To use all functions of this page, please activate cookies in your browser.
my.chemeurope.com
With an accout for my.chemeurope.com you can always see everything at a glance – and you can configure your own website and individual newsletter.
- My watch list
- My saved searches
- My saved topics
- My newsletter
Exonuclease III
Additional recommended knowledgeFunctionThe preferred substrates are blunt or recessed 3´-termini, although ExoIII also acts at nicks in duplex DNA to produce single-strand gaps. The enzyme is not active on single-stranded DNA, and thus 3´-protruding termini are resistant to cleavage. The degree of resistance depends on the length of the extension, with extensions 4 bases or longer being essentially resistant to cleavage. This property is used to produce unidirectional deletions from a linear molecule with one resistant (3´-overhang) and one susceptible (blunt or 5´-overhang) terminus [3]. ExoIII activity depends partially on the DNA helical structure [4] and displays sequence dependence (C>A=T>G) [5]. ExoIII has also been reported to have RNase H, 3´-phosphatase and AP-endonuclease activities [1]. RegulationTemperature, salt concentration and the ratio of enzyme to DNA greatly affect enzyme activity, requiring reaction conditions to be tailored to specific applications. References
|
||||||||||||||||||||||||
This article is licensed under the GNU Free Documentation License. It uses material from the Wikipedia article "Exonuclease_III". A list of authors is available in Wikipedia. |