylamines, arylhydroxylamines and arylhydrazines.[1][2][3] They have wide specificity for aromatic amines, particularly serotonin, and can also catalyze acetyl transfer between arylamines without CoA. N-acetyltransferases are cytosolic enzymes found in the liver and many tissues of most mammalian species, except the dog and fox, which cannot acetylate xenobiotics.[4] Acetyl groups are important in the conjugation of metabolites from the liver, to allow excretion of the byproducts (phase II metabolism). This is especially important in the metabolism and excretion of drug products (drug metabolism).
- ^ Evans DA (1989). "N-acetyltransferase". Pharmacology & Therapeutics. 42 (2): 157–234. doi:10.1016/0163-7258(89)90036-3. PMID 2664821.
- ^ Ma Y, Ghoshdastider U, Wang J, Ye W, Dötsch V, Filipek S, Bernhard F, Wang X (2012). "Cell-free expression of human glucosamine 6-phosphate N-acetyltransferase (HsGNA1) for inhibitor screening". Protein Expr. Purif. 86 (2): 120–6. doi:10.1016/j.pep.2012.09.011. PMID 23036358.
- ^ Sim, Edith; Lack, Nathan; Wang, Chan-Ju; et al. (May 2008). "Arylamine N-acetyltransferases: Structural and functional implications of polymorphisms". Toxicology. 254 (3): 170–183. doi:10.1016/j.tox.2008.08.022. PMID 18852012.
- ^ Klaassen, Curtis D. (2008). Casarett and Doull's Toxicology: The Basic Science of Poisons 7th Ed. McGraw-Hill. ISBN 978-0071470513.