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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Activation of cyclic nucleotide phosphodiesterase by a monosaccharide precursor of Escherichia coli lipid A.

The E. coli lipid A precursor lipid X (N2,O3-diacylglucosamine 1-phosphate) activates calmodulin-dependent cyclic nucleotide phosphodiesterase in a noncooperative, calcium-independent manner by increasing its Vmax and decreasing its Km for substrate. The glycolipid produces half-maximal activation at 11 micrograms/ml and does not further enhance activation by calcium-calmodulin. Lipid X activation of phosphodiesterase requires the presence of the O3-linked hydroxymyristoyl residue. These findings suggest that lipid X could produce some of its biological effects by modulating intracellular cAMP levels.[1]

References

  1. Activation of cyclic nucleotide phosphodiesterase by a monosaccharide precursor of Escherichia coli lipid A. Walters, J.D., Jirsa, R.C. FEBS Lett. (1988) [Pubmed]
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