Multiple drug resistant TB has become common in Mycobacterium tuberculosis infections.  Consequently, new drugs and new drug targets are needed to treat M. tuberculosis infections.  One interesting class of new drug targets is an enzyme family known as lipases, which are essential to the virulence of the bacteria and are used to sustain a persistent infection of TB. M. tuberculosis has a large number of lipases which are used to cleave ester bonds in lipids, including LipF (Rv3487c), a proposed phospholipase whose activity is essential to latent TB infections. To characterize the substrate specificity of LipF, the DNA sequence encoding LipF was isolated from M. tuberculosis genomic DNA and the protein expressed in E. coli, refolded from inclusion bodies, and purified to homogeneity. The enzymatic activity of LipF was then characterized against a library of esterase substrates and the substrate specificity compared to mammalian esterase activity.

Cloning, purification, and enzymatic characterization of LipF (Rv3487c) from <i>Mycobacterium tuberculosis</i>

243rd National Meeting (2012)

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.

Cloning, purification, and enzymatic characterization of LipF (Rv3487c) from Mycobacterium tuberculosis