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1 n reading frame (ylgG) specifying a putative Nudix hydrolase.
2 ties that were not consistent with the known Nudix hydrolases.
3 and suggest a common catalytic mechanism for Nudix hydrolases.
4 mary structure, unique among all other known Nudix hydrolases.
5 unctional, and evolutionary relationships to Nudix hydrolases.
8 and the purified protein was identified as a Nudix hydrolase active on FAD, adenosine 5'-triphospho-5
11 y characteristic of a family of enzymes, the Nudix hydrolases, active on a variety of nucleoside diph
12 n to be associated with skin infections, the Nudix hydrolase and its associated genes may have a role
13 island-like emm region that included a novel Nudix hydrolase, and, further, this cluster appears to b
14 ther, contain a mutT motif characteristic of nudix hydrolases, and are conserved in all sequenced pox
17 mined the crystal structure, at 1.4A, of the Nudix hydrolase DR1025 from the extremely radiation resi
18 four structural superfamilies: MutT-related (Nudix) hydrolases, dUTPase, ITPase (Maf/HAM1) and all-al
21 ide triphosphate pyrophophohydrolases of the Nudix hydrolase family discovered thus far, Orf135 is hi
28 The genome of Bacillus cereus contains 26 Nudix hydrolase genes, second only to its closest relati
30 th Mg2+, Zn2+, or Mn2+ and, like most of the Nudix hydrolases, has an alkaline pH optimum between 8.5
34 pporting the notion that the function of the Nudix hydrolases is to monitor the concentrations of rea
36 each subunit comprised of the ligand-binding Nudix hydrolase-like domain and the DNA-binding winged-h
37 des a decapping protein (ASFV-DP) that has a Nudix hydrolase motif and decapping activity in vitro He
38 decapping activity of D10 is dependent on a Nudix hydrolase motif that is also present in the VACV D
39 SFV) g5R gene encodes a protein containing a Nudix hydrolase motif which in terms of sequence appears
41 cterization of a human cDNA encoding a novel nudix hydrolase NUDT5 for the hydrolysis of ADP-sugars.
43 ocida encodes PnhA, which is a member of the Nudix hydrolase subfamily of dinucleoside oligophosphate
44 omogeneity and identified as a member of the Nudix hydrolase subfamily of dinucleoside oligophosphate
45 eness of a human pathogen as a member of the Nudix hydrolase subfamily of dinucleoside oligophosphate
46 ly been identified to encode a member of the Nudix hydrolase subfamily which acts specifically on din
47 oxynucleoside triphosphates or other typical Nudix hydrolase substrates, required a physiological lev
48 udA had hydrolytic activity typical of other Nudix hydrolases, such as Escherichia coli YgdP, in that
50 k we have identified a new sub-family of the Nudix hydrolase superfamily recognizable by a specific a
51 e ytkD of Bacillus subtilis, a member of the Nudix hydrolase superfamily, has been cloned and express
52 A pyrophosphohydrolase RppH, a member of the Nudix hydrolase superfamily, triggers this degradation p
55 hosphatase NUDT9 belongs to a superfamily of Nudix hydrolases that catabolize potentially toxic compo
59 l-molecule kinases and IDI is similar to the nudix hydrolases, which act on nucleotide diphosphatecon
60 U" (where U is usually Leu, Val, or Ile) are Nudix hydrolases, which catalyze the hydrolysis of a var
61 sional structure of DR-CoAse, the first of a Nudix hydrolase with this specificity, reveals that this
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