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Evaluation of possible active site residues in GSTZ 1-1

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dc.contributor.authorCoggan, Marjorie
dc.contributor.authorLiu, Dan
dc.contributor.authorChelvanayagam, Gareth
dc.contributor.authorAnderson, Warwick P
dc.contributor.authorAnders, Michael
dc.contributor.authorBoard, Philip
dc.date.accessioned2015-12-13T23:20:25Z
dc.date.available2015-12-13T23:20:25Z
dc.date.issued2001
dc.date.updated2015-12-12T09:03:05Z
dc.description.abstractZeta class of glutathione transferases are responsible for several novel glutathione-dependent reactions including the isomerization of maleylacetoacetate to fumarylacetoacetate and the biotransformation of α halo acids such as dichloroacetic acid (DCA).
dc.identifier.issn0009-2797
dc.identifier.urihttp://hdl.handle.net/1885/90689
dc.publisherElsevier
dc.sourceChemico-Biological Interactions
dc.subjectKeywords: Dichloroacetic acid; Glutathione transferase zeta; Mutagenesis
dc.titleEvaluation of possible active site residues in GSTZ 1-1
dc.typeJournal article
local.bibliographicCitation.lastpage187
local.bibliographicCitation.startpage185
local.contributor.affiliationCoggan, Marjorie, College of Medicine, Biology and Environment, ANU
local.contributor.affiliationLiu, Dan, College of Medicine, Biology and Environment, ANU
local.contributor.affiliationChelvanayagam, Gareth, College of Medicine, Biology and Environment, ANU
local.contributor.affiliationAnderson, Warwick P, Monash University
local.contributor.affiliationAnders, Michael, University of Rochester
local.contributor.affiliationBoard, Philip, College of Medicine, Biology and Environment, ANU
local.contributor.authoruidCoggan, Marjorie, u7400157
local.contributor.authoruidLiu, Dan, u4245938
local.contributor.authoruidChelvanayagam, Gareth, u950151
local.contributor.authoruidBoard, Philip, u7701651
local.description.notesImported from ARIES
local.description.refereedYes
local.identifier.absfor110106 - Medical Biochemistry: Proteins and Peptides (incl. Medical Proteomics)
local.identifier.ariespublicationMigratedxPub21124
local.identifier.citationvolume133
local.identifier.scopusID2-s2.0-0003206680
local.type.statusPublished Version

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