File Download

There are no files associated with this item.

  Links for fulltext
     (May Require Subscription)
Supplementary

Article: Bacterial scavengase p20 is structurally and functionally related to peroxiredoxins

TitleBacterial scavengase p20 is structurally and functionally related to peroxiredoxins
Authors
Issue Date1997
PublisherAcademic Press. The Journal's web site is located at http://www.elsevier.com/wps/find/journaldescription.cws_home/622790/description
Citation
Biochemical And Biophysical Research Communications, 1997, v. 233 n. 3, p. 848-852 How to Cite?
AbstractScavengase p20 was recently identified as a novel family of bacterial antioxidant enzymes possessing thioredoxin-linked thiol peroxidase activity. In this study, the Escherichia coli gene coding for scavengase p20 was isolated from three different strains and the nucleotide sequence was determined. Multiple alignment of amino acid sequence revealed that a previously unidentified Cys-61 is most conserved among all bacterial p20 scavengases and corresponds to the active site in the well characterized peroxiredoxins. Phylogenetic analysis further supported that scavengase p20 is a novel subfamily of peroxiredoxins. Site directed mutagenesis studies demonstrated that Cys-61 is indispensable for the antioxidant activities of scavengase p20. Taken together, our findings strongly suggest that the p20 scavengases are structurally and functionally related to peroxiredoxins.
Persistent Identifierhttp://hdl.handle.net/10722/147426
ISSN
2015 Impact Factor: 2.371
2015 SCImago Journal Rankings: 1.152
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorZhou, Yen_US
dc.contributor.authorWan, XYen_US
dc.contributor.authorWang, HLen_US
dc.contributor.authorYan, ZYen_US
dc.contributor.authorDe Hou, Yen_US
dc.contributor.authorJin, DYen_US
dc.date.accessioned2012-05-29T06:03:38Z-
dc.date.available2012-05-29T06:03:38Z-
dc.date.issued1997en_US
dc.identifier.citationBiochemical And Biophysical Research Communications, 1997, v. 233 n. 3, p. 848-852en_US
dc.identifier.issn0006-291Xen_US
dc.identifier.urihttp://hdl.handle.net/10722/147426-
dc.description.abstractScavengase p20 was recently identified as a novel family of bacterial antioxidant enzymes possessing thioredoxin-linked thiol peroxidase activity. In this study, the Escherichia coli gene coding for scavengase p20 was isolated from three different strains and the nucleotide sequence was determined. Multiple alignment of amino acid sequence revealed that a previously unidentified Cys-61 is most conserved among all bacterial p20 scavengases and corresponds to the active site in the well characterized peroxiredoxins. Phylogenetic analysis further supported that scavengase p20 is a novel subfamily of peroxiredoxins. Site directed mutagenesis studies demonstrated that Cys-61 is indispensable for the antioxidant activities of scavengase p20. Taken together, our findings strongly suggest that the p20 scavengases are structurally and functionally related to peroxiredoxins.en_US
dc.languageengen_US
dc.publisherAcademic Press. The Journal's web site is located at http://www.elsevier.com/wps/find/journaldescription.cws_home/622790/descriptionen_US
dc.relation.ispartofBiochemical and Biophysical Research Communicationsen_US
dc.subject.meshAmino Acid Sequenceen_US
dc.subject.meshAntioxidants - Chemistry - Metabolismen_US
dc.subject.meshBase Sequenceen_US
dc.subject.meshBinding Sites - Geneticsen_US
dc.subject.meshCloning, Molecularen_US
dc.subject.meshConserved Sequenceen_US
dc.subject.meshDna Primers - Geneticsen_US
dc.subject.meshDna, Bacterial - Geneticsen_US
dc.subject.meshEscherichia Coli - Genetics - Metabolismen_US
dc.subject.meshEscherichia Coli Proteinsen_US
dc.subject.meshGenes, Bacterialen_US
dc.subject.meshMolecular Sequence Dataen_US
dc.subject.meshMolecular Structureen_US
dc.subject.meshMutagenesis, Site-Directeden_US
dc.subject.meshPeriplasmic Proteinsen_US
dc.subject.meshPeroxidases - Chemistry - Genetics - Metabolismen_US
dc.subject.meshPhylogenyen_US
dc.subject.meshSequence Homology, Amino Aciden_US
dc.titleBacterial scavengase p20 is structurally and functionally related to peroxiredoxinsen_US
dc.typeArticleen_US
dc.identifier.emailJin, DY:dyjin@hkucc.hku.hken_US
dc.identifier.authorityJin, DY=rp00452en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1006/bbrc.1997.6564en_US
dc.identifier.pmid9168946-
dc.identifier.scopuseid_2-s2.0-0031589201en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0031589201&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume233en_US
dc.identifier.issue3en_US
dc.identifier.spage848en_US
dc.identifier.epage852en_US
dc.identifier.isiWOS:A1997WX53800053-
dc.publisher.placeUnited Statesen_US
dc.identifier.scopusauthoridZhou, Y=7405368674en_US
dc.identifier.scopusauthoridWan, XY=8770795200en_US
dc.identifier.scopusauthoridWang, HL=8081373900en_US
dc.identifier.scopusauthoridYan, ZY=7402519934en_US
dc.identifier.scopusauthoridDe Hou, Y=6504616940en_US
dc.identifier.scopusauthoridJin, DY=7201973614en_US

Export via OAI-PMH Interface in XML Formats


OR


Export to Other Non-XML Formats