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  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. (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.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0010-736F-B Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0010-7370-5
Genre: Journal Article

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Cicicopol, C., Author
Peters, J.1, Author              
Kellermann, J.1, Author              
Baumeister, W.1, Author              
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1External Organizations, ou_persistent22              

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Free keywords: Pep synthase; Pep-utilizing; Archaea; Hyperthermophilic.; Phosphotransferase system; Nucleotide-sequence; Pyruvate; Dikinase; Cloning; Genes.; Biochemistry & biophysics.
 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]

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 Dates: 1994-12-19
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Method: -
 Identifiers: eDoc: 318412
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Title: FEBS Letters
Source Genre: Journal
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Pages: - Volume / Issue: 356 (2-3) Sequence Number: - Start / End Page: 345 - 350 Identifier: -