Esterase activity of high-Km aldehyde dehydrogenase from rat liver mitochondria.
Aldehyde dehydrogenase possessing an esterolytic activity has been purified to homogeneity from rat liver mitochondria. Steady-state kinetic studies suggest that the esterolytic reaction follows an ordered uni-bi mechanism. The formation of an acyl enzyme intermediate via nucleophilic catalysis during the esterase reaction is established kinetically using a series of substrates with varying acyl carbon chains and substituted phenyl octanoates with varying electronic effects. The enzyme was reconstituted into phospholipid vesicles. A significant increase in binding capacity is observed when the enzyme is encapsulated into liposomes containing 4% diphosphatidylglycerol.
Senior
D J
DJ
Ottawa-Carleton Chemistry Institute, Carleton University, Ont., Canada.
Tsai
C S
CS
D000444:Aldehyde Dehydrogenase / Q000037:antagonists & inhibitors / Q000302:isolation & purification / Q000378:metabolism*; D000818:Animals; D004339:Drug Compounding; D004950:Esterases / Q000037:antagonists & inhibitors / Q000302:isolation & purification / Q000378:metabolism*; D007700:Kinetics; D008081:Liposomes; D008565:Membrane Proteins / Q000378:metabolism; D008930:Mitochondria, Liver / Q000201:enzymology*; D051381:Rats; D013379:Substrate Specificity
D008081:Liposomes; D008565:Membrane Proteins; D000444:Aldehyde Dehydrogenase; D004950:Esterases