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Article

Structural flexibility enhances the reactivity of the bioremediator glycerophosphodiesterase by fine-tuning its mechanism of hydrolysis.

Journal of the American Chemical Society - 26 Aug 2009

Hadler Kieran S, Mitić Natasa, Ely Fernanda, Hanson Graeme R, Gahan Lawrence R, Larrabee James A, Ollis David L, Schenk Gerhard

Abstract excerpt

The glycerophosphodiesterase from Enterobacter aerogenes (GpdQ) belongs to the family of binuclear metallohydrolases and has attracted recent attention due to its potential in bioremediation. Formation of a catalytically competent binuclear center is promoted by the substrate (Hadler et al. J. Am. Chem. Soc. 2008, 130, 14129). Using the paramagnetic properties of Mn(II), we estimated the K(d) values for the metal...

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PMID: 19653693
DOI: 10.1021/ja903534f

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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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