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Conference Paper: Characterization and mutational analysis of an exopolyphosphatase from Mycobacterium smegmatis
Title | Characterization and mutational analysis of an exopolyphosphatase from Mycobacterium smegmatis |
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Authors | |
Keywords | Biochemistry Enzymes Microbiology and Physiology and biochemistry |
Issue Date | 2011 |
Publisher | International Association for Dental Research. |
Citation | The 25th IADR-SEA Division Annual Scientific Meeting, Singapore, 28-30 October 2011. How to Cite? |
Abstract | Inorganic 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) ... |
Description | Oral Communication Session 6: abstract no. 134 |
Persistent Identifier | http://hdl.handle.net/10722/137699 |
DC Field | Value | Language |
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dc.contributor.author | Choi, MY | en_US |
dc.contributor.author | Wong, LLY | en_US |
dc.contributor.author | Tanner, JA | en_US |
dc.contributor.author | Watt, RM | en_US |
dc.date.accessioned | 2011-08-26T14:31:43Z | - |
dc.date.available | 2011-08-26T14:31:43Z | - |
dc.date.issued | 2011 | en_US |
dc.identifier.citation | The 25th IADR-SEA Division Annual Scientific Meeting, Singapore, 28-30 October 2011. | en_US |
dc.identifier.uri | http://hdl.handle.net/10722/137699 | - |
dc.description | Oral Communication Session 6: abstract no. 134 | - |
dc.description.abstract | Inorganic 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.language | eng | en_US |
dc.publisher | International Association for Dental Research. | - |
dc.relation.ispartof | IADR-SEA 2011 Annual Scientific Meeting | en_US |
dc.subject | Biochemistry | - |
dc.subject | Enzymes | - |
dc.subject | Microbiology and Physiology and biochemistry | - |
dc.title | Characterization and mutational analysis of an exopolyphosphatase from Mycobacterium smegmatis | en_US |
dc.type | Conference_Paper | en_US |
dc.identifier.email | Choi, MY: meiychoi@hku.hk | en_US |
dc.identifier.email | Wong, LLY: lapywong@hku.hk | en_US |
dc.identifier.email | Tanner, JA: jatanner@hku.hk | en_US |
dc.identifier.email | Watt, RM: rmwatt@hku.hk | en_US |
dc.identifier.authority | Tanner, JA=rp00495 | en_US |
dc.identifier.authority | Watt, RM=rp00043 | en_US |
dc.description.nature | link_to_OA_fulltext | - |
dc.identifier.hkuros | 190349 | en_US |
dc.description.other | The 25th IADR-SEA Division Annual Scientific Meeting, Singapore, 28-30 October 2011. | - |