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.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Gajiwala KS,Margosiak S,Lu J,Cortez J,Su Y,Nie Z,Appelt Kdoi
10.1016/j.febslet.2009.08.001subject
Has Abstractpub_date
2009-09-03 00:00:00pages
2939-46issue
17eissn
0014-5793issn
1873-3468pii
S0014-5793(09)00614-0journal_volume
583pub_type
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