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Probing the mechanisms for the selectivity and promiscuity of methyl parathion hydrolase

Purg, Miha; Pabis, Anna; Baier, Florian; Tokuriki, Nobuhiko; Jackson, Colin; Kamerlin, Shina Caroline Lynn

Description

Diverse organophosphate hydrolases have convergently evolved the ability to hydrolyse man-made organophosphates. Thus, these enzymes are attractive model systems for studying the factors shaping enzyme functional evolution. Methyl parathion hydrolase (MPH) is an enzyme from the metallo-β-lactamase superfamily, which hydrolyses a wide range of organophosphate, aryl ester and lactone substrates. In addition, MPH demonstrates metal-ion-dependent selectivity patterns. The origins of this remain...[Show more]

CollectionsANU Research Publications
Date published: 2016-11-13
Type: Journal article
URI: http://hdl.handle.net/1885/114196
Source: Philosophical transactions. Series A, Mathematical, physical, and engineering sciences
DOI: 10.1098/rsta.2016.0150

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