Thermotoga maritima Phosphofructokinases: Expression and Characterization of Two Unique Enzymes

AUTOR(ES)

Ding, Yan-Huai R.

FONTE

American Society for Microbiology

RESUMO

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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