Deoxynucleoside Triphosphate and Pyrophosphate Binding Sites in the Catalytically Competent Ternary Complex for the Polymerase Reaction Catalyzed by DNA Polymerase I (Klenow Fragment)-Reference-Cited by-同舟云学术

Deoxynucleoside Triphosphate and Pyrophosphate Binding Sites in the Catalytically Competent Ternary Complex for the Polymerase Reaction Catalyzed by DNA Polymerase I (Klenow Fragment)

Published:1995-01 Issue:4 Volume:270 Page:1945-1954
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Astatke Mekbib,Grindley Nigel D.F.,Joyce Catherine M.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference49 articles.

1. Structure of large fragment of Escherichia coli DNA polymerase I complexed with dTMP

2. A domain of the klenow fragment ofEscherichia coli DNA polymerase I has polymerase but no exonuclease activity

3. The 3′-5′ exonuclease of DNA polymerase I of Escherichia coli: contribution of each amino acid at the active site to the reaction.

4. Identification of residues critical for the polymerase activity of the Klenow fragment of DNA polymerase I from Escherichia coli.

5. Side chains involved in catalysis of the polymerase reaction of DNA polymerase I from Escherichia coli.

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