Skip navigation
Skip navigation

The structure of an enzyme-product complex reveals the critical role of a terminal hydroxide nucleophile in the bacterial phosphotriesterase mechanism

Jackson, Colin; Kim, Hye-Kyung; Carr, Paul D; Liu, Jian-Wei; Ollis, David


A detailed understanding of the catalytic mechanism of enzymes is an important step toward improving their activity for use in biotechnology. In this paper, crystal soaking experiments and X-ray crystallography were used to analyse the mechanism of the Agrobacterium radiobacter phosphotriesterase, OpdA, an enzyme capable of detoxifying a broad range of organophosphate pesticides. The structures of OpdA complexed with ethylene glycol and the product of dimethoate hydrolysis, dimethyl...[Show more]

CollectionsANU Research Publications
Date published: 2005
Type: Journal article
Source: Biochimica et Biophysica Acta: International journal of Biochemistry and Biophysics
DOI: 10.1016/j.bbapap.2005.06.008


File Description SizeFormat Image
01_Jackson_The_structure_of_an_2005.pdf378.33 kBAdobe PDF    Request a copy

Items in Open Research are protected by copyright, with all rights reserved, unless otherwise indicated.

Updated:  17 November 2022/ Responsible Officer:  University Librarian/ Page Contact:  Library Systems & Web Coordinator