Search

Pulse labelling experiments and enzyme studies show that Thermoproteus tenax is able to degrade glucose via the Embden-Meyerhof-Parnas (EMP) pathway. T. tenax is the first archeum for which the glycolytic EMP pathway could be established. One of the key enzymes, 6-phosphofructokinase of T. tenax depends on (pyrophosphate-fructose-6-phosphate-1-phosphotransferase) instead of ATP as found in some bacterial and eucaryal species. In addition to the intermediates of the EMP pathway the intermediary products of the non-phosphorylated Entner-Doudoroff pathway were also detected by pulse labelling experiments indicating that under chemoorganotrophic conditions at least 2 glycolytic pathways are operative in T. tenax.

The archaebacterial EF-Tu equivalent factor was purified by affinity chromatography from 6 sulphur-dependent thermophiles (Sulfolobus, Thermoproteus, Desulfurococcus, Pyrodictium, Thermococcus and Thermoplasma) and from 4 methanogens (Methanobacterium, Methanococcus, Methanosarcina and Methanolobus). By SDS-PAGE the Mr of the archaebacterial factor was found to range from 47 000 to 53 000, like that of most eubacteria (EF-Tu) and eukaryotes (EF-1α).