Primary structure of a multimeric protein, homologous to the PEP-utilizing enzyme family and isolated from a hyperthermophilic archaebacterium.
A large protein complex (approx. 2000 kDa) was found in the cytosol of the hyperthermophilic archaebacterium Staphylothermus marinus. 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.
Cicicopol
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Max-Planck-Institut für Biochemie, Martinsried, Germany.
Peters
J
J
Kellermann
J
J
Baumeister
W
W
D000595:Amino Acid Sequence; D001105:Archaea / Q000235:genetics / Q000378:metabolism*; D001419:Bacteria / Q000201:enzymology / Q000235:genetics; D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D001483:Base Sequence; D003600:Cytosol / Q000378:metabolism; D005798:Genes, Bacterial; D006358:Hot Temperature; D046911:Macromolecular Substances; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010728:Phosphoenolpyruvate / Q000378:metabolism*; D017866:Phosphotransferases (Paired Acceptors) / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D017386:Sequence Homology, Amino Acid
D001426:Bacterial Proteins; D046911:Macromolecular Substances; D010728:Phosphoenolpyruvate; C091150:PEP homomultimer, Staphylothermus; D017866:Phosphotransferases (Paired Acceptors); C022509:pyruvate, water dikinase