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Biochem Cell Biol. 1990 Apr;68(4):758-63.

Esterase activity of high-Km aldehyde dehydrogenase from rat liver mitochondria.

Author information

1
Ottawa-Carleton Chemistry Institute, Carleton University, Ont., Canada.

Abstract

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.

PMID:
2223001
DOI:
10.1139/o90-109
[Indexed for MEDLINE]

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