Kinetics of the inactivation of the protein-lipid complex, firefly luciferase, by sodium deoxycholate and its reactivation by phosphatidylcholine.
Firefly luciferase has been shown to be a protein-lipid complex. Phospholipids and neutral lipids bound to luciferase have been identified. Sodium deoxycholate rapidly inactivated the enzyme, but an excess of phosphatidylcholine recovered luciferase activity. From the kinetics of inactivation and reactivation, a mechanism for interaction of the enzyme with detergents and phospholipids has been proposed. The substrates ATP and Mg2+ stabilized luciferase during delipidation.
Ugarova
N N
NN
Department of Chemistry, Lomonosov Moscow State University, U.S.S.R.
Dukhovich
A F
AF
Shvets
S V
SV
Philippova
N Y
NY
Berezin
I V
IV
D000255:Adenosine Triphosphate / Q000494:pharmacology; D000818:Animals; D001517:Coleoptera / Q000201:enzymology; D003840:Deoxycholic Acid / Q000494:pharmacology*; D004793:Enzyme Reactivators; D007700:Kinetics; D008156:Luciferases / Q000037:antagonists & inhibitors* / Q000378:metabolism; D008274:Magnesium / Q000494:pharmacology; D010713:Phosphatidylcholines / Q000494:pharmacology*
D004793:Enzyme Reactivators; D010713:Phosphatidylcholines; D003840:Deoxycholic Acid; D000255:Adenosine Triphosphate; D008156:Luciferases; D008274:Magnesium