Molecular interactions in the hydrogen belts of membranes. Glucose-6-phosphatase, lysophosphatidylcholine, and cholesterol.
Microsomal glucose-6-phosphatase from rat liver is activated by phosphatidylcholine but inhibited by lysophosphatidylcholine. Inhibition occurs not by membrane lysis but in an intact bilayer; it is reversible; and it is overcome by addition of cholesterol but not if the cholesterol-hydroxyl group is blocked. An analog of lysophosphatidylcholine deprived of hydrogen bonding sites, 1-ether-2- deoxylysophosphatidylcholine , is a partial activator, and its effect on the enzyme in a phosphatidylcholine bilayer is not modulated by cholesterol. It appears to be one of the functions of cholesterol to buffer the lysophospholipids in membranes by complexing with them through hydrogen bonding in the hydrogen belt region. Lysophosphatidylcholine/cholesterol association is favored over phosphatidylcholine/cholesterol association.
D000818:Animals; D002784:Cholesterol / Q000378:metabolism*; D005952:Glucose-6-Phosphatase / Q000378:metabolism*; D006860:Hydrogen Bonding; D008244:Lysophosphatidylcholines / Q000378:metabolism*; D008563:Membrane Lipids / Q000378:metabolism; D008862:Microsomes, Liver / Q000201:enzymology*; D010713:Phosphatidylcholines / Q000378:metabolism; D051381:Rats; D013329:Structure-Activity Relationship
D008244:Lysophosphatidylcholines; D008563:Membrane Lipids; D010713:Phosphatidylcholines; D002784:Cholesterol; D005952:Glucose-6-Phosphatase