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The Mycobacterium Tuberculosis FAS-II Dehydratases and Methyltransferases Define the Specificity of the Mycolic Acid Elongation Complexes

Abstract : Background: The human pathogen Mycobacterium tuberculosis (Mtb) has the originality of possessing a multifunctional mega-enzyme FAS-I (Fatty Acid Synthase-I), together with a multi-protein FAS-II system, to carry out the biosynthesis of common and of specific long chain fatty acids: the mycolic acids (MA). MA are the main constituents of the external mycomembrane that represents a tight permeability barrier involved in the pathogenicity of Mtb. The MA biosynthesis pathway is essential and contains targets for efficient antibiotics. We have demonstrated previously that proteins of FAS-II interact specifically to form specialized and interconnected complexes. This finding suggested that the organization of FAS-II resemble to the architecture of multifunctional mega-enzyme like the mammalian mFAS-I, which is devoted to the fatty acid biosynthesis.
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https://hal.archives-ouvertes.fr/hal-01883511
Contributor : Didier Zerbib Connect in order to contact the contributor
Submitted on : Tuesday, March 23, 2021 - 10:46:54 AM
Last modification on : Wednesday, October 20, 2021 - 3:44:06 AM

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Sylvain Cantaloube, Romain Veyron-Churlet, Nabila Haddache, Mamadou Daffe, Didier Zerbib. The Mycobacterium Tuberculosis FAS-II Dehydratases and Methyltransferases Define the Specificity of the Mycolic Acid Elongation Complexes. PLoS ONE, Public Library of Science, 2011, 6 (12), ⟨10.1371/journal.pone.0029564⟩. ⟨hal-01883511⟩

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