Crystal structures of bacterial FabH suggest a molecular basis for the substrate specificity of the enzyme |
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Authors: | Ketan S Gajiwala Joseph Cortez Zhe Nie |
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Institution: | Quorex Pharmaceuticals, 1890 Rutherford Road, #200 Carlsbad, CA 92008, United States |
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Abstract: | FabH (β-ketoacyl-acyl carrier protein synthase III) is unique in that it initiates fatty acid biosynthesis, is inhibited by long-chain fatty acids providing means for feedback control of the process, and dictates the fatty acid profile of the organism by virtue of its substrate specificity. We report the crystal structures of bacterial FabH enzymes from four different pathogenic species: Enterococcus faecalis, Haemophilus influenzae, Staphylococcus aureus and Escherichia coli. Structural data on the enzyme from different species show important differences in the architecture of the substrate-binding sites that parallel the inter-species diversity in the substrate specificities of these enzymes. |
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Keywords: | FabH Fatty acid biosynthesis Substrate specificity Protein structure Enzyme inhibition |
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