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

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: https://hdl.handle.net/11858/00-001M-0000-0010-736F-B Version Permalink: https://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: Date issued: 1994-12-19

Publication Status: Issued

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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: -