Abstract
The emergence of drug resistant strains of important human pathogens has created an urgent necessity to find new targets and novel antitubercular agents. According to the literature survey, we noticed that enoyl ACP reductase is one of the most promising targets. This enzyme is the most important catalyst for the FAS II synthesis of mycolic acid, which is the most essential component of the mycobacterial cell wall. This review summarizes the progress made in the design of enoyl ACP reductase inhibitors and the role played by 3D-structure of the enzyme in drug design process.
Keywords: Drug design, Enoyl ACP reductase, Enoyl ACP reductase inhibitors, FAS-II.
Mini-Reviews in Medicinal Chemistry
Title:Enoyl ACP Reductase as Effective Target for the Synthesized Novel Antitubercular Drugs: A-State-of-the-Art
Volume: 14 Issue: 8
Author(s): Shrinivas D. Joshi, Sheshagiri R. Dixit, Uttam A. More, Tejraj M. Aminabhavi, Venkatrao H. Kulkarni and Andanappa K. Gadad
Affiliation:
Keywords: Drug design, Enoyl ACP reductase, Enoyl ACP reductase inhibitors, FAS-II.
Abstract: The emergence of drug resistant strains of important human pathogens has created an urgent necessity to find new targets and novel antitubercular agents. According to the literature survey, we noticed that enoyl ACP reductase is one of the most promising targets. This enzyme is the most important catalyst for the FAS II synthesis of mycolic acid, which is the most essential component of the mycobacterial cell wall. This review summarizes the progress made in the design of enoyl ACP reductase inhibitors and the role played by 3D-structure of the enzyme in drug design process.
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Cite this article as:
Joshi D. Shrinivas, Dixit R. Sheshagiri, More A. Uttam, Aminabhavi M. Tejraj, Kulkarni H. Venkatrao and Gadad K. Andanappa, Enoyl ACP Reductase as Effective Target for the Synthesized Novel Antitubercular Drugs: A-State-of-the-Art, Mini-Reviews in Medicinal Chemistry 2014; 14 (8) . https://dx.doi.org/10.2174/1389557514666140820112524
DOI https://dx.doi.org/10.2174/1389557514666140820112524 |
Print ISSN 1389-5575 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5607 |
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