Tuberculosis (TB) is one of the worlds deadliest diseases, causing over 2.5-3 million deaths per year. The causative agent of tuberculosis, Mycobacterium tuberculosis, is especially difficult to treat, as it often forms a long-term dormant infection in a patient's lungs. M. tuberculosis acquires energy during dormant infection by degrading host cell lipids for energy, making enzymes involved in lipid metabolism promising drug targets for treating TB. Amongst lipid metabolizing enzymes are 30 different lipases of which the majority are currently uncharacterized. To determine potential inhibitors for TB lipases, we are characterizing the enzymatic activity and substrate specificity of LipW, one of the 30 TB lipases. To do this, we measured the enzymatic activity of two mycobacterial LipW homologues against a library of fluorogenic enzyme substrates. LipW was found to have broad substrate specificity with substrates containing between four and eight carbons.

Characterization of substrate specificity of LipW, a lipase linked to tuberculosis

246th National Meeting (2013)

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