title: Crystal structures of bacterial FabH suggest a molecular basis for the substrate specificity of the enzyme.
abstract: FabH (beta-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.
authors: Quorex Pharmaceuticals, Carlsbad, CA 92008, USA. ketan.gajiwala@pfizer.com
authors: Ketan S
authors: KS
authors: Gajiwala
authors: Stephen
authors: S
authors: Margosiak
authors: Jia
authors: J
authors: Lu
authors: Joseph
authors: J
authors: Cortez
authors: Ying
authors: Y
authors: Su
authors: Zhe
authors: Z
authors: Nie
authors: Krzysztof
authors: K
authors: Appelt
mesh_terms: D015099:3-Oxoacyl-(Acyl-Carrier-Protein) Synthase / Q000737:chemistry* / Q000378:metabolism; D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism; D018360:Crystallography, X-Ray; D013293:Enterococcus faecalis / Q000201:enzymology; D004926:Escherichia coli / Q000201:enzymology; D006193:Haemophilus influenzae / Q000201:enzymology; D008958:Models, Molecular; D008969:Molecular Sequence Data; D015394:Molecular Structure; D016415:Sequence Alignment; D013211:Staphylococcus aureus / Q000201:enzymology; D013379:Substrate Specificity
chemical_list: D001426:Bacterial Proteins; D015099:3-Oxoacyl-(Acyl-Carrier-Protein) Synthase