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.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Gajiwala KS,Margosiak S,Lu J,Cortez J,Su Y,Nie Z,Appelt K

doi

10.1016/j.febslet.2009.08.001

subject

Has Abstract

pub_date

2009-09-03 00:00:00

pages

2939-46

issue

17

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(09)00614-0

journal_volume

583

pub_type

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