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Conference Paper: Biochemical characterization of Gppa-ppx homologues from Mycobacterium tuberculosis

TitleBiochemical characterization of Gppa-ppx homologues from Mycobacterium tuberculosis
Authors
KeywordsBiochemistry
Enzymes
Infection
Microbiology and Physiology and biochemistry
Issue Date2011
PublisherInternational Association for Dental Research.
Citation
The 25th IADR-SEA Division Annual Scientific Meeting, Singapore, 28-30 October 2011. How to Cite?
AbstractInorganic polyphosphate (poly-P), guanosine pentaphosphate (pppGpp) and guanosine tetraphosphate (ppGpp) are present within all bacterial cells. These molecules play a variety of important physiological roles; especially regarding stress resistance, virulence and biofilm formation. In E. coli, distinct exopolyphosphatase (Ppx) and guanosine pentaphosphate hydrolase (Gppa) enzymes accept both poly-P and pppGpp as substrates. However, in many bacterial species, the enzymes responsible for poly-P and pppGpp hydrolysis remain to be established. The Mycobacterium tuberculosis genome has no apparent ppx gene, but encodes two putative Gppa-ppx homologues: Rv0496 and Rv1026, whose functions have not yet been characterized ...
DescriptionPoster Session - Microbiology/Immunology II: abstract no. 180
Persistent Identifierhttp://hdl.handle.net/10722/137698

 

DC FieldValueLanguage
dc.contributor.authorChoi, MYen_US
dc.contributor.authorWong, LYen_US
dc.contributor.authorWang, Yen_US
dc.contributor.authorChen, Wen_US
dc.contributor.authorTanner, JAen_US
dc.contributor.authorWatt, RMen_US
dc.date.accessioned2011-08-26T14:31:42Z-
dc.date.available2011-08-26T14:31:42Z-
dc.date.issued2011en_US
dc.identifier.citationThe 25th IADR-SEA Division Annual Scientific Meeting, Singapore, 28-30 October 2011.en_US
dc.identifier.urihttp://hdl.handle.net/10722/137698-
dc.descriptionPoster Session - Microbiology/Immunology II: abstract no. 180-
dc.description.abstractInorganic polyphosphate (poly-P), guanosine pentaphosphate (pppGpp) and guanosine tetraphosphate (ppGpp) are present within all bacterial cells. These molecules play a variety of important physiological roles; especially regarding stress resistance, virulence and biofilm formation. In E. coli, distinct exopolyphosphatase (Ppx) and guanosine pentaphosphate hydrolase (Gppa) enzymes accept both poly-P and pppGpp as substrates. However, in many bacterial species, the enzymes responsible for poly-P and pppGpp hydrolysis remain to be established. The Mycobacterium tuberculosis genome has no apparent ppx gene, but encodes two putative Gppa-ppx homologues: Rv0496 and Rv1026, whose functions have not yet been characterized ...-
dc.languageengen_US
dc.publisherInternational Association for Dental Research.-
dc.relation.ispartofIADR-SEA Division Annual Scientific Meeting, 2011en_US
dc.subjectBiochemistry-
dc.subjectEnzymes-
dc.subjectInfection-
dc.subjectMicrobiology and Physiology and biochemistry-
dc.titleBiochemical characterization of Gppa-ppx homologues from Mycobacterium tuberculosisen_US
dc.typeConference_Paperen_US
dc.identifier.emailChoi, MY: meiychoi@hku.hken_US
dc.identifier.emailWong, LY: lapywong@hku.hken_US
dc.identifier.emailChen, W: chenwy@hku.hken_US
dc.identifier.emailTanner, JA: jatanner@hku.hken_US
dc.identifier.emailWatt, RM: rmwatt@hku.hken_US
dc.identifier.authorityChen, W=rp01487en_US
dc.identifier.authorityTanner, JA=rp00495en_US
dc.identifier.authorityWatt, RM=rp00043en_US
dc.description.naturelink_to_OA_fulltext-
dc.identifier.hkuros190348en_US
dc.description.otherThe 25th IADR-SEA Division Annual Scientific Meeting, Singapore, 28-30 October 2011.-

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