Email the author Insights into the structure and 3D spatial arrangement of the b-ketoacyl carrier protein synthases
Abstract
The b-ketoacyl carrier protein synthases (the KAS enzymes) are key enzymes that can be used as potential anti-Plasmodium drug targets. In bacteria, three KAS enzymes have been identified (KAS I, KAS II and KAS III), whilst in Plasmodium a KAS I/II and KAS III enzyme has been reported. The protein has a total of four active sites, which have been found to be different to each other, rather than four copies of the same active site. The active sites differ not only in the type of interaction they establish with the ligand, but, in the case of Cerulenin as a ligand, the active sites of the KAS I/II enzyme also differ in the number of residues involved in the ligand protein interaction. This is very interesting biochemically, because these differences imply that the affinity of each active site for binding to the ligand might be different as well.
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References
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