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Article: Mutagenic analysis of the conserved residues in dehalogenase IVa of Burkholderia cepacia MBA4

TitleMutagenic analysis of the conserved residues in dehalogenase IVa of Burkholderia cepacia MBA4
Authors
KeywordsBurkholderia cepacia
L-2-haloacid dehalogenase
Mutagenic analysis
Issue Date2001
PublisherBlackwell Publishing Ltd. The Journal's web site is located at http://www.blackwellpublishing.com/journal.asp?ref=0378-1097&site=1
Citation
Fems Microbiology Letters, 2001, v. 204 n. 1, p. 135-140 How to Cite?
AbstractAmino and carboxyl terminal deletion derivatives of dehalogenase IVa (DehIVa) of Burkholderia cepacia MBA4 were constructed and analyzed for enzyme activity and for protein integrity. The results suggested that the majority of the protein is indispensable. Point mutations on 29 conserved charged and/or polar residues were generated and characterized. Derivatives D11E, D11N, D11S and D181N were totally inactive while mutant N178D was defective in catalysis. Mutations of other conserved residues displayed varying effects. Mutation that enhances DehIVa activity has been shown to be inhibitory in other dehalogenase and essential conserved residues in DehIVa have been shown to be dispensable in others. This suggests there is no general rule for the importance of these conserved residues. © 2001 Federation of European Microbiological Societies. Published by Elsevier Science B.V. All rights reserved.
Persistent Identifierhttp://hdl.handle.net/10722/68585
ISSN
2015 Impact Factor: 1.858
2015 SCImago Journal Rankings: 1.126
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorPang, BCMen_HK
dc.contributor.authorTsang, JSHen_HK
dc.date.accessioned2010-09-06T06:05:54Z-
dc.date.available2010-09-06T06:05:54Z-
dc.date.issued2001en_HK
dc.identifier.citationFems Microbiology Letters, 2001, v. 204 n. 1, p. 135-140en_HK
dc.identifier.issn0378-1097en_HK
dc.identifier.urihttp://hdl.handle.net/10722/68585-
dc.description.abstractAmino and carboxyl terminal deletion derivatives of dehalogenase IVa (DehIVa) of Burkholderia cepacia MBA4 were constructed and analyzed for enzyme activity and for protein integrity. The results suggested that the majority of the protein is indispensable. Point mutations on 29 conserved charged and/or polar residues were generated and characterized. Derivatives D11E, D11N, D11S and D181N were totally inactive while mutant N178D was defective in catalysis. Mutations of other conserved residues displayed varying effects. Mutation that enhances DehIVa activity has been shown to be inhibitory in other dehalogenase and essential conserved residues in DehIVa have been shown to be dispensable in others. This suggests there is no general rule for the importance of these conserved residues. © 2001 Federation of European Microbiological Societies. Published by Elsevier Science B.V. All rights reserved.en_HK
dc.languageengen_HK
dc.publisherBlackwell Publishing Ltd. The Journal's web site is located at http://www.blackwellpublishing.com/journal.asp?ref=0378-1097&site=1en_HK
dc.relation.ispartofFEMS Microbiology Lettersen_HK
dc.rightsF E M S Microbiology Letters. Copyright © Blackwell Publishing Ltd.en_HK
dc.subjectBurkholderia cepaciaen_HK
dc.subjectL-2-haloacid dehalogenaseen_HK
dc.subjectMutagenic analysisen_HK
dc.titleMutagenic analysis of the conserved residues in dehalogenase IVa of Burkholderia cepacia MBA4en_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0378-1097&volume=204&spage=135&epage=140&date=2001&atitle=Mutagenic+analysis+of+the+conserved+residues+in+dehalogenase+IVa+of+Burkholderia+cepacia+MBA4en_HK
dc.identifier.emailTsang, JSH: jshtsang@hku.hken_HK
dc.identifier.authorityTsang, JSH=rp00792en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1016/S0378-1097(01)00396-2en_HK
dc.identifier.pmid11682192-
dc.identifier.scopuseid_2-s2.0-0035899924en_HK
dc.identifier.hkuros65451en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0035899924&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume204en_HK
dc.identifier.issue1en_HK
dc.identifier.spage135en_HK
dc.identifier.epage140en_HK
dc.identifier.isiWOS:000172003700024-
dc.publisher.placeUnited Kingdomen_HK
dc.identifier.scopusauthoridPang, BCM=36893364200en_HK
dc.identifier.scopusauthoridTsang, JSH=7102483508en_HK

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