Endo-deoxyribonuclease from Streptomyces rimosus.
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 (M(r) approximately 21,000; pI approximately 9.5) stable in a broad pH range but unstable to higher temperature. The enzyme has an absolute requirement for Mg2+ or Mn2+, 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.
Vukelić
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B
Department of Organic Chemistry and Biochemistry, Rudjer Bosković Institute, Zagreb, Croatia.
Ritonja
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Vitale
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L
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000302:isolation & purification* / Q000378:metabolism; D004706:Endodeoxyribonucleases / Q000302:isolation & purification* / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D008274:Magnesium / Q000378:metabolism; D008345:Manganese / Q000378:metabolism; D008969:Molecular Sequence Data; D010118:Oxytetracycline / Q000096:biosynthesis; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D013302:Streptomyces / Q000201:enzymology*; D013438:Sulfhydryl Compounds / Q000378:metabolism; D013696:Temperature
D001426:Bacterial Proteins; D013438:Sulfhydryl Compounds; D008345:Manganese; D004706:Endodeoxyribonucleases; C098343:endodeoxyribonuclease, Streptomyces rimosus; D008274:Magnesium; D010118:Oxytetracycline