Functional characterization of β-ketoacyl-ACP reductase (FabG) from Plasmodium falciparum
S Pillai, C Rajagopal, M Kapoor, G Kumar… - Biochemical and …, 2003 - Elsevier
The malaria parasite, Plasmodium falciparum, unlike its human host, utilizes type II fatty acid
synthesis, in which steps of fatty acid biosynthesis are catalyzed by independent enzymes.
Due to this difference, the enzymes of this pathway are a potential target of newer
antimalarials. Here we report the functional characterization of Plasmodium FabG expressed
in Escherichia coli. The purified recombinant FabG from P. falciparum is soluble and active.
The Km of the enzyme for acetoacetyl-CoA was estimated to be 75μM with a Vmax of 0.0054 …
synthesis, in which steps of fatty acid biosynthesis are catalyzed by independent enzymes.
Due to this difference, the enzymes of this pathway are a potential target of newer
antimalarials. Here we report the functional characterization of Plasmodium FabG expressed
in Escherichia coli. The purified recombinant FabG from P. falciparum is soluble and active.
The Km of the enzyme for acetoacetyl-CoA was estimated to be 75μM with a Vmax of 0.0054 …
Functional characterization of β-ketoacyl-ACP reductase (FabG) from Plasmodium falciparum.
SP Smitha Pillai, CR Chitra Rajagopal, MK Mili Kapoor… - 2003 - cabidigitallibrary.org
The malaria parasite, Plasmodium falciparum, unlike its human host, utilizes type II fatty acid
synthesis, in which steps of fatty acid biosynthesis are catalyzed by independent Enzymes.
Due to this difference, the enzymes of this pathway are a potential target of newer
antimalarials. Here we report the functional characterization of Plasmodium FabG expressed
in Escherichia coli. The purified recombinant FabG from P. falciparum is soluble and active.
The K m of the enzyme for acetoacetyl-CoA was estimated to be 75 µM with a V max of …
synthesis, in which steps of fatty acid biosynthesis are catalyzed by independent Enzymes.
Due to this difference, the enzymes of this pathway are a potential target of newer
antimalarials. Here we report the functional characterization of Plasmodium FabG expressed
in Escherichia coli. The purified recombinant FabG from P. falciparum is soluble and active.
The K m of the enzyme for acetoacetyl-CoA was estimated to be 75 µM with a V max of …
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