Primary structure of a multimeric protein, homologous to the PEP-utilizing enzyme family and isolated from a hyperthermophilic archaebacterium
| Autor: | Wolfgang Baumeister, Christiana Cicicopol, Josef Kellermann, Jürgen Peters |
|---|---|
| Rok vydání: | 1994 |
| Předmět: |
Multiprotein complex
Hot Temperature Macromolecular Substances Molecular Sequence Data Biophysics Biology Hyperthermophilic Biochemistry Phosphoenolpyruvate Cytosol Bacterial Proteins Structural Biology Genetics Amino Acid Sequence Molecular Biology Gene chemistry.chemical_classification Bacteria Base Sequence Sequence Homology Amino Acid Nucleic acid sequence Protein primary structure PEP-utilizing Cell Biology PEP group translocation biology.organism_classification Molecular biology Archaea Molecular Weight Phosphotransferases (Paired Acceptors) Enzyme chemistry Genes Bacterial PEP synthase |
| Zdroj: | FEBS letters. 356(2-3) |
| ISSN: | 0014-5793 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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