File Download

There are no files associated with this item.

  Links for fulltext
     (May Require Subscription)
Supplementary

Article: Purple acid phosphatase-like sequences in prokaryotic genomes and the characterization of an atypical purple alkaline phosphatase from Burkholderia cenocepacia J2315

TitlePurple acid phosphatase-like sequences in prokaryotic genomes and the characterization of an atypical purple alkaline phosphatase from Burkholderia cenocepacia J2315
Authors
KeywordsBurkholderia
Phosphatase
Protein phosphatase
Purple acid phosphatase
Purple alkaline phosphatase
Twin-arginine signal peptide
Issue Date2009
PublisherElsevier BV. The Journal's web site is located at http://www.elsevier.com/locate/gene
Citation
Gene, 2009, v. 440 n. 1-2, p. 1-8 How to Cite?
AbstractPurple acid phosphatases (PAP) are a group of dimetallic phosphohydrolase first identified in eukaryotes. Bioinformatics analysis revealed 57 prokaryotic PAP-like sequences in the genomes of 43 bacteria and 4 cyanobacteria species. A putative PAP gene (BcPAP) from the bacteria Burkholderia cenocepacia J2315 was chosen for further studies. Synteny analysis showed that this gene is present as an independent gene in most of the members of the genus Burkholderia. The predicted 561 a.a. polypeptide of BcPAP was found to harbour all the conserved motifs of the eukaryotic PAPs and an N-terminal twin-arginine translocation signal. Expression and biochemical characterization of BcPAP in Escherichia coli revealed that this enzyme has a relatively narrow substrate spectrum, preferably towards phosphotyrosine, phosphoserine and phosphoenolpyruvate. Interestingly, this enzyme was found to have a pH optimum at 8.5, rather than an acidic optima exhibited by eukaryotic PAPs. BcPAP contains a dimetallic ion centre composed of Fe and Zn, and site-directed mutagenesis confirmed that BcPAP utilizes the invariant residues for metal-ligation and catalysis. The enzyme is secreted by the wild type bacteria and its expression is regulated by the availability of orthophosphate. Our findings suggest that not all members in the PAP family have acidic pH optimum and broad substrate specificity. © 2009 Elsevier B.V. All rights reserved.
Persistent Identifierhttp://hdl.handle.net/10722/68857
ISSN
2015 Impact Factor: 2.319
2015 SCImago Journal Rankings: 1.043
ISI Accession Number ID
Funding AgencyGrant Number
University Research Committee of the University of Hong Kong
Funding Information:

This work was supported by the University Research Committee of the University of Hong Kong (grant no. 200511159084).

References

 

DC FieldValueLanguage
dc.contributor.authorYeung, SLen_HK
dc.contributor.authorCheng, Cen_HK
dc.contributor.authorLui, TKOen_HK
dc.contributor.authorTsang, JSHen_HK
dc.contributor.authorChan, WTen_HK
dc.contributor.authorLim, BLen_HK
dc.date.accessioned2010-09-06T06:08:21Z-
dc.date.available2010-09-06T06:08:21Z-
dc.date.issued2009en_HK
dc.identifier.citationGene, 2009, v. 440 n. 1-2, p. 1-8en_HK
dc.identifier.issn0378-1119en_HK
dc.identifier.urihttp://hdl.handle.net/10722/68857-
dc.description.abstractPurple acid phosphatases (PAP) are a group of dimetallic phosphohydrolase first identified in eukaryotes. Bioinformatics analysis revealed 57 prokaryotic PAP-like sequences in the genomes of 43 bacteria and 4 cyanobacteria species. A putative PAP gene (BcPAP) from the bacteria Burkholderia cenocepacia J2315 was chosen for further studies. Synteny analysis showed that this gene is present as an independent gene in most of the members of the genus Burkholderia. The predicted 561 a.a. polypeptide of BcPAP was found to harbour all the conserved motifs of the eukaryotic PAPs and an N-terminal twin-arginine translocation signal. Expression and biochemical characterization of BcPAP in Escherichia coli revealed that this enzyme has a relatively narrow substrate spectrum, preferably towards phosphotyrosine, phosphoserine and phosphoenolpyruvate. Interestingly, this enzyme was found to have a pH optimum at 8.5, rather than an acidic optima exhibited by eukaryotic PAPs. BcPAP contains a dimetallic ion centre composed of Fe and Zn, and site-directed mutagenesis confirmed that BcPAP utilizes the invariant residues for metal-ligation and catalysis. The enzyme is secreted by the wild type bacteria and its expression is regulated by the availability of orthophosphate. Our findings suggest that not all members in the PAP family have acidic pH optimum and broad substrate specificity. © 2009 Elsevier B.V. All rights reserved.en_HK
dc.languageengen_HK
dc.publisherElsevier BV. The Journal's web site is located at http://www.elsevier.com/locate/geneen_HK
dc.relation.ispartofGeneen_HK
dc.rightsGene. Copyright © Elsevier BV.en_HK
dc.subjectBurkholderiaen_HK
dc.subjectPhosphataseen_HK
dc.subjectProtein phosphataseen_HK
dc.subjectPurple acid phosphataseen_HK
dc.subjectPurple alkaline phosphataseen_HK
dc.subjectTwin-arginine signal peptideen_HK
dc.titlePurple acid phosphatase-like sequences in prokaryotic genomes and the characterization of an atypical purple alkaline phosphatase from Burkholderia cenocepacia J2315en_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0378-1119&volume=440&spage=1&epage=8&date=2009&atitle=Purple+acid+phosphatase-like+sequences+in+prokaryotic+genomes+and+the+characterization+of+an+atypical+purple+alkaline+phosphatase+from+Burkholderia+cenocepacia+J2315en_HK
dc.identifier.emailTsang, JSH: jshtsang@hku.hken_HK
dc.identifier.emailChan, WT: wtchan@hku.hken_HK
dc.identifier.emailLim, BL: bllim@hkucc.hku.hken_HK
dc.identifier.authorityTsang, JSH=rp00792en_HK
dc.identifier.authorityChan, WT=rp00668en_HK
dc.identifier.authorityLim, BL=rp00744en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1016/j.gene.2009.04.002en_HK
dc.identifier.pmid19376213-
dc.identifier.scopuseid_2-s2.0-65549149196en_HK
dc.identifier.hkuros158441en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-65549149196&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume440en_HK
dc.identifier.issue1-2en_HK
dc.identifier.spage1en_HK
dc.identifier.epage8en_HK
dc.identifier.isiWOS:000266747900001-
dc.publisher.placeNetherlandsen_HK
dc.identifier.scopusauthoridYeung, SL=26642849000en_HK
dc.identifier.scopusauthoridCheng, C=7404797223en_HK
dc.identifier.scopusauthoridLui, TKO=26536246300en_HK
dc.identifier.scopusauthoridTsang, JSH=7102483508en_HK
dc.identifier.scopusauthoridChan, WT=7403918827en_HK
dc.identifier.scopusauthoridLim, BL=7201983917en_HK

Export via OAI-PMH Interface in XML Formats


OR


Export to Other Non-XML Formats