Release of anchored membrane enzymes by lipoamidase.
Lipoamidase is found to be able to release various membrane-anchored enzymes from the membrane compartment of pig brain. Released enzymes revealed their intact enzyme activities in the soluble fraction. Lipoamidase could release at least two types of anchored enzymes, i.e. glycosyl-phosphatidylinositol-bonded and myristoylated enzymes, but not integral membrane bound enzymes. The reaction was competitively inhibited by lipoyllysine. This releasing mechanism found in the membranes may play important roles in the secretory mechanism of extracellular enzymes and also in the cellular signal-transduction system through topological changes in cellular enzymes.
Oizumi
J
J
Division of Metabolism, National Children's Medical Research Center, Tokyo, Japan.
Hayakawa
K
K
D000577:Amides; D000581:Amidohydrolases / Q000494:pharmacology*; D000818:Animals; D002462:Cell Membrane / Q000187:drug effects* / Q000201:enzymology; D004952:Esters; D006868:Hydrolysis; D008239:Lysine / Q000031:analogs & derivatives / Q000494:pharmacology; D008565:Membrane Proteins / Q000378:metabolism*; D019814:Myristic Acid; D009227:Myristic Acids; D019308:Palmitic Acid; D010169:Palmitic Acids; D013552:Swine; D008063:Thioctic Acid / Q000031:analogs & derivatives / Q000494:pharmacology
D000577:Amides; D004952:Esters; D008565:Membrane Proteins; D009227:Myristic Acids; D010169:Palmitic Acids; D019814:Myristic Acid; C067769:lipoyllysine; D019308:Palmitic Acid; D008063:Thioctic Acid; D000581:Amidohydrolases; C023940:lipoamidase; D008239:Lysine