The Klenow fragment of DNA polymerase I from Escherichia coli has two enzymatic activities: DNA polymerase and 3'-5' exonuclease. The crystal structure showed that the fragment is folded into two distinct domains. The smaller domain has a binding site for deoxynucleoside monophosphate and a divalent
Phosphorylation of Escherichia coli poly(A) polymerase I and effects of this modification on the enzyme activity
✍ Scribed by Jacek Jasiecki; Grzegorz Węgrzyn
- Book ID
- 109329396
- Publisher
- John Wiley and Sons
- Year
- 2006
- Tongue
- English
- Weight
- 176 KB
- Volume
- 261
- Category
- Article
- ISSN
- 0378-1097
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