Thermotoga maritima phosphofructokinases: expression and characterization of two unique enzymes |
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Authors: | Ding Y R Ronimus R S Morgan H W |
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Institution: | Thermophile Research Unit, Department of Biological Sciences, The University of Waikato, Hamilton, New Zealand. |
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Abstract: | A pyrophosphate-dependent phosphofructokinase (PPi-PFK) and an ATP-dependent phosphofructokinase (ATP-PFK) from Thermotoga maritima have been cloned and characterized. The PPi-PFK is unique in that the Km and Vmax values indicate that polyphosphate is the preferred substrate over pyrophosphate; the enzyme in reality is a polyphosphate-dependent PFK. The ATP-PFK was not significantly affected by common allosteric effectors (e.g., phosphoenolpyruvate) but was strongly inhibited by PPi and polyphosphate. The results suggest that the control of the Embden-Meyerhof pathway in this organism is likely to be modulated by pyrophosphate and/or polyphosphate. |
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