Browsing Citations Only by Author "O'Handley, Suzanne"
Now showing items 1-10 of 10
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Atomic structure of the DNA repair [4Fe-4S] enzyme endonuclease III
Kuo, C.; McRee, D.; Fisher, C.; O'Handley, Suzanne; Cunningham, R.; Tainer, J. (American Association for the Advancement of Science: Science, 1992-10-16)The crystal structure of the DNA repair enzyme endonuclease III, which recognizes and cleaves DNA at damaged bases, has been solved to 2.0 angstrom resolution with an R factor of 0.185. This iron-sulfur [4Fe-4S] enzyme is ... -
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 ... -
Identification and characterization of the nudix hydrolase from the Archaeon, Methanococcus jannaschii, as a highly specific ADP-ribose pyrophosphatase
Sheikh, Saifuddin; O'Handley, Suzanne; Dunn, Christopher; Bessman, Maurice (The American Society for Biochemistry and Molecular Biology: Journal of Biological Chemistry, 1998-08-14)The MJ1149 gene from the Archaeon, Methanococcus jannaschii, has been cloned and expressed in Escherichia coli. The 19-kDa protein containing the Nudix box, GX5EX7REUXEEXGU, has been purified and identified as a highly ... -
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 ... -
Orf135 from Escherichia coli is a nudix hydrolase specific for CTP, dCTP, and 5-methyl-dCTP
O'Handley, Suzanne; Dunn, Christopher; Bessman, Maurice (The American Society for Biochemistry and Molecular Biology:, 2001-02-23)Orf135 from Escherichia coli is a new member of the Nudix (nucleoside diphosphate linked to some other moiety, x) hydrolase family of enzymes with substrate specificity for CTP, dCTP, and 5-methyl-dCTP. The gene has been ... -
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 ... -
Structural characterization of an n-acetyl-2-aminofluorene (AAF) modified DNA oligomer by NMR, energy minimization, and molecular dynamics
O'Handley, Suzanne; Sanford, David; Xu, Rong; Lester, Cathy; Hingerty, Brian; Broyde, Suse; Krugh, Thomas (American Chemical Society: Biochemistry, 1993-03-16)An N-acetyl-2-aminofluorene (AAF) modified deoxyoligonucleotide duplex, d(Cl-C2-A3-C4-[AAF-G5]-C6-A7-C8-C9)-d(GlO-G1 l-T12-G13-C14-G 15-T16-G 17-G18), was studied by one- and twodimensional NMR spectroscopy. Eight of the ... -
Structure and mechanism of MT-ADPRase, a nudix hydrolase from Mycobacterium tuberculosis
Kang, L.; Gabelli, S.; Cunningham, J.; O'Handley, Suzanne; Amzel, L. (Elsevier: Structure, 2003-08)Nudix hydrolases are a family of proteins that contain the characteristic sequence GX(5)EX(7)REUXEEXG(I/L/V), the Nudix box. They catalyze the hydrolysis of a variety of nucleoside diphosphate derivatives such as ADP-ribose, ... -
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 ... -
YZGD from Paenibacillus thiaminolyticus, a pyridoxal phosphatase of the HAD (haloacid dehalogenase) superfamily and a versatile member of the Nudix (nucleoside diphosphate x) hydrolase superfamily
Tirrell, Isaac; Wall, Jennifer; Daley, Christopher; Denial, Sarah; Tennis, Frances; Galens, Kevin; O'Handley, Suzanne (Portland Press: Biochemical Journal, 2006-03-15)YZGD from Paenibacillus thiaminolyticus is a novel bifunctional enzyme with both PLPase (pyridoxal phosphatase) and Nudix (nucleoside diphosphate x) hydrolase activities. The PLPase activity is catalysed by the HAD (haloacid ...