Endo-deoxyribonuclease from Streptomyces rimosus
| Autor: | B. Vukelić, Lj. Vitale, A. Ritonja |
|---|---|
| Rok vydání: | 1995 |
| Předmět: |
Stereochemistry
Molecular Sequence Data Oxytetracycline Applied Microbiology and Biotechnology Streptomyces Bacterial Proteins Magnesium Amino Acid Sequence Sulfhydryl Compounds chemistry.chemical_classification Manganese Endodeoxyribonucleases Sequence Homology Amino Acid biology Endo-deoxyribonuclease Streptomyces rimosus Isolation Characterization Streptomycetaceae Temperature Protein primary structure Deoxyribonuclease General Medicine Hydrogen-Ion Concentration biology.organism_classification Enzyme Biochemistry chemistry Actinomycetales Sequence Alignment Bacteria Biotechnology |
| Zdroj: | Applied Microbiology and Biotechnology. 43:1056-1060 |
| ISSN: | 1432-0614 0175-7598 |
| DOI: | 10.1007/bf00166925 |
| Popis: | From filtrates of an oxytetracycline-producing culture of Streptomyces rimosus a deoxyribonuclease was purified to homogeneity and determined to be a potent endo-DNase. It is a monomeric, basic protein (Mr≈ 21 000 ; pI≈ 9.5) stable in a broad pH range but unstable to higher temperature.The enzyme has an absolute requirement for Mg^2+ or Mn^2+, and for its full activity requires free SH groups and a low-ionic-strength environment. Its N-terminal primary structure differs from that of other nucleases. The presence of DNase in culture filtrates of the oxytetracycline producer Streptomyces rimosus was reported by Penzikova et al. (1976), but the properties of the enzyme were not studied. An interest in improving the S. rimosus strain and adapting antibiotic production from waste waters, motivated the isolation and characterization of an extracellular nuclease of this microorganism. |
| Databáze: | OpenAIRE |
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