Structural Insight into the Mechanism of Substrate Specificity and Catalytic Activity of an HD-Domain Phosphohydrolase: The 5′-Deoxyribonucleotidase YfbR from Escherichia coli-Reference-Cited by-同舟云学术

Structural Insight into the Mechanism of Substrate Specificity and Catalytic Activity of an HD-Domain Phosphohydrolase: The 5′-Deoxyribonucleotidase YfbR from Escherichia coli

Published:2008-04 Issue:1 Volume:378 Page:215-226
ISSN:0022-2836
Container-title:Journal of Molecular Biology
language:en
Short-container-title:Journal of Molecular Biology

Author:

Zimmerman Matthew D.,Proudfoot Michael,Yakunin Alexander,Minor Wladek

Publisher

Elsevier BV

Subject

Molecular Biology,Structural Biology

Reference56 articles.

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3. The HD domain of the Escherichia coli tRNA nucleotidyltransferase has 2′,3′-cyclic phosphodiesterase, 2′-nucleotidase, and phosphatase activities;Yakunin;J. Biol. Chem.,2004

4. Cloning the spoT gene of Escherichia coli: identification of the spoT gene product;An;J. Bacteriol.,1979

5. Biochemical characterization of TT1383 from Thermus thermophilus identifies a novel dNTP triphosphohydrolase activity stimulated by dATP and dTTP;Kondo;J. Biochem. (Tokyo),2004

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