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Schlagwörter:
Pep synthase; Pep-utilizing; Archaea; Hyperthermophilic.; Phosphotransferase system; Nucleotide-sequence; Pyruvate; Dikinase; Cloning; Genes.; Biochemistry & biophysics.
Zusammenfassung:
A large protein complex (approx. 2000 kDa) was found in the cytosol of the hyperthermophilic archaebacterium Staphylothermus marinas. The purified protein was shown to be a homomultimer of 93 kDa subunits, the primary structure of which was determined by nucleotide sequence analysis. The protein belongs to the family of phosphoenolpyruvate-utilizing enzymes and represents the first member characterized in archaebacteria. Its homomultimeric organisation differs from the typically dimeric structure of its eubacterial and eukaryotic counterparts. [References: 16]
