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Substrate-induced conformational change and isomerase activity of dienelactone hydrolase and its site-specific mutants

Walker, Ian; Hennessy, James E; Ollis, David; Easton, Christopher

Description

Studies of the interactions of dienelactone hydrolase (DLH) and its mutants with both E and Z dienelactone substrates show that the enzyme exhibits two different conformational responses specific for hydrolysis of each of its substrate isomers. DLH facilitates hydrolysis of the Z dienelactone through an unusual charge-relay system that is initiated by interaction between the substrate carboxylate and an enzyme arginine residue that activates an otherwise non-nucleophilic cysteine. The E...[Show more]

CollectionsANU Research Publications
Date published: 2012
Type: Journal article
URI: http://hdl.handle.net/1885/61615
Source: ChemBioChem
DOI: 10.1002/cbic.201200232

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