Issue 8, 2000
From the journal:

Chemical Communications

Site-directed mutagenesis of dienelactone hydrolase produces dienelactone isomerase

Ian Walker,a   Christopher J. Easton*a  and  David L. Ollis*a  

* Corresponding authors

a Research School of Chemistry, Australian National University, Canberra, ACT 0200, Australia.
E-mail: easton@rsc.anu.edu.au; ollis@rsc.anu.edu.au

Abstract

Replacing the active site Cys-123 of dienelactone hydrolase with Ser completely changes the catalysis displayed by the protein, from hydrolysis of the substrate E- and Z-dienelactones to maleylacetate by the native enzyme, to interconversion of the substrates by the mutant, dienelactone isomerase.

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Article information

DOI
https://doi.org/10.1039/B000365O
Article type
Communication
Submitted
10 Jan 2000
Accepted
06 Mar 2000
First published
31 Mar 2000

Chem. Commun., 2000, 671-672

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Site-directed mutagenesis of dienelactone hydrolase produces dienelactone isomerase

I. Walker, C. J. Easton and D. L. Ollis, Chem. Commun., 2000, 671 DOI: 10.1039/B000365O

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