Site-directed mutagenesis of dienelactone hydrolase produces dienelactone isomerase

dc.contributor.authorWalker, Ian
dc.contributor.authorEaston, Christopher
dc.contributor.authorOllis, David
dc.date.accessioned2015-12-13T23:18:05Z
dc.date.available2015-12-13T23:18:05Z
dc.date.issued2000
dc.date.updated2015-12-12T08:55:25Z
dc.description.abstractReplacing 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.
dc.identifier.issn1359-7345
dc.identifier.urihttp://hdl.handle.net/1885/90004
dc.publisherRoyal Society of Chemistry
dc.sourceChemical Communications
dc.subjectKeywords: hydrolase; isomerase; lactone; article; catalysis; enzyme active site; enzyme activity; enzyme modification; hydrolysis; isomerism; site directed mutagenesis
dc.titleSite-directed mutagenesis of dienelactone hydrolase produces dienelactone isomerase
dc.typeJournal article
local.bibliographicCitation.lastpage672
local.bibliographicCitation.startpage671
local.contributor.affiliationWalker, Ian, College of Physical and Mathematical Sciences, ANU
local.contributor.affiliationEaston, Christopher, College of Physical and Mathematical Sciences, ANU
local.contributor.affiliationOllis, David, College of Physical and Mathematical Sciences, ANU
local.contributor.authoruidWalker, Ian, u4044638
local.contributor.authoruidEaston, Christopher, u9500570
local.contributor.authoruidOllis, David, u9200080
local.description.notesImported from ARIES
local.description.refereedYes
local.identifier.absfor030499 - Medicinal and Biomolecular Chemistry not elsewhere classified
local.identifier.ariespublicationMigratedxPub20261
local.identifier.citationvolume8
local.identifier.scopusID2-s2.0-0034696912
local.type.statusPublished Version

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