Beta-ketoacyl-ACP synthase I/II from Plasmodium falciparum (PfFabB/F)--is it B or F?

Shilpi Sharma, Shailendra Kumar Sharma, Namita Surolia, Avadhesha Surolia

Index: IUBMB Life 61(6) , 658-62, (2009)

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Abstract

Condensing enzymes play an important and decisive role in terms of fatty acid composition of any organism. They can be classified as condensing enzymes involved in initiating the cycle and enzymes involved in elongating the initiated fatty acyl chain. In E. coli, two isoforms for the elongation condensing enzymes (FabB and FabF) exists whereas Plasmodium genome contains only one isoform. By in vitro complementation studies in E. coli CY244 cells, we show that PfFabB/F functions like E. coli FabF as the growth of the mutant cells could be rescued only in the presence of oleic acid. But unlike bacterial enzyme, PfFabB/F does not increase the cis-vaccenic acid content in the mutant cells upon lowering the growth temperature. This study thus highlights the distinct properties of P. falciparum FabF which sets it apart from E. coli and most other enzymes of this family described so far.(c) 2009 IUBMB.