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Site-directed mutagenesis of dienelactone hydrolase produces dienelactone isomerase

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Date

2000

Authors

Walker, Ian
Easton, Christopher
Ollis, David

Journal Title

Journal ISSN

Volume Title

Publisher

Royal Society of Chemistry

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.

Description

Keywords

Keywords: hydrolase; isomerase; lactone; article; catalysis; enzyme active site; enzyme activity; enzyme modification; hydrolysis; isomerism; site directed mutagenesis

Citation

URI

http://hdl.handle.net/1885/90004

Collections

ANU Research Publications

Source

Chemical Communications

Type

Journal article

Book Title

Entity type

Access Statement

License Rights

DOI

Restricted until

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