PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 8798636-9 1996 The Mg2+ ion enhances binding to dUTPase of dUTP by a factor of 100 and dUDP by a factor of 10. magnesium ion 4-8 Deoxyuridine triphosphatase Drosophila melanogaster 33-40 8393252-4 1993 While the dUTPase was not completely dependent on the addition of divalent cations, its activity was stimulated markedly by Zn2+, Mg2+, and Mn2+. magnesium ion 130-134 Deoxyuridine triphosphatase Drosophila melanogaster 10-17 8604980-2 1996 The substrate dUMP and the cofactor Mg2+ protect against inactivation and modification, in agreement with the study on E. coli dUTPase (Vertessy et al. magnesium ion 36-40 Deoxyuridine triphosphatase Drosophila melanogaster 127-134 8604980-9 1996 As a consequence of Tyr-93 derivatization, the Mg2+-dependent interaction between the substrate-analogue dUDP and E. coli dUTPase becomes impaired as shown by circular dichroism spectroscopy, here presented as a tool for monitoring ligand binding to the active site. magnesium ion 47-51 Deoxyuridine triphosphatase Drosophila melanogaster 122-129 15939294-6 2005 The optimal activity of SPbeta dUTPase proved to be dependent on the presence of divalent metal ions, with Mg(2+) conferring the highest activity. magnesium ion 107-113 Deoxyuridine triphosphatase Drosophila melanogaster 31-38 31748385-4 2020 Here, we present the crystal structures of the ASFV dUTPase in complex with the product dUMP and cofactor Mg2+ at a resolution of 2.2 A. magnesium ion 106-110 Deoxyuridine triphosphatase Drosophila melanogaster 52-59 31748385-11 2020 Here, we solved the crystal structure of the ASFV dUTPase-dUMP-Mg2+ complex. magnesium ion 63-67 Deoxyuridine triphosphatase Drosophila melanogaster 50-57 17452782-1 2007 Deoxyuridine triphosphate nucleotidohydrolase (dUTPase) catalyzes the hydrolysis of dUTP to dUMP and pyrophosphate in the presence of Mg(2+) ions. magnesium ion 134-140 Deoxyuridine triphosphatase Drosophila melanogaster 47-54 3027979-3 1987 There was no apparent divalent cation requirement, but the HSV-2-induced dUTPase was inhibited by EDTA (0.1 mM) and this inhibition was reversed by either Co2+ (0.5 mM) or Mg2+ (0.5 mM). magnesium ion 172-176 Deoxyuridine triphosphatase Drosophila melanogaster 73-80 6147344-4 1984 While the HSV-1-induced dUTPase exhibited activity in the absence of added divalent cations, the activity was stimulated by Mg2+ and inhibited by EDTA. magnesium ion 124-128 Deoxyuridine triphosphatase Drosophila melanogaster 24-31 14724274-6 2004 In contrast to the bacterial enzyme, Mg(2+) binding modulates conformation of fly dUTPase, as identified by spectroscopy and by increment in melting temperature. magnesium ion 37-43 Deoxyuridine triphosphatase Drosophila melanogaster 82-89 12369927-5 2001 One of the main reasons for this limited information is the lack of the three-dimensional structure of a dUTPase enzyme with an ordered Gly-rich P-loop motif with a bound substrate and Mg(2+) ion. magnesium ion 185-191 Deoxyuridine triphosphatase Drosophila melanogaster 105-112 10657253-7 2000 dUTPase activity is highly dependent on Mg(2+) concentrations and markedly sensitive to the phosphatase inhibitor, NaF. magnesium ion 40-46 Deoxyuridine triphosphatase Drosophila melanogaster 0-7