Site-directed mutagenesis of dienelactone hydrolase produces dienelactone isomerase
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Walker, Ian
Easton, Christopher
Ollis, David
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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.
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Chemical Communications