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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