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Article

A double role for a strictly conserved serine: further insights into the dUTPase catalytic mechanism.

Biochemistry - 29 Jul 2008

Palmén Lorena González, Becker Kristian, Bülow Leif, Kvassman Jan-Olov

Abstract excerpt

Ser72 at the active site of the Escherichia coli dUTPase has been mutated to an alanine, and the properties of the mutant have been investigated. The serine is absolutely conserved among the monomeric and trimeric dUTPases (including the bifunctional dCTP deaminase:dUTPases), and it has been proposed to promote catalysis by balancing negative charge at the oxygen that bridges the alpha- and beta-phosphorus of the...

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PMID: 18597482
DOI: 10.1021/bi800325j

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

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