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Journal of Bacteriology, January 2001, p. 791-794, Vol. 183, No. 2
0021-9193/01/$04.00+0   DOI: 10.1128/JB.183.2.791-794.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Thermotoga maritima Phosphofructokinases: Expression and Characterization of Two Unique Enzymes

Yan-Huai R. Ding, Ron S. Ronimus, and Hugh W. Morgan*

Thermophile Research Unit, Department of Biological Sciences, The University of Waikato, Hamilton, New Zealand

Received 5 June 2000/Accepted 25 October 2000

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.

* Corresponding author. Mailing address: Thermophile Research Unit, The University of Waikato, Private Bag 3105, Hamilton, New Zealand. Phone: 64-7-8388266. Fax: 64-7-8384324. E-mail: h.morgan{at}waikato.ac.nz.

Journal of Bacteriology, January 2001, p. 791-794, Vol. 183, No. 2
0021-9193/01/$04.00+0   DOI: 10.1128/JB.183.2.791-794.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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