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(Received for publication, August 25,
1995; and in revised form, December 1, 1995) The lpcA locus has been identified in Escherichia
coli K12 novobiocin-supersensitive mutants that produce a short
lipopolysaccharide (LPS) core which lacks glyceromannoheptose and
terminal hexoses. We have characterized lpcA as a single gene
mapping around 5.3 min (246 kilobases) on the E. coli K12
chromosome and encoding a 22.6-kDa cytosolic protein. Recombinant
plasmids containing only lpcA restored a complete core LPS in
the E. coli strain
Volume 271,
Number 7,
Issue of February 16, 1996 pp. 3608-3614
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
711. We show that this strain has an
IS5-mediated chromosomal deletion of 35 kilobases that
eliminates lpcA. The LpcA protein showed discrete similarities
with a family of aldose/ketose isomerases and other proteins of unknown
function. The isomerization of sedoheptulose 7-phosphate, into a
phosphosugar presumed to be D-glycero-D-mannoheptose
7-phosphate, was detected in enzyme reactions with cell extracts of E. coli lpcA
and of lpcA mutants
containing the recombinant lpcA gene. We concluded that LpcA
is the phosphoheptose isomerase used in the first step of
glyceromannoheptose synthesis. We also demonstrated that lpcA is conserved among enteric bacteria, all of which contain
glyceromannoheptose in the inner core LPS, indicating that LpcA is an
essential component in a conserved biosynthetic pathway of inner core
LPS.
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