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Crystal structures of bacterial FabH suggest a molecular basis for the substrate specificity of the enzyme
Author(s) -
Gajiwala Ketan S.,
Margosiak Stephen,
Lu Jia,
Cortez Joseph,
Su Ying,
Nie Zhe,
Appelt Krzysztof
Publication year - 2009
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2009.08.001
Subject(s) - acyl carrier protein , enzyme , biochemistry , fatty acid , transferase , bacteria , fatty acid synthase , enterococcus faecalis , biology , staphylococcus aureus , escherichia coli , biosynthesis , microbiology and biotechnology , chemistry , stereochemistry , gene , genetics
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.