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          Institute: MPI für Biochemie     Collection: Structural Biology (W. Baumeister)     Display Documents



ID: 318412.0, MPI für Biochemie / Structural Biology (W. Baumeister)
Primary structure of a multimeric protein, homologous to the pep-utilizing enzyme family and isolated from a hyperthermophilic archaebacterium
Authors:Cicicopol, C.; Peters, J.; Kellermann, J.; Baumeister, W.
Date of Publication (YYYY-MM-DD):1994-12-19
Title of Journal:FEBS Letters
Volume:356
Issue / Number:2-3
Start Page:345
End Page:350
Audience:Not Specified
Abstract / Description: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]
Free Keywords:Pep synthase; Pep-utilizing; Archaea; Hyperthermophilic.; Phosphotransferase system; Nucleotide-sequence; Pyruvate; Dikinase; Cloning; Genes.; Biochemistry & biophysics.
External Publication Status:published
Document Type:Article
Communicated by:Anton Hillebrand
Affiliations:MPI für Biochemie/Structural Biology (W. Baumeister)/
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