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A fully active DNA polymerase I from Escherichia coli lacking stoichiometric zinc

✍ Scribed by Kim E. Walton; Peter C. FitzGerald; Mary S. Herrmann; W.David Behnke

Book ID
115756366
Publisher
Elsevier Science
Year
1982
Tongue
English
Weight
718 KB
Volume
108
Category
Article
ISSN
0006-291X

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πŸ“œ SIMILAR VOLUMES

A domain of the klenow fragment of Esche
A domain of the klenow fragment of Escherichia coli DNA polymerase I has polymerase but no exonuclease activity
✍ P. S. Freemont; Dr. D. L. Ollis; T. A. Steitz; C. M. Joyce πŸ“‚ Article πŸ“… 1986 πŸ› John Wiley and Sons 🌐 English βš– 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