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• W2017496198 abstract "The mechanism of action of the ATP-dependent DNAase from Micrococcus luteus , an enzyme which presumably is involved in the process of genetic recombination, has been investigated with partially purified or extensively purified enzyme (approximately 50 % pure). We have shown that the enzyme requires linear double-stranded DNA for activity. Double-stranded DNA with extended single-stranded regions or single-stranded DNA are degraded at a greatly reduced rate and circular double-stranded DNA is completely refractory towards the enzyme. Glycerol gradient sedimentation analysis as well as phase partition experiments have shown that the enzyme forms a stable complex with linear double-stranded DNA, but not with single-stranded DNA or circular double-stranded DNA. For this reaction ATP is not required. Maximally two enzyme molecules will bind to a linear duplex, probably one to each end. Results from kinetic experiments suggest that the formation of the enzyme-DNA complex is a necessary intermediate in the overall degradation process. Degradation after the formation of the DNA-enzyme complex is a first-order process, its rate being proportional to the concentration of the complex. At 0°C one enzyme molecule needs about 30 min to degrade one T7 DNA molecule." @default.
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• W2017496198 date "1973-02-01" @default.
• W2017496198 modified "2023-09-25" @default.
• W2017496198 title "Properties of an ATP-dependent deoxyribonuclease from Micrococcus luteus Evidence for a stable DNA-enzyme complex" @default.
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• W2017496198 doi "https://doi.org/10.1016/0005-2787(73)90398-5" @default.
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