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-phosphatidylinosi...

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Veröffentlicht in:	Molecular and cellular biochemistry 1992-09, Vol.115 (1), p.11-17
Hauptverfasser:	OIZUMI, J, HAYAKAWA, K
Format:	Artikel
Sprache:	eng
Schlagworte:	Amides Amidohydrolases - pharmacology Analytical, structural and metabolic biochemistry Animals Biological and medical sciences Cell Membrane - drug effects Cell Membrane - enzymology Enzymes and enzyme inhibitors Esters Fundamental and applied biological sciences. Psychology Hydrolases Hydrolysis Lysine - analogs & derivatives Lysine - pharmacology Membrane Proteins - metabolism Myristic Acid Myristic Acids Palmitic Acid Palmitic Acids Swine Thioctic Acid - analogs & derivatives Thioctic Acid - pharmacology
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Zusammenfassung:	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.
ISSN:	0300-8177 1573-4919
DOI:	10.1007/BF00229090