Biochemical characterization of an aryl acetic ester hydrolase isolated from human monocytes.
A carboxylic-ester hydrolase was isolated from the leukocytes of a patient with myelomonocytic leukemia. Its relative molecular mass as estimated by sucrose density-gradient sedimentation is about 70 000. The purified enzyme is specific for acetyl esters of aromatic alcohols. It is inhibited by fluoride, but insensitive to eserine or p-chloromercuriphenylsulfonate. Hydrolysis of 1-naphthyl acetate was optimal above pH 6.0; of o-nitrophenyl acetate, above 8.0. The common catalytic site for the two types of substrates on the enzyme was confirmed by competitive inhibition data.
D000085:Acetates; D002265:Carboxylic Ester Hydrolases / Q000302:isolation & purification / Q000378:metabolism*; D005459:Fluorides / Q000494:pharmacology; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007951:Leukemia, Myeloid / Q000201:enzymology*; D008297:Male; D008875:Middle Aged; D008970:Molecular Weight; D009000:Monocytes / Q000201:enzymology*; D009284:Naphthols / Q000378:metabolism
D000085:Acetates; D009284:Naphthols; D002265:Carboxylic Ester Hydrolases; D005459:Fluorides