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Article: Cloning and characterization of a cryptic haloacid dehalogenase from Burkholderia cepacia MBA4

TitleCloning and characterization of a cryptic haloacid dehalogenase from Burkholderia cepacia MBA4
Authors
Issue Date1999
PublisherAmerican Society for Microbiology.
Citation
Journal Of Bacteriology, 1999, v. 181 n. 19, p. 6003-6009 How to Cite?
AbstractBurkholderia cepacia MBA4 has been shown to produce a single dehalogenase batch culture. Moreover, other cryptic dehalogenases were also detected when the cells were grown in continuous culture. In this paper, we report the cloning and characterization of one of the cryptic dehalogenases in MBA4. This cryptic haloacid dehalogenase, designated Chd1, was expressed constitutively in Escherichia coli. This recombinant Chd1 had a relative molecular weight of 58,000 and existed predominantly as a dimer. The subunits had a relative molecular weight of 27,000. Chd1 exhibited isomer specificity, being active towards the L-isomer of 2-monochloropropionic acid only. The structural gene, chd1, was isolated on a 1.7-kb PstI fragment. This fragment contains a functional promoter, because expression of chd1 in E. coli is orientation independent. The nucleotide sequence of this fragment was determined and characterized. An open reading frame of 840 bp encoding a putative peptide of 280 amino acids was identified. This corresponds closely with the size of the subunit. The nucleotide sequence of chd1 did not show any homology with those of other dehalogenase genes. Comparison of the predicted amino acid sequence, however, shows significant homology, ranging from 42 to 50%, with the amino acid sequences of many other dehalogenases. Chd1 is unusual in having a long leader sequence, a property of periplasmic enzymes.
Persistent Identifierhttp://hdl.handle.net/10722/68461
ISSN
2015 Impact Factor: 3.198
2015 SCImago Journal Rankings: 2.216
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorTsang, JSHen_HK
dc.contributor.authorSam, Len_HK
dc.date.accessioned2010-09-06T06:04:49Z-
dc.date.available2010-09-06T06:04:49Z-
dc.date.issued1999en_HK
dc.identifier.citationJournal Of Bacteriology, 1999, v. 181 n. 19, p. 6003-6009en_HK
dc.identifier.issn0021-9193en_HK
dc.identifier.urihttp://hdl.handle.net/10722/68461-
dc.description.abstractBurkholderia cepacia MBA4 has been shown to produce a single dehalogenase batch culture. Moreover, other cryptic dehalogenases were also detected when the cells were grown in continuous culture. In this paper, we report the cloning and characterization of one of the cryptic dehalogenases in MBA4. This cryptic haloacid dehalogenase, designated Chd1, was expressed constitutively in Escherichia coli. This recombinant Chd1 had a relative molecular weight of 58,000 and existed predominantly as a dimer. The subunits had a relative molecular weight of 27,000. Chd1 exhibited isomer specificity, being active towards the L-isomer of 2-monochloropropionic acid only. The structural gene, chd1, was isolated on a 1.7-kb PstI fragment. This fragment contains a functional promoter, because expression of chd1 in E. coli is orientation independent. The nucleotide sequence of this fragment was determined and characterized. An open reading frame of 840 bp encoding a putative peptide of 280 amino acids was identified. This corresponds closely with the size of the subunit. The nucleotide sequence of chd1 did not show any homology with those of other dehalogenase genes. Comparison of the predicted amino acid sequence, however, shows significant homology, ranging from 42 to 50%, with the amino acid sequences of many other dehalogenases. Chd1 is unusual in having a long leader sequence, a property of periplasmic enzymes.en_HK
dc.languageengen_HK
dc.publisherAmerican Society for Microbiology.en_HK
dc.relation.ispartofJournal of Bacteriologyen_HK
dc.rightsJournal of Bacteriology. Copyright © American Society for Microbiology.en_HK
dc.titleCloning and characterization of a cryptic haloacid dehalogenase from Burkholderia cepacia MBA4en_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0021-9193&volume=181&spage=6003&epage=6009&date=1999&atitle=Cloning+and+characterization+of+a+cryptic+haloacid+dehalogenase+from++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.pmid10498712-
dc.identifier.scopuseid_2-s2.0-0032871075en_HK
dc.identifier.hkuros47230en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0032871075&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume181en_HK
dc.identifier.issue19en_HK
dc.identifier.spage6003en_HK
dc.identifier.epage6009en_HK
dc.identifier.isiWOS:000082835200014-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridTsang, JSH=7102483508en_HK
dc.identifier.scopusauthoridSam, L=6602908601en_HK

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