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


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2004-03-25

AUTHORS

Omita A. Trivedi, Pooja Arora, Vijayalakshmi Sridharan, Rashmi Tickoo, Debasisa Mohanty, Rajesh S. Gokhale

ABSTRACT

The metabolic repertoire in nature is augmented by generating hybrid metabolites from a limited set of gene products. In mycobacteria, several unique complex lipids are produced by the combined action of fatty acid synthases and polyketide synthases (PKSs), 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. More... »

PAGES

441

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/nature02384

DOI

http://dx.doi.org/10.1038/nature02384

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1003431588

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/15042094


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