Function
Nudix hydrolase (NDX) hydrolyses a wide range of organic pyrophosphatases including nucleoside di- and triphosphates, dinucleoside and diphosphoinositol polyphosphates, nucleotide sugars and RNA caps[1]. In prokaryotes the number of Nudix genes varies from 0 to over 30. Mammals have around 24 Nudix genes. NDX proteins contain the GX5EX7REUXEEXGU signature sequence[2]. An example of a well-studied Nudix enzyme is NudT16. Human NDX 16 is called U8-SNORNA-capping enzyme.
- Nudix hydrolase 7 has a role in peroxisomal acyl-CoA homeostasis[3].
- Nudix hydrolase 15 is a negative regulator of thiopurine activation and toxicity.
Relevance
NDX 7 eliminates potentially toxic nucleotide metabolites from the cell. The NDX of E. coli is named MutT and is able to neutralize the promutagenic compound 7,8-dihydro-oxoguanosine triphosphate thus preventing its incorporation into DNA[4].
Structural highlights
The structure contains the NDX signature sequence and [5]. Monomer A is colored deepskyblue, monomer B is colored salmon, water molecules are shown as red spheres.
3D structures of Nudix hydrolase
Nudix hydrolase 3D structures
