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Xenobiotic‐metabolizing enzymes in Bacillus anthracis : molecular and functional analysis of a truncated arylamine N ‐acetyltransferase isozyme
Author(s) -
Kubiak Xavier,
Duval Romain,
Pluvinage Benjamin,
Chaffotte Alain F,
Dupret JeanMarie,
RodriguesLima Fernando
Publication year - 2017
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.13647
Subject(s) - isozyme , xenobiotic , biology , arylamine n acetyltransferase , biochemistry , enzyme , acetyltransferases , gene , bacillus cereus , genetics , acetylation , bacteria
The arylamine N-acetyltransferases (NATs) are xenobiotic-metabolizing enzymes that play an important role in the detoxification and/or bioactivation of arylamine drugs and xenobiotics. In bacteria, NATs may contribute to the resistance against antibiotics such as isoniazid or sulfamides through their acetylation, which makes this enzyme family a possible drug target. Bacillus anthracis, a bacterial species of clinical significance, expresses three NAT isozymes with distinct structural and enzymatic properties, including an inactive isozyme ((BACAN)NAT3). (BACAN)NAT3 features both a non-canonical Glu residue in its catalytic triad and a truncated C-terminus domain. However, the role these unusual characteristics play in the lack of activity of the (BACAN)NAT3 isozyme remains unclear.