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(Received for publication, June 26, 1996, and in revised form, August 12, 1996)
From the There are two genes, fabA and
fabZ, encoding
Volume 271, Number 44,
Issue of November 1, 1996
pp. 27795-27801
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
-Hydroxyacyl-Acyl Carrier Protein
Dehydratases in Escherichia coli Fatty Acid
Biosynthesis
and§
Department of Biochemistry, St. Jude
Children's Research Hospital, Memphis, Tennessee 38101 and the
§ Department of Biochemistry, University of Tennessee,
Memphis, Tennessee 38163
-hydroxyacyl-acyl carrier protein (ACP)
dehydratases that function in the dissociated, type II fatty acid
synthase system of Escherichia coli. We have investigated
their roles in fatty acid synthesis by purifying the two proteins and
reconstituting cycles of fatty acid synthesis in vitro
using five other purified proteins. FabA and FabZ exhibited broad,
overlapping chain length specificities. The FabZ dehydratase
efficiently catalyzed the dehydration of short chain
-hydroxyacyl-ACPs and long chain saturated and unsaturated
-hydroxyacyl-ACPs. FabA was most active on intermediate chain length
-hydroxyacyl-ACPs and also possessed significant activity toward
both short and long chain saturated -hydroxyacyl-ACPs.
Significantly, FabA was virtually inactive in the dehydration of long
chain unsaturated -hydroxyacyl-ACP. The introduction of the
double bond at the 10-carbon stage of fatty acid synthesis by FabA was
only detected in the presence of -ketoacyl-ACP synthase I (FabB). A
yeast two-hybrid analysis failed to detect an interaction between FabA
and FabB, therefore the channeling of intermediates toward unsaturated
fatty acid synthesis by FabB was attributed to the affinity of the
condensing enzyme for cis-decenoyl-ACP. The broad substrate
specificity of FabZ coupled with the inactivity of FabA toward a long
chain unsaturated -hydroxyacyl-ACP provides a biochemical
explanation for the phenotypes of cells with genetically altered levels
of the two dehydratases.
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