The Escherichia coli Gene Encoding the UDP-2,3-diacylglucosamine Pyrophosphatase of Lipid A Biosynthesis *
Journal of Biological Chemistry, ISSN: 0021-9258, Vol: 277, Issue: 29, Page: 25937-25946
2002
- 69Citations
- 68Captures
- 1Mentions
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Metrics Details
- Citations69
- Citation Indexes69
- 69
- CrossRef50
- Captures68
- Readers68
- 68
- Mentions1
- References1
- 1
Article Description
UDP-2,3-diacylglucosamine hydrolase is believed to catalyze the fourth step of lipid A biosynthesis in Escherichia coli. This reaction involves pyrophosphate bond hydrolysis of the precursor UDP-2,3-diacylglucosamine to yield 2,3-diacylglucosamine 1-phosphate and UMP. To identify the gene encoding this hydrolase, E. coli lysates generated with individual λ clones of the ordered Kohara library were assayed for overexpression of the enzyme. The sequence of λ clone 157[6E7], promoting overproduction of hydrolase activity, was examined for genes encoding hypothetical proteins of unknown function. The amino acid sequence of one such open reading frame, ybbF, is 50.5% identical to a Haemophilus influenzae hypothetical protein and is also conserved in most other Gram-negative organisms, but is absent in Gram-positives. Cell extracts prepared from cells overexpressing ybbF behind the T7 lac promoter have ∼540 times more hydrolase activity than cells with vector alone. YbbF was purified to ∼60% homogeneity, and its catalytic properties were examined. Enzymatic activity is maximal at pH 8 and is inhibited by 0.01% (or more) Triton X-100. The apparent K m for UDP-2,3-diacylglucosamine is 62 μ m. YbbF requires a diacylated substrate and does not cleave CDP-diacylglycerol. 31 P NMR studies of the UMP product generated from UDP-2,3-diacylglucosamine in the presence of 40% H 2 18 0 show that the enzyme attacks the α-phosphate group of the UDP moiety. Because ybbF encodes the specific UDP-2,3-diacylglucosamine hydrolase involved in lipid A biosynthesis, it is now designated lpxH.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/S0021925819663271; http://dx.doi.org/10.1074/jbc.m204067200; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=0037135537&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/12000770; http://www.jbc.org/lookup/doi/10.1074/jbc.M204067200; https://syndication.highwire.org/content/doi/10.1074/jbc.M204067200; https://linkinghub.elsevier.com/retrieve/pii/S0021925819663271; https://dx.doi.org/10.1074/jbc.m204067200
American Society for Biochemistry & Molecular Biology (ASBMB)
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