毒力
水解酶
结核分枝杆菌
微生物学
生物
分枝杆菌
病菌
单元格信封
免疫系统
脂质代谢
细胞内
酶
细胞外
肺结核
生物化学
细菌
遗传学
基因
医学
病理
大肠杆菌
出处
期刊:Current Protein & Peptide Science
[Bentham Science Publishers]
日期:2016-08-04
卷期号:18 (3): 190-210
被引量:29
标识
DOI:10.2174/1389203717666160729093515
摘要
The α/β hydrolase fold superfamily is an ancient and widely diversified group of primarily hydrolytic enzymes. In this review, the adaptations of these proteins to the pathogenic lifestyle of Mycobacterium tuberculosis (Mtb), the causative agent of tuberculosis, are examined. Of the 105 α/β hydrolases identified in Mtb, many are associated with lipid metabolism, particularly in the biosynthesis and maintenance of the Mtb's unique cell envelope, as well in the large number of extracellular lipases that are likely responsible for degradation of host lipid material. α/β hydrolase fold proteins are also involved in the evasion and modulation of the immune response, detoxification and metabolic adaptations, including growth, response to acidification of the intracellular environment and dormancy. A striking feature of Mtb's α/β hydrolases is their diversification into virulence-associated niches. It is clear that the α/β hydrolase fold family has made a significant contribution to Mtb's remarkable success as a pathogen. Keywords: α/β hydrolase fold, esterase, lipase, cholinesterase, Mycobacterium tuberculosis, virulence.
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