Abstract
Tuberculosis (TB) kills over two million people every year. We are currently studying a series of known or putative enzyme drug targets from MTB that includes InhA, the NADH‐dependent enoyl‐ACP reductase from the MTB fatty acid biosynthesis (FASII) pathway.InhA is a validated target for drug discovery and we are investigating the interaction with the natural acyl carrier protein substrate (AcpM). Based on studies with the E. coli enoyl reductase homologue, we hypothesized that three basic residues close to the substrate binding loop in InhA, R195, R225, and K233, interact with acidic residues in the AcpM recognition helix. We also have evidence that an additional set of basic residues close to AcpM Helix II, R45, R49, R53, play a critical role in AcpM recognition by InhA. Our studies also have implications for the ability of acyl carrier protein to recognize and interact with a diverse array of intracellular protein targets.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
