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- Title
CLONING, EXPRESSION AND PARTIAL CHARACTERIZATION OF THE C. ELEGANS EEED8.8 GENE PRODUCT, A SPECIFIC ADP-RIBOSE DIPHOSPHATASE, MEMBER OF NUDIX HYDROLASE FAMILY.
- Authors
Abdelraheim, Salama R.; Abdelelghany, Hend M.; Melennan, A. G.
- Abstract
The C. Elegans homologue of the human YSA1 protein, EEED8.8 (Nudix6), has been expressed as a thioredoxin fusion protein in Escherichia coll. It is an ADP-sugar pyrophosphatase with similar activities towards ADP-ribose and [DP-ribose. It is a specific ADP-ribose (adenosine 5'-diphosphoribose) pyrophosphatase with no activities towards other nucleotides. The products of ADP-ribose hydrolysis were AMP and ribose 5-phosphate. Km and kcat values with ADP-ribose were 143.8±35.69 µm & 18.9±2.485 µmol/min per mg protein using ADP-ribose as substrate respectively. The optimal activity was at pH 7.2 with 10 mM Mg2+ fluoride was inhibitory, with an IC50 of 40 µM. A major proposed function of the Mutt motif proteins is to eliminate toxic nucleotide metabolites from the cell.
- Subjects
MOLECULAR cloning; GENE expression; ADENOSINE diphosphate; RIBOSE phosphates; HYDROLASES; CAENORHABDITIS elegans; INORGANIC pyrophosphatase; THIOREDOXIN-interacting protein
- Publication
Egyptian Journal of Biochemistry & Molecular Biology, 2013, Vol 31, Issue 1, p49
- ISSN
1687-1502
- Publication type
Article