Binding of activated isoniazid with acetyl-CoA carboxylase from Mycobacterium tuberculosis

Unissa, A N and Sudha, Subramanian and Selvakumar, N and Hassan, Sameer (2011) Binding of activated isoniazid with acetyl-CoA carboxylase from Mycobacterium tuberculosis. Bioinformation, 7 (3). pp. 107-111. ISSN Print 0973-8894 | Online 0973-2063

Archive 201137.pdf - Published Version Download (238kB)

Abstract

AccD6 (acetyl coenzyme A (CoA) carboxylase), plays an important role in mycolic acid synthesis of Mycobacterium tuberculosis (Mtb). Induced gene expression by isoniazid (isonicotinylhydrazine - INH), anti-tuberculosis drug) shows the expression of accD6. It is our interest to study the binding of activated INH with the AccD6 model using molecular docking procedures. The study predicts a primary binding site for activated INH (isonicotinyl acyl radical) in AccD6 as a potential target.

Affiliation:	ICMR-National Institute for Research in Tuberculosis
Item Type:	Article
Uncontrolled Keywords:	AccD6; INADH; INH; M. tuberculosis; acetyl-CoA; docking; modeling, M. tuberculosis, AccD6, INH, INADH, acetyl-CoA.
Subjects:	Tuberculosis > Laboratory Research > Bacteriological
Divisions:	Basic Science Research > Bacteriology
Depositing User:	Dr. Rathinasabapati R
Date Deposited:	21 Jun 2022 05:42
Last Modified:	21 Jun 2022 05:42
URI:	http://eprints.nirt.res.in/id/eprint/1110

Actions (login required)

View Item