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Molecular Interaction of Novel Compound 2-Methylheptyl Isonicotinate Produced by Streptomyces sp. 201 with Dihydrodipicolinate Synthase (DHDPS) Enzyme of Mycobacterium tuberculosis for its Antibacterial Activity

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Abstract

Antibiotic resistance is a growing problem in multi-drug-resistant tuberculosis which is caused by Mycobacterium tuberculosis (MTB). Hence there is an urgent need for designing or developing a novel or potent anti-tubercular agent. The Lysine/DAP biosynthetic pathway is a promising target because of its role in cell wall and amino acid biosynthesis. In our study we performed a molecular docking analysis of a novel antibacterial isolated from Streptomyces sp. 201 at three different binding site of dihydrodipicolinate synthase (DHDPS) enzyme of MTB. The molecular docking studies suggest that the novel molecule shows favourable interaction at the three different binding sites as compared to five experimentally known inhibitors of DHDPS.

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Acknowledgments

S.P.S thanks Director, NEIST, Jorhat for providing fellowship. The authors also thank Department of Biotechnology, Govt of India for providing Bioinformatics Infrastructure Facility and CSIR for providing financial support.

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Authors and Affiliations

  1. Bioinformatics Infrastructure Facility, Biotechnology Division, North-East Institute of Science & Technology (CSIR), Jorhat, 785006, Assam, India

    Salam Pradeep Singh, T. C. Bora & R. L. Bezbaruah

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  1. Salam Pradeep Singh
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  2. T. C. Bora
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  3. R. L. Bezbaruah
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Correspondence to Salam Pradeep Singh.

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Singh, S.P., Bora, T.C. & Bezbaruah, R.L. Molecular Interaction of Novel Compound 2-Methylheptyl Isonicotinate Produced by Streptomyces sp. 201 with Dihydrodipicolinate Synthase (DHDPS) Enzyme of Mycobacterium tuberculosis for its Antibacterial Activity. Indian J Microbiol 52, 427–432 (2012). https://doi.org/10.1007/s12088-012-0252-4

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  • DOI: https://doi.org/10.1007/s12088-012-0252-4

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