Pyrococcus furiosis: Difference between revisions

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''Pyrococcus Furiosus''  
''Pyrococcus Furiosus''  


''Pyrococcus furiosus ''is an hyperthermophilic organism found in submarine vents, its DNA polymerase is thus stable at very high temperatures (thermostable). Pfu DNA polymerase is an archeal DNA polymerase so it is classed as a Family B polymerase. Pfu polymerase is especially useful as it has a 3' to 5' proofreading exonuclease ability for excision of an incorrect DNA base pair after which the polymerase re-inserts the correct base pair.<ref />&nbsp;Edward M. Kennedy, Christopher Hergott, Stephen Dewhurst, and Baek Kim. (2009)&nbsp;The Mechanistic Architecture of the Thermostable Pyrococcus Furiosus Family B DNA Polymerase Motif A and its Interaction with dNTP Substrate. Journal of Biochemistry 48(47): 1116-11168<ref />.  
''Pyrococcus furiosus ''is an hyperthermophilic organism found in submarine vents, its DNA polymerase is thus stable at very high temperatures (thermostable). Pfu DNA polymerase is an archeal DNA polymerase so it is classed as a Family B polymerase. Pfu polymerase is especially useful as it has a 3' to 5' proofreading exonuclease ability for excision of an incorrect DNA base pair after which the polymerase re-inserts the correct base pair.&nbsp;
 
 
 
Reference.
 
Edward M. Kennedy, Christopher Hergott, Stephen Dewhurst, and Baek Kim. (2009)&nbsp;The Mechanistic Architecture of the Thermostable Pyrococcus Furiosus Family B DNA Polymerase Motif A and its Interaction with dNTP Substrate. Journal of Biochemistry 48(47): 1116-11168.  


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Revision as of 15:39, 12 November 2011

 

Pyrococcus Furiosus

Pyrococcus furiosus is an hyperthermophilic organism found in submarine vents, its DNA polymerase is thus stable at very high temperatures (thermostable). Pfu DNA polymerase is an archeal DNA polymerase so it is classed as a Family B polymerase. Pfu polymerase is especially useful as it has a 3' to 5' proofreading exonuclease ability for excision of an incorrect DNA base pair after which the polymerase re-inserts the correct base pair. 


Reference.

Edward M. Kennedy, Christopher Hergott, Stephen Dewhurst, and Baek Kim. (2009) The Mechanistic Architecture of the Thermostable Pyrococcus Furiosus Family B DNA Polymerase Motif A and its Interaction with dNTP Substrate. Journal of Biochemistry 48(47): 1116-11168.