| Primary Identifier | IPR044512 | Type | Family |
| Short Name | DPYD |
| description | This entry represents dihydropyrimidine dehydrogenases (DPYD, also known as Dihydrothymine dehydrogenases andDihydrouracil dehydrogenases) which are involved in pyrimidine base degradation. These enzymes initiate the degradation pathway catalysing the reduction of uracil and thymine using NADH or NADPH as a specific cosubstrate. The mammalian DPYD is the first and rate-limiting enzyme of the pyrimidine catabolic pathway, and catalyses the NADPH-dependent reduction of uracil and thymine to 5,6-dihydro derivatives. It consists of two identical subunits, each of them carrying one FMN, one FAD cofactor, and four 4Fe-4S clusters. This enzyme contains separate binding sites for NADPH and pyrimidines. In E. coli, it is an heterotetramer formed by PreT-PreA subunits that, in addition to the uracil and thymine reduction, it is able to catalyse the reverse reaction [, ]. In Arabidopsis, this enzyme is important for proper seed germination and seed production, and it is also involved in the recycling of nitrogen from nucleobases to general nitrogen metabolism []. |
