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Article

Investigation of the role of a second conserved serine in carboxylesterases via site-directed mutagenesis.

Archives of biochemistry and biophysics - 15 Oct 2004

Stok Jeanette E, Goloshchapov Andrey, Song Cheng, Wheelock Craig E, Derbel Maher B H, Morisseau Christophe, Hammock Bruce D

Abstract excerpt

Carboxylesterases are enzymes that catalyze the hydrolysis of ester and amide moieties. These enzymes have an active site that is composed of a nucleophile (Ser), a base (His), and an acid (Glu) that is commonly known as a catalytic triad. It has previously been observed that the majority of carboxylesterases and lipases contain a second conserved serine in their active site [Proteins, 34 (1999) 184]. To...

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Identifiers

PMID: 15369824
DOI: 10.1016/j.abb.2004.06.020

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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