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Activation of cyclic nucleotide phosphodiesterase by a monosaccharide precursor of Escherichia coli lipid A
Author(s) -
Walters John D.,
Jirsa Richard C.
Publication year - 1988
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(88)80044-9
Subject(s) - phosphodiesterase , biochemistry , cyclic nucleotide phosphodiesterase , chemistry , calmodulin , escherichia coli , nucleotide , calcium , cyclic nucleotide , intracellular , residue (chemistry) , substrate (aquarium) , enzyme , biology , gene , organic chemistry , ecology
The E. coli lipid A precursor lipid X ( N 2 , O 3 ‐diacylglucosamine 1‐phosphate) activates calmodulin‐dependent cyclic nucleotide phosphodiesterase in a noncooperative, calcium‐independent manner by increasing its V max and decreasing its K m for substrate. The glycolipid produces half‐maximal activation at 11 μg/ml and does not further enhance activation by calcium‐calmodulin. Lipid X activation of phosphodiesterase requires the presence of the O 3 ‐linked hydroxymyristoyl residue. These findings suggest that lipid X could produce some of its biological effects by modulating intracellular cAMP levels.