Browsing Citations Only by Author "Frick, David"
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Escherichia coli orf17 codes for a nucleoside triphosphate pyrophosphohydrolase member of the MutT family of proteins
O'Handley, Suzanne; Frick, David; Bullions, Linda; Mildvan, Albert; Bessman, Maurice (The American Society for Biochemistry and Molecular Biology: Journal of Biological Chemistry, 1996-10-04)The product of the Escherichia coli orf17 gene is a novel nucleoside triphosphate pyrophosphohydrolase with a preference for dATP over the other canonical (deoxy)nucleoside triphosphates, and it catalyzes the hydrolysis ... -
The MutT proteins or "Nudix" hydrolases, a family of versatile, widely distributed, "housecleaning" enzymes
Bessman, Maurice; Frick, David; O'Handley, Suzanne (The American Society for Biochemistry and Molecular Biology: Journal of Biological Chemistry, 1996-10-11)Our studies on the biochemical basis of spontaneous mutations took an interesting and unexpected turn when we discovered that a small region of amino acid homology between the MutT protein of Escherichia coli and the MutX ... -
Orf186 represents a new member of the nudix hydrolases, active on adenosine(5)triphospho(5)adenosine, ADP-ribose, and NADH
O'Handley, Suzanne; Frick, David; Dunn, Christopher; Bessman, Maurice (The American Society for Biochemistry and Molecular Biology: Journal of Biological Chemistry, 1998-02-06)Orf186, a new member of the Nudix hydrolase family of genes, has been cloned and expressed, and the protein has been purified and identified as an enzyme highly specific for compounds of ADP. Its three major substrates are ... -
Studies on the ADP-ribose pyrophosphatase subfamily of the nudix hydrolases and tentative identification of trgB, a gene associated with tellurite resistance
Dunn, Christopher; O'Handley, Suzanne; Frick, David; Bessman, Maurice (The American Society for Biochemistry and Molecular Biology: Journal of Biological Chemistry, 1999-11-05)Four Nudix hydrolase genes, ysa1 from Saccharomyces cerevisiae, orf209 from Escherichia coli, yqkg from Bacillus subtilis, and hi0398 from Hemophilus influenzae were amplified, cloned into an expression vector, and transformed ...