| Description | Nudix hydrolases, which are commonly found in all kingdoms of life, are pyrophosphohydrolases predominantly acting on substrates that contain a nucleotide diphosphate linked to another moiety X [ , ]. These substrates include nucleoside triphosphates, nucleotide sugars, dinucleoside polyphosphates, dinucleotide coenzymes and capped RNAs. In some cases, phosphohydrolase activity has been observed with nucleoside diphopshates and some non-nucletoide substrates. These enzymes posses an almost universally conserved, charateristic twenty-three-amino acid motif, Gx(5)Ex(5)[UA]xREx(2)EExGU (where U is an aliphatic, hydrophobic amino acid residue), necessary for catalytic activity. Some members of this family protect cells by degrading potentially mutagenic oxidised nucleotides, while others control the levels of metabolic intermediates and signalling compounds. This entry represents a number of proteins which contain the characteristic Nudix domain. One of the characterised protein in this entry, PCD1, is a peroxisomal coenzyme A (CoA) diphosphatase catalysing the cleavage of coenzyme A into ADP and phosphopantetheine, with a strong preference for oxidised CoA disulphide as its substrate [ ]. PCD1 may function, therefore, to maintain the capacity for beta-oxidation of fatty acids. It has also been shown to degrade oxo-dGTP and so may also be involved in protecting the cell from mutagenic oxidised nucleotides []. | Name | NUDIX hydrolase, NudL, conserved site |
| Short Name | NUDIX_hydrolase_NudL_CS | Type | Conserved_site |
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