Functional role of catalytic triad and oxyanion hole-forming residues on enzyme activity of Escherichia coli thioesterase I/protease I/phospholipase L1

The Biochemical Journal
Li-Chiun LeeJei-Fu Shaw

Abstract

Escherichia coli TAP (thioesterase I, EC 3.1.2.2) is a multifunctional enzyme with thioesterase, esterase, arylesterase, protease and lysophospholipase activities. Previous crystal structural analyses identified its essential amino acid residues as those that form a catalytic triad (Ser10-Asp154-His157) and those involved in forming an oxyanion hole (Ser10-Gly44-Asn73). To gain an insight into the biochemical roles of each residue, site-directed mutagenesis was employed to mutate these residues to alanine, and enzyme kinetic studies were conducted using esterase, thioesterase and amino-acid-derived substrates. Of the residues, His157 is the most important, as it plays a vital role in the catalytic triad, and may also play a role in stabilizing oxyanion conformation. Ser10 also plays a very important role, although the small residual activity of the S10A variant suggests that a water molecule may act as a poor substitute. The water molecule could possibly be endowed with the nucleophilic-attacking character by His157 hydrogen-bonding. Asp154 is not as essential compared with the other two residues in the triad. It is close to the entrance of the substrate tunnel, therefore it predominantly affects substrate accessibility. Gly44 ...Continue Reading

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Citations

Feb 7, 2012·Applied and Environmental Microbiology·Toon NicolayStijn Spaepen
Oct 28, 2014·Frontiers in Microbiology·Trudy Torto-AlaliboBrett M Tyler
Dec 10, 2013·Applied Microbiology and Biotechnology·Steven D Schreck, Amy M Grunden
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Oct 2, 2013·BioResearch Open Access·Ambreen AyubAsma Haque
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Apr 30, 2017·Science·Daniel A DiRoccoIan W Davies
Dec 11, 2020·FEMS Microbiology Letters·Amelia M LijewskiBrett M Barney
Jun 8, 2021·Journal of Basic Microbiology·Junjie QiuChuan Wang
Sep 1, 2008·EcoSal Plus·John E Cronan, Charles O Rock
Jul 3, 2021·Molecules : a Journal of Synthetic Chemistry and Natural Product Chemistry·Ahmed Numan, Matthew Brichacek

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