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Beta-Ketoacyl-ACP Synthase I/II from Plasmodium falciparum (PfFabB/F)-Is it B or F?

Sharma, Shilpi and Sharma, Shailendra Kumar and Surolia, Namita and Surolia, Avadhesha (2009) Beta-Ketoacyl-ACP Synthase I/II from Plasmodium falciparum (PfFabB/F)-Is it B or F? In: IUBMB LIFE, 61 (6). pp. 658-662.

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Official URL: http://www3.interscience.wiley.com/journal/1224025...

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/ functions like E. coli FabF as the growth of the mutant cells could 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.

Item Type: Journal Article
Additional Information: Copyright of this article belongs to Taylor and Francis Group.
Keywords: malaria;Plasmodium falciparum;beta-ketoacyl-acyl carrier protein synthase I/II (PfFabB/F);complementation; fatty acids;thermal. modulation; cis-vaccenic acid; mass spectrometry
Department/Centre: Division of Biological Sciences > Molecular Biophysics Unit
Date Deposited: 10 Jul 2009 10:22
Last Modified: 19 Sep 2010 05:35
URI: http://eprints.iisc.ernet.in/id/eprint/21004

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