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J. Biol. Chem., Vol. 261, Issue 14, 6239-6247, May, 1986
JP Walsh and RM Bell
Efficient delivery of hydrophobic water-insoluble substrates and cofactors
to membrane-bound enzymes is a recurring problem which has impeded kinetic
analyses. Kinetic analysis of the Escherichia coli sn- 1,2-diacylglycerol
kinase, an extremely hydrophobic integral membrane protein of 122 residues,
was facilitated by the development of a mixed micellar assay. beta-Octyl
glucoside micelles quantitatively solubilized diacylglycerol kinase from
membranes of strains which overproduced the enzyme up to 250-fold and
provided an effective method to disperse and deliver the hydrophobic
water-insoluble substrate, sn- 1,2-dioleoyglycerol. Diacylglycerol kinase
was active in mixed micelles containing octyl glucoside and
dioleoyglycerol. Several phospholipids stimulated activity up to 6-fold,
suggesting a cofactor function. Activation by phospholipids was not
stereospecific and was mimicked partially by fatty acids. Half-maximal
activation was observed at 1 mol % cardiolipin, suggesting that a small
number of phospholipids are sufficient to activate the enzyme. Activity was
dependent on the mole fractions of dioleoylglycerol and phospholipid in the
mixed micelles, but independent of micelle number. Several lines of
evidence indicated that the transfer of diacylglycerol between micelles was
much more rapid than its utilization by the enzyme. Diacylglycerol kinase
exhibited Michaelis-Menten kinetics with respect to diacylglycerol and
MgATP. A second Mg2+ ion (in addition to MgATP) was required for activity.
When Mg2+ was excluded from the assay, Mn2+, Zn2+, Cd2+, and Co2+ supported
activity to lesser extents. These data establish a suitable system for
in-depth kinetic analysis of the E. coli diacylglycerol kinase and its
phospholipid cofactor requirements.
sn-1,2-Diacylglycerol kinase of Escherichia coli. Mixed micellar analysis of the phospholipid cofactor requirement and divalent cation dependence
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