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Mutational and structural studies of the diisopropylfluorophosphatase from Loligo vulgaris shed new light on the catalytic mechanism of the enzyme.

Biochemistry - 28 Jun 2005

Katsemi Vicky, Lücke Christian, Koepke Juergen, Löhr Frank, Maurer Steffen, Fritzsch Günter, Rüterjans Heinz

Abstract excerpt

The active site, the substrate binding site, and the metal binding sites of the diisopropylfluorophosphatase (DFPase) from Loligo vulgaris have been modified by means of site-directed mutagenesis to improve our understanding of the reaction mechanism. Enzymatic characterization of mutants located in the major groove of the substrate binding pocket indicates that large hydrophobic side chains at these positions...

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PMID: 15966726
DOI: 10.1021/bi0500675

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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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