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Miscoding Potential of the N 2 -Ethyl-2‘-deoxyguanosine DNA Adduct by the Exonuclease-Free Klenow Fragment of Escherichia coli DNA Polymerase I †

✍ Scribed by Terashima, Isamu; Matsuda, Tomonari; Fang, Tzan-Wei; Suzuki, Naomi; Kobayashi, Jun; Kohda, Kohfuku; Shibutani, Shinya


Book ID
125950612
Publisher
American Chemical Society
Year
2001
Tongue
English
Weight
126 KB
Volume
40
Category
Article
ISSN
0006-2960

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A domain of the klenow fragment of Esche
✍ P. S. Freemont; Dr. D. L. Ollis; T. A. Steitz; C. M. Joyce 📂 Article 📅 1986 🏛 John Wiley and Sons 🌐 English ⚖ 868 KB

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