Diversity in enoyl-acyl carrier protein reductases |
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Authors: | R. P. Massengo-Tiassé J. E. Cronan |
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Affiliation: | (1) Departments of Microbiology, B103, Chemical and Life Sciences Laboratory, University of Illinois at Urbana-Champaign, 601 S. Goodwin Ave, Urbana, IL 61801, USA;(2) Department of Biochemistry, University of Illinois at Urbana-Champaign, Urbana, IL 61801, USA |
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Abstract: | The enoyl-acyl carrier protein reductase (ENR) is the last enzyme in the fatty acid elongation cycle. Unlike most enzymes in this essential pathway, ENR displays an unusual diversity among organisms. The growing interest in ENRs is mainly due to the fact that a variety of both synthetic and natural antibacterial compounds are shown to specifically target their activity. The primary anti-tuberculosis drug, isoniazid, and the broadly used antibacterial compound, triclosan, both target this enzyme. In this review, we discuss the diversity of ENRs, and their inhibitors in the light of current research progress. Received 3 November 2008; received after revision 5 December 2008; accepted 8 December 2008 |
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Keywords: | KeywordHeading" >. Enoyl-acyl carrier protein reductase fatty acid biosynthesis Fatty acid synthesis II triclosan shortchain dehydrogenase reductase medium-chain dehydrogenase reductase |
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