Mycobacterium tuberculosis Arylamine N-Acetyltransferase Acetylates and Thus Inactivates para-Aminosalicylic Acid

被引：7

作者：

Wang, Xude ^{[1
,2
]}

Yang, Shanshan ^{[1
]}

Gu, Jing ^{[1
]}

Deng, Jiaoyu ^{[1
]}

机构：

[1] Chinese Acad Sci, Wuhan Inst Virol, Key Lab Agr & Environm Microbiol, Wuhan, Peoples R China

[2] Foshan Univ, Sch Stomatol & Med, Foshan, Peoples R China

来源：

ANTIMICROBIAL AGENTS AND CHEMOTHERAPY | 2016年 / 60卷 / 12期

基金：

中国国家自然科学基金;

关键词：

CHROMOSOMAL LOCALIZATION; PSEUDOMONAS-AERUGINOSA; ISONIAZID METABOLISM; EXPRESSION; GENES; PHARMACOGENETICS; POLYMORPHISMS; SUBSTRATE; SMEGMATIS; MECHANISM;

D O I：

10.1128/AAC.01312-16

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

Mycobacterium tuberculosis arylamine N-acetyltransferase (TBNAT) is able to acetylate para-aminosalicylic acid (PAS) both in vitro and in vivo as determined by high-performance liquid chromatography (HPLC) and electrospray ionization-mass spectrometry (ESI-MS) techniques. The antituberculosis activity of the acetylated PAS is significantly reduced. As a result, overexpression of TBNAT in M. tuberculosis results in PAS resistance, as determined by MIC tests and drug exposure experiments. Taken together, our results suggest that TBNAT from M. tuberculosis is able to inactivate PAS by acetylating the compound.

引用

页码：7505 / 7508

页数：4