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Following directed evolution with crystallography: structural changes observed in changing the substrate specificity of dienelactone hydrolase

Kim, Hye-Kyung; Liu, Jian-Wei; Carr, Paul D; Ollis, David

Description

The enzyme dienelactone hydrolase (DLH) has undergone directed evolution to produce a series of mutant proteins that have enhanced activity towards the non-physiological substrates α-naphthyl acetate and p-nitrophenyl acetate. In terms of steady-state ki

dc.contributor.authorKim, Hye-Kyung
dc.contributor.authorLiu, Jian-Wei
dc.contributor.authorCarr, Paul D
dc.contributor.authorOllis, David
dc.date.accessioned2015-12-13T22:53:42Z
dc.identifier.issn0907-4449
dc.identifier.urihttp://hdl.handle.net/1885/81927
dc.description.abstractThe enzyme dienelactone hydrolase (DLH) has undergone directed evolution to produce a series of mutant proteins that have enhanced activity towards the non-physiological substrates α-naphthyl acetate and p-nitrophenyl acetate. In terms of steady-state ki
dc.publisherMunksgaard International Publishers
dc.sourceActa Crystallographica Section D: Biological Crystallography
dc.subjectKeywords: 1 naphthyl acetate; alpha-naphthyl acetate; benzylsulfonyl fluoride; carboxylesterase; carboxymethylenebutenolidase; naphthol derivative; article; binding site; chemistry; directed molecular evolution; drug antagonism; enzyme specificity; enzymology; Esch
dc.titleFollowing directed evolution with crystallography: structural changes observed in changing the substrate specificity of dienelactone hydrolase
dc.typeJournal article
local.description.notesImported from ARIES
local.description.refereedYes
local.identifier.citationvolume61
dc.date.issued2005
local.identifier.absfor060199 - Biochemistry and Cell Biology not elsewhere classified
local.identifier.ariespublicationMigratedxPub10231
local.type.statusPublished Version
local.contributor.affiliationKim, Hye-Kyung, College of Physical and Mathematical Sciences, ANU
local.contributor.affiliationLiu, Jian-Wei, College of Physical and Mathematical Sciences, ANU
local.contributor.affiliationCarr, Paul D, College of Physical and Mathematical Sciences, ANU
local.contributor.affiliationOllis, David, College of Physical and Mathematical Sciences, ANU
local.description.embargo2037-12-31
local.bibliographicCitation.issue7
local.bibliographicCitation.startpage920
local.bibliographicCitation.lastpage931
local.identifier.doi10.1107/S0907444905009042
dc.date.updated2015-12-11T10:58:47Z
local.identifier.scopusID2-s2.0-24644450583
CollectionsANU Research Publications

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