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- W66454448 endingPage "54" @default.
- W66454448 startingPage "1" @default.
- W66454448 abstract "The enzymes, cholinesterases, esterases, and lipases, catalyze the hydrolysis of carboxyl esters. It has been shown that enzymatic carboxyl ester cleavage is governed by a mechanism, which is similar for different enzymes. Evidence has been derived from studies on the kinetics of the interaction of these enzymes with substrates and inhibitors and specifically from chemical analysis of the active site. The similarity in mechanism might be because of the presence of a common or related active site in different carboxyl esterases. This chapter presents the information on enzymes, their substrates and inhibitors, which contributes to an understanding of the molecular basis of the general mechanism of enzymatic ester hydrolysis. It further presents the data that is relevant for an understanding of the molecular basis of substrate specificities of individual enzymes. Enzymes that hydrolyze choline esters are usually sub-divided into acetyl-, propionyl-, butyryl- or benzoyl-cholinesterases depending on the choline ester that is hydrolyzed at the highest rate. The ability to act on undissolved substrates has been proposed to differentiate lipases from other carboxylesterases like ali-esterases that act only on substrates in solution." @default.
- W66454448 created "2016-06-24" @default.
- W66454448 creator A5077168254 @default.
- W66454448 creator A5080626949 @default.
- W66454448 date "1965-01-01" @default.
- W66454448 modified "2023-09-27" @default.
- W66454448 title "Cholinesterases, Esterases and Lipases" @default.
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