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

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 ac...

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Autores principales: Unissa, Ameeruddin Nusrath, Sudha, Subramanian, Selvakumar, Nagamiah, Hassan, Sameer
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Biomedical Informatics 2011
Materias:
Hypothesis
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3218310/
https://www.ncbi.nlm.nih.gov/pubmed/22125378
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author Unissa, Ameeruddin Nusrath
Sudha, Subramanian
Selvakumar, Nagamiah
Hassan, Sameer
author_facet Unissa, Ameeruddin Nusrath
Sudha, Subramanian
Selvakumar, Nagamiah
Hassan, Sameer
author_sort Unissa, Ameeruddin Nusrath
collection PubMed
description 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.
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spelling pubmed-32183102011-11-28 Binding of activated isoniazid with acetyl-CoA carboxylase from Mycobacterium tuberculosis Unissa, Ameeruddin Nusrath Sudha, Subramanian Selvakumar, Nagamiah Hassan, Sameer Bioinformation Hypothesis 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. Biomedical Informatics 2011-09-28 /pmc/articles/PMC3218310/ /pubmed/22125378 Text en © 2011 Biomedical Informatics This is an open-access article, which permits unrestricted use, distribution, and reproduction in any medium, for non-commercial purposes, provided the original author and source are credited.
spellingShingle Hypothesis
Unissa, Ameeruddin Nusrath
Sudha, Subramanian
Selvakumar, Nagamiah
Hassan, Sameer
Binding of activated isoniazid with acetyl-CoA carboxylase from Mycobacterium tuberculosis
title Binding of activated isoniazid with acetyl-CoA carboxylase from Mycobacterium tuberculosis
title_full Binding of activated isoniazid with acetyl-CoA carboxylase from Mycobacterium tuberculosis
title_fullStr Binding of activated isoniazid with acetyl-CoA carboxylase from Mycobacterium tuberculosis
title_full_unstemmed Binding of activated isoniazid with acetyl-CoA carboxylase from Mycobacterium tuberculosis
title_short Binding of activated isoniazid with acetyl-CoA carboxylase from Mycobacterium tuberculosis
title_sort binding of activated isoniazid with acetyl-coa carboxylase from mycobacterium tuberculosis
topic Hypothesis
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3218310/
https://www.ncbi.nlm.nih.gov/pubmed/22125378
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AT selvakumarnagamiah bindingofactivatedisoniazidwithacetylcoacarboxylasefrommycobacteriumtuberculosis
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