Primary structure of a multimeric protein, homologous to the pep-utilizing 
enzyme family and isolated from a hyperthermophilic archaebacterium

Cicicopol, C.; Peters, J.; Kellermann, J.; Baumeister, W.

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Primary structure of a multimeric protein, homologous to the pep-utilizing enzyme family and isolated from a hyperthermophilic archaebacterium

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Cicicopol, C., Peters, J., Kellermann, J., & Baumeister, W. (1994). Primary structure of a multimeric protein, homologous to the pep-utilizing enzyme family and isolated from a hyperthermophilic archaebacterium. FEBS Letters, 356(2-3), 345-350.

Cite as: https://hdl.handle.net/11858/00-001M-0000-0010-736F-B

Abstract

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]