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Arylamine N ‐acetyltransferases: a structural perspective
Author(s) -
Zhou Xiaotong,
Ma Zhiguo,
Dong Dong,
Wu Baojian
Publication year - 2013
Publication title -
british journal of pharmacology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.432
H-Index - 211
eISSN - 1476-5381
pISSN - 0007-1188
DOI - 10.1111/bph.12182
Subject(s) - acetyltransferases , nat , arylamine n acetyltransferase , acetyltransferase , enzyme , chemical biology , acetylation , biochemistry , computational biology , biology , histone acetyltransferases , active site , cancer , chemistry , genetics , gene , computer science , computer network
Arylamine N ‐acetyltransferase ( NAT ) plays an important role in metabolism and detoxification of many compounds including drugs and environmental carcinogens through chemical modification of the amine group with an acetyl group. Recent studies have suggested that NATs are also involved in cancer cell growth and inhibition of the enzymes may be a potential target for cancer chemotherapy. Three‐dimensional (3 D ) structures are available for NATs from both prokaryotes and eukaryotes. These structures provide valuable insights into the acetylation mechanism, features of the active site and the structural determinants that govern substrate/inhibitor‐binding specificity. Such insights allow a more precise understanding of the structure–activity relationships for NAT substrates and inhibitors. Furthermore, the structural elucidation of NATs has generated powerful tools in the design of small molecule inhibitors that should alleviate cancer, based on the important role of the enzyme in cancer biology.