EC Number   |
Title |
Organism |
|---|
    3.5.1.6 | Crystal structure and pH-dependent allosteric regulation of human beta-ureidopropionase, an enzyme involved in anticancer drug metabolism |
Homo sapiens |
| 3.5.1.6 | Dihydropyrimidinase and beta-ureidopropionase gene variation and severe fluoropyrimidine-related toxicity |
Homo sapiens |
| 3.5.1.6 | A functional analysis of the pyrimidine catabolic pathway in Arabidopsis |
Arabidopsis thaliana |
| 3.5.1.6 | A radiochemical assay for beta-ureidopropionase using radiolabeled N-carbamyl-beta-alanine obtained via hydrolysis of [2-14C]5,6-dihydrouracil |
Homo sapiens |
| 3.5.1.6 | A radiochemical assay for beta-ureidopropionase using radiolabeled N-carbamyl-beta-alanine obtained via hydrolysis of [2-14C]5,6-dihydrouracil |
Rattus rattus |
| 3.5.1.6 | Activity of pyrimidine degradation enzymes in normal tissues |
Homo sapiens |
| 3.5.1.6 | Amidohydrolases of the reductive pyrimidine catabolic pathway: Purification, characterization, structure, reaction mechanisms and enzyme deficiency |
Arabidopsis thaliana |
| 3.5.1.6 | Amidohydrolases of the reductive pyrimidine catabolic pathway: Purification, characterization, structure, reaction mechanisms and enzyme deficiency |
Bos taurus |
| 3.5.1.6 | Amidohydrolases of the reductive pyrimidine catabolic pathway: Purification, characterization, structure, reaction mechanisms and enzyme deficiency |
Caenorhabditis elegans |
| 3.5.1.6 | Amidohydrolases of the reductive pyrimidine catabolic pathway: Purification, characterization, structure, reaction mechanisms and enzyme deficiency |
Dictyostelium discoideum |
