The Nudix family is a protein family of phosphohydrolases.[1][2][3] Using water-mediated catalysis they break a phosphate bond in their substrate to create two products. Substrates hydrolysed by Nudix enzymes comprise a wide range of organic pyrophosphates, including nucleoside di- and triphosphates, dinucleoside and diphosphoinositol polyphosphates, nucleotide sugars and RNA caps, with varying degrees of substrate specificity.[3] Nudix stands for Nucleoside Diphosphate linked to X. There are two components to the Nudix family: the so-called Nudix fold of a beta sheet with alpha helices on each side and the Nudix motif which contains catalytic and metal-binding amino acids. The Nudix motif is GXXXXXEXXXXXXXREUXEEXGU where U is Isoleucine, Leucine, or Valine and X is any amino acid. This forms a short helix which (usually) contains the catalytic amino acids. Nudix family enzymes include Dcp2 of the decapping complex, ADP-ribose diphosphatase, MutT, ADPRase, Ap4A, RppH, and many others.[4]
References
^Bessman MJ, Frick DN, O'Handley SF (October 1996). "The MutT proteins or "Nudix" hydrolases, a family of versatile, widely distributed, "housecleaning" enzymes". J. Biol. Chem. 271 (41): 25059–62. doi:10.1074/jbc.271.41.25059. PMID8810257.{{cite journal}}: CS1 maint: unflagged free DOI (link)
^Mildvan AS, Xia Z, Azurmendi HF, et al. (January 2005). "Structures and mechanisms of Nudix hydrolases". Arch. Biochem. Biophys. 433 (1): 129–43. doi:10.1016/j.abb.2004.08.017. PMID15581572.
