10.22376/ijpbs.2019.10.1.p1-12 Volume 3 Issue 1 2012 (January - March) Isoniazid, an important drug in the anti-tuberculosis therapy, the enzyme catalase-peroxidase (KatG) plays a key role in activating isoniazid (INH). Mutation in lessThan i greaterThan katG lessThan /i greaterThan gene is a major mechanism of INH resistance in lessThan i greaterThan M. tuberculosis lessThan /i greaterThan . Several derivatives of INH show activity against TB and multi-drug resistant TB. With lessThan sup greaterThan lessThan /sup greaterThan the aim of finding new compounds, in this study, the derivatives of INH were docked directly with wild type and the mutated models of KatG from lessThan i greaterThan M. tuberculosis lessThan /i greaterThan using lessThan i greaterThan in-silico lessThan /i greaterThan approaches. Docking results suggests that compounds-10, 12 and 13 were the high scoring derivatives of INH to bind with mutants of KatG. These models represent the first lessThan i greaterThan in-silico lessThan /i greaterThan evidence for the binding interaction of KatG and its mutants with INH derivatives. The models may provide useful insights for designing new anti-TB agents in order to overcome the resistance developed with INH. A. Nusrath Unissa, Sameer Hassan And N. Selvakumar Mycobacterium tuberculosis, KatG, INH resistance, INH derivatives, Mutants, Docking. 314-326