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Conference Paper: Characterization and mutational analysis of an exopolyphosphatase from Mycobacterium smegmatis

TitleCharacterization and mutational analysis of an exopolyphosphatase from Mycobacterium smegmatis
Authors
KeywordsBiochemistry
Enzymes
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) is a linear polymer comprising tens to hundreds of orthophosphate residues linked by ‘high-energy' phosphoanhydride bonds. These bio-polymers are found within all living cells, and have been shown to have a wide variety of important physiological functions. In most bacteria, the hydrolysis of Poly-P chains to monophosphate is predominantly mediated by exopolyphosphatase (Ppx) enzymes. However many bacterial species, lack identifiable Ppx enzymes. Mycobacterium smegmatis, an important model organism for tuberculosis-related experimental systems, lacks an identifiable Ppx protein, but encodes a protein sharing homology with both guanosine pentaphosphate hydrolase and Ppx enzymes (Msmeg_5413) ...
DescriptionOral Communication Session 6: abstract no. 134
Persistent Identifierhttp://hdl.handle.net/10722/137699

 

DC FieldValueLanguage
dc.contributor.authorChoi, MYen_US
dc.contributor.authorWong, LLYen_US
dc.contributor.authorTanner, JAen_US
dc.contributor.authorWatt, RMen_US
dc.date.accessioned2011-08-26T14:31:43Z-
dc.date.available2011-08-26T14:31:43Z-
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/10722/137699-
dc.descriptionOral Communication Session 6: abstract no. 134-
dc.description.abstractInorganic polyphosphate (poly-P) is a linear polymer comprising tens to hundreds of orthophosphate residues linked by ‘high-energy' phosphoanhydride bonds. These bio-polymers are found within all living cells, and have been shown to have a wide variety of important physiological functions. In most bacteria, the hydrolysis of Poly-P chains to monophosphate is predominantly mediated by exopolyphosphatase (Ppx) enzymes. However many bacterial species, lack identifiable Ppx enzymes. Mycobacterium smegmatis, an important model organism for tuberculosis-related experimental systems, lacks an identifiable Ppx protein, but encodes a protein sharing homology with both guanosine pentaphosphate hydrolase and Ppx enzymes (Msmeg_5413) ...-
dc.languageengen_US
dc.publisherInternational Association for Dental Research.-
dc.relation.ispartofIADR-SEA Division Annual Scientific Meeting, 2011en_US
dc.subjectBiochemistry-
dc.subjectEnzymes-
dc.subjectMicrobiology and Physiology and biochemistry-
dc.titleCharacterization and mutational analysis of an exopolyphosphatase from Mycobacterium smegmatisen_US
dc.typeConference_Paperen_US
dc.identifier.emailChoi, MY: meiychoi@hku.hken_US
dc.identifier.emailWong, LLY: lapywong@hku.hken_US
dc.identifier.emailTanner, JA: jatanner@hku.hken_US
dc.identifier.emailWatt, RM: rmwatt@hku.hken_US
dc.identifier.authorityTanner, JA=rp00495en_US
dc.identifier.authorityWatt, RM=rp00043en_US
dc.description.naturelink_to_OA_fulltext-
dc.identifier.hkuros190349en_US
dc.description.otherThe 25th IADR-SEA Division Annual Scientific Meeting, Singapore, 28-30 October 2011.-

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