Characterization of the Mycobacterial Acyl-CoA Carboxylase Holo Complexes Reveals Their Functional Expansion into Amino Acid Catabolism

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Tuberculosis is deadly human disease caused by infection with the bacterium Mycobacterium tuberculosis. This pathogen has a complex metabolism with many genes required for the synthesis of components of its unique cell envelope. We have investigated a family of closely related genes coding for different acyl CoA carboxylase enzyme complexes with previously unexplained genetic redundancy that have been thought to have an involvement in the synthesis of these cell envelope components. We identified five functional multienzyme complexes. Of the two complexes with hitherto unknown function we chose to investigate, one specifically and to our surprise it is required for the degradation of the amino acid leucine. To our knowledge this is the first demonstration that mycobacteria have a specific pathway for leucine degradation and thus broaden the functional diversity associated with acyl CoA carboxylase coding genes.

Vyšlo v časopise: Characterization of the Mycobacterial Acyl-CoA Carboxylase Holo Complexes Reveals Their Functional Expansion into Amino Acid Catabolism. PLoS Pathog 11(2): e32767. doi:10.1371/journal.ppat.1004623
Kategorie: Research Article
prolekare.web.journal.doi_sk: https://doi.org/10.1371/journal.ppat.1004623

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