Biochemical characterization of deblocking aminopeptidase from hyperthermophilic archaeon Thermococcus onnurineus NA1

2007 ◽  
Vol 104 (3) ◽  
pp. 188-194 ◽  
Author(s):  
Hyun Sook Lee ◽  
Yona Cho ◽  
Yun Jae Kim ◽  
Kwanghyun Nam ◽  
Jung-Hyun Lee ◽  
...  
Keyword(s):  
Biochemical Characterization ◽  
Thermococcus Onnurineus Na1 ◽  
Hyperthermophilic Archaeon

scholarly journals Genetic and biochemical characterization of a short-chain alcohol dehydrogenase from the hyperthermophilic archaeon Pyrococcus furiosu s

2001 ◽  
Vol 268 (10) ◽  
pp. 3062-3068 ◽  
Author(s):  
John van der Oost ◽  
Wilfried G. B. Voorhorst ◽  
Servé W. M. Kengen ◽  
Ans C. M. Geerling ◽  
Vincent Wittenhorst ◽  
...  
Keyword(s):  
Alcohol Dehydrogenase ◽  
Biochemical Characterization ◽  
Short Chain ◽  
Chain Alcohol ◽  
Hyperthermophilic Archaeon ◽  
Short Chain Alcohol

scholarly journals Biochemical adaptations of two sugar kinases from the hyperthermophilic archaeon Pyrococcus furiosus

2002 ◽  
Vol 366 (1) ◽  
pp. 121-127 ◽  
Author(s):  
Corné H. VERHEES ◽  
Denise G.M. KOOT ◽  
Thijs J.G. ETTEMA ◽  
Cor DIJKEMA ◽  
Willem M. de VOS ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Biochemical Characterization ◽  
Pyrococcus Furiosus ◽  
Phosphoryl Group ◽  
Hyperthermophilic Archaeon ◽  
High Affinity ◽  
Optimal Activity ◽  
Genes Encoding ◽  
Modified Embden Meyerhof Pathway

The hyperthermophilic archaeon Pyrococcus furiosus possesses a modified Embden—Meyerhof pathway, including an unusual ADP-dependent glucokinase (ADP-GLK) and an ADP-dependent phosphofructokinase. In the present study, we report the characterization of a P. furiosus galactokinase (GALK) and its comparison with the P. furiosus ADP-GLK. The pyrococcal genes encoding the ADP-GLK and GALK were functionally expressed in Escherichia coli, and the proteins were subsequently purified to homogeneity. Both enzymes are specific kinases with an optimal activity at approx. 90°C. Biochemical characterization of these enzymes confirmed that the ADP-GLK is unable to use ATP as the phosphoryl group donor, but revealed that GALK is ATP-dependent and has an extremely high affinity for ATP. There is a discussion about whether the unusual features of these two classes of kinases might reflect adaptations to a relatively low intracellular ATP concentration in the hyperthermophilic archaeon P. furiosus.

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