Disease relevance of NUDT9

• For two of the 64 hypothetical proteins: PA1167 from Pseudomonas aeruginosa, an alginate lyase (EC 4.2.2.3) and Rv1700 of Mycobacterium tuberculosis H37Rv, an ADP-ribose diphosphatase (EC 3.6.1.13), we have detected annotation lag of more than two years in databases [1].

High impact information on NUDT9

• We furthermore analyzed the mutation I1405E/L1406F in the Nudix box of TRPM2, because a considerably decreased AD-PRase activity of the TRPM2 NUDT9-H protein in comparison to the NUDT9 pyrophosphatase has been attributed to the reverse exchange EF --> IL [2].
• We have recently characterized the protein product of the human NUDT9 gene as a highly specific ADP-ribose (ADPR) pyrophosphatase [3].
• Investigation of the physical and enzymatic properties of NUDT9 indicates that it is functional as a monomer, optimally active at near neutral pH, and that it requires divalent metal ions and an intact Nudix motif for enzymatic activity [3].
• Using green fluorescence protein tagging, we demonstrate that the predicted human NUDT9 alpha protein is targeted highly specifically to mitochondria, whereas the predicted protein of the NUDT9 beta transcript, which is missing this sequence, exhibits no clear subcellular localization [3].
• We determined crystal structures of NUDT9 in the presence and in the absence of the reaction product ribose 5'-phosphate [4].

Biological context of NUDT9

• Furthermore, C17orf25 may suppress the cell growth by interaction with NUDT9 [5].
• The gene C17orf25 was isolated from the liver by RACE PCR. nudt9 gene was screened by yeast two-hybrid method in MatchMaker human HeLa cDNA library [5].
• Adenosine diphosphate ribose (ADPR) pyrophosphohydrolase (ADPR-PPase), which catalyzes the hydrolysis of ADPR to yield adenosine monophosphate (AMP) and ribose-5'-phosphate, was assayed in human penile foreskin [6].

Associations of NUDT9 with chemical compounds

• Human ADP-ribose pyrophosphatase NUDT9 belongs to a superfamily of Nudix hydrolases that catabolize potentially toxic compounds in the cell [4].
• The specific, submicromolar-K(m) ADP-ribose pyrophosphatase purified from human placenta is enzymically indistinguishable from recombinant NUDT9 protein, including a selectivity for Mn(2+) as activating cation and increase in K(m) for ADP-ribose, both elicited by H(2)O(2) [7].

Other interactions of NUDT9

• NUDT9 shares 39% sequence identity with the C-terminal cytoplasmic domain of the ADPR-gated calcium channel TRPM2, which exhibits low but specific enzyme activity [4].

References