Abstract
The recent upsurge of life-threatening multidrug- and extreme drug- resistant tuberculosis along with HIV co-infection urge the need of new drug targets and drugs to cripple the survival and infection of Mycobacterium tuberculosis. The current scenario of tuberculosis might be dealt by targeting pathogen’s enzymes that participate in both cell wall and lipid metabolism.
Highlights
The recent upsurge of life-threatening multidrug- and extreme drug- resistant tuberculosis along with HIV co-infection urge the need of new drug targets and drugs to cripple the survival and infection of Mycobacterium tuberculosis [1,2,3,4,5]
The current scenario of tuberculosis might be dealt by targeting pathogen’s enzymes that participate in both cell wall and lipid metabolism [6,7,8]
Ala300 which might be involved in substrate binding and recognition
Summary
Ala300 which might be involved in substrate binding and recognition. The comparison of Rv3802c model with human MGL [PDB Id: 3HJU, chain A] and cutinases [PDB id: 1CEX, chain A] identified Thr and Gln176 as the putative oxyanion hole residues which might be involved in the substrate binding and in stabilizing the tetrahedral intermediate for catalysis. Recent research effort revealed that tetrahydrolipstatin, a human lipase inhibitor binds irreversibly to both MSMEG_6394 and Rv3802c and exhibting antitubercular activity [10,11]. All these evidences point to the suitability of Rv3802c as promising drug target
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