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Nucleic Acids Research
Article . 1978 . Peer-reviewed
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Substrate dependence of the mechanism of EcoRI endonuclease

Authors: R A, Rubin; P, Modrich;

Substrate dependence of the mechanism of EcoRI endonuclease

Abstract

The mechanism of EcoRI endonuclease is substrate dependent. At 37 degrees dissociation of the enzyme-Form II DNA intermediates of ColE1 DNA and bacteriophage G4 RFI DNA is negligible. Therefore, both DNA strands with in the EcoRI sequence are cleaved during a single binding event. However, double strand cleavage of SV40 DNA occurs without dissociation of the enzyme in only 75% of the catalytic events. This mechanistic difference presumably reflects sequence differences about the EcoRI sites of these DNA's.

Related Organizations
Keywords

DNA, Bacterial, Kinetics, Base Sequence, DNA, Viral, Bacteriocin Plasmids, Escherichia coli, DNA Restriction Enzymes, Simian virus 40, Substrate Specificity

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    influence
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selected citations
These citations are derived from selected sources.
This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Citations provided by BIP!
popularity
This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network.
BIP!Popularity provided by BIP!
influence
This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Influence provided by BIP!
impulse
This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network.
BIP!Impulse provided by BIP!
72
Average
Top 10%
Top 10%
gold