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Enzymic activation and transfer of fatty acids as acyl-adenylates in mycobacteria

Author

Listed:
  • Omita A. Trivedi

    (National Institute of Immunology, Aruna Asaf Ali Marg)

  • Pooja Arora

    (National Institute of Immunology, Aruna Asaf Ali Marg)

  • Vijayalakshmi Sridharan

    (National Institute of Immunology, Aruna Asaf Ali Marg)

  • Rashmi Tickoo

    (National Institute of Immunology, Aruna Asaf Ali Marg)

  • Debasisa Mohanty

    (National Institute of Immunology, Aruna Asaf Ali Marg)

  • Rajesh S. Gokhale

    (National Institute of Immunology, Aruna Asaf Ali Marg)

Abstract

The metabolic repertoire in nature is augmented by generating hybrid metabolites from a limited set of gene products1,2,3. In mycobacteria, several unique complex lipids are produced by the combined action of fatty acid synthases and polyketide synthases (PKSs)4,5,6, although it is not clear how the covalently sequestered biosynthetic intermediates are transferred from one enzymatic complex to another. Here we show that some of the 36 annotated fadD genes, located adjacent to the PKS genes in the Mycobacterium tuberculosis genome, constitute a new class of long-chain fatty acyl-AMP ligases (FAALs). These proteins activate long-chain fatty acids as acyl-adenylates, which are then transferred to the multifunctional PKSs for further chain extension. This mode of activation and transfer of fatty acids is contrary to the previously described universal mechanism involving the formation of acyl-coenzyme A thioesters. Similar mechanisms may operate in the biosynthesis of other lipid-containing metabolites and could have implications in engineering novel hybrid products.

Suggested Citation

  • Omita A. Trivedi & Pooja Arora & Vijayalakshmi Sridharan & Rashmi Tickoo & Debasisa Mohanty & Rajesh S. Gokhale, 2004. "Enzymic activation and transfer of fatty acids as acyl-adenylates in mycobacteria," Nature, Nature, vol. 428(6981), pages 441-445, March.
    • Handle: RePEc:nat:nature:v:428:y:2004:i:6981:d:10.1038_nature02384
    DOI: 10.1038/nature02384
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