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Conformational Disorganization within the Active Site of a Recently Evolved Organophosphate Hydrolase Limits Its Catalytic Efficiency

Mabbitt, Peter; Correy, Galen; Meirelles, Tamara; Fraser, Nicholas; Coote, Michelle; Jackson, Colin

Description

The evolution of new enzymatic activity is rarely observed outside of the laboratory. In the agricultural pest Lucilia cuprina, a naturally occurring mutation (Gly137Asp) in α-esterase 7 (LcαE7) results in acquisition of organophosphate hydrolase activity and confers resistance to organophosphate insecticides. Here, we present an X-ray crystal structure of LcαE7:Gly137Asp that, along with kinetic data, suggests that Asp137 acts as a general base in the new catalytic mechanism. Unexpectedly, the...[Show more]

CollectionsANU Research Publications
Date published: 2016-03-08
Type: Journal article
URI: http://hdl.handle.net/1885/209991
Source: Biochemistry
DOI: 10.1021/acs.biochem.5b01322
Access Rights: Open Access

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