| Primary Identifier | IPR045121 | Type | Family |
| Short Name | CoAse |
| description | Coenzyme A pyrophosphatase (CoAse), a member of the Nudix hydrolase superfamily, functions to catalyse the elimination of oxidized inactive CoA, which can inhibit CoA-utilizing enzymes. The need of CoAses mainly arises under conditions of oxidative stress. CoAse has a conserved Nudix fold and requires a single divalent cation for catalysis. In addition to a signature Nudix motif G[X5]E[X7]REUXEEXGU, where U is Ile, Leu, or Val, CoAse contains an additional motif upstream called the NuCoA motif (LLTXT(SA)X3RX3GX3FPGG) which is postulated to be involved in CoA recognition []. CoA plays a central role in lipid metabolism. It is involved in the initial steps of fatty acid synthesis in the cytosol, in the oxidation of fatty acids and the citric acid cycle in the mitochondria, and in the oxidation of long-chain fatty acids in peroxisomes. CoA has the important role of activating fatty acids for further modification into key biological signalling molecules [, ].Proteins in this family include Nudt7 and Nudt8. Nudt7 mediates the cleavage of CoA, CoA esters and oxidized CoA with similar efficiencies, yielding 3',5'-ADP and the corresponding 4'-phosphopantetheine derivative as products. Preferentially hydrolyzes medium-chain acyl-CoAs and bile acid-CoAs []. This entry also includes yeast Pcd1, which act as peroxisomal pyrophosphatase with specificity for coenzyme A and CoA derivatives [, ]. |
