EC Number   |
General Information |
Reference |
|---|
    3.5.1.6 | malfunction |
beta-ureidopropionase deficiency is a rare inborn error of metabolism (IEM) affecting pyrimidine metabolism. Enzyme deficiency, due to enzyme mutation, R326Q, and Dravet syndrome, combine cause intractable and recurrent convulsions, global developmental delay and microcephaly. Excessive amount of beta-ureidopropionic acid and beta-ureidoisobutyric acid, the two disease-specific markers for beta-ureidopropionase deficiency. Differentiation between Dravet syndrome and beta-ureidopropionase deficiency is clinically challenging since both conditions share overlapping clinical features, usage of NMR or GC-MS is helpful in laboratory diagnosis |
733675 |
| 3.5.1.6 | malfunction |
beta-ureidopropionase deficient patients show neurological abnormalities (intellectual disabilities, seizures, abnormal tonus regulation, microcephaly, and malformations on neuro-imaging) and markedly elevated levels of N-carbamyl-beta-alanine and N-carbamyl-beta-aminoisobutyric acid in urine and plasma, phenotypes of six missense and one splice-site mutants, overview |
733382 |
| 3.5.1.6 | malfunction |
enzyme mutational analysis: association between the c.-80C>G (rs2070474) genetic enzyme variant and gastrointestinal toxicity, strong positive correlation between the carriers of the c.-80GG genotype and the development of severe (grade 3-4) mucositis. Gene UPB1 variants may contribute to the development of 5-fluorouracil-related toxicity in some fluoropyrimidine-treated patients, but with less importance that the alterations in the dihydropyrimidine dehydrogenase (EC 1.3.1.2) gene |
734844 |
| 3.5.1.6 | metabolism |
beta-ureidopropionase is the third enzyme of the pyrimidine degradation pathway |
733382 |
| 3.5.1.6 | metabolism |
beta-ureidopropionase is the third enzyme of the pyrimidine degradation pathway and it catalyzes the conversion of N-carbamyl-beta-alanine and N-carbamyl-beta-aminoisobutyric acid to beta-alanine and beta-aminoisobutyric acid, respectively, and ammonia and CO2 |
734810 |
| 3.5.1.6 | metabolism |
PYD3 is involved in the reductive pathway for the degradation of pyrimidine nucleotides, functional and mutational analysis of the catabolic pathway, overview |
700487 |
| 3.5.1.6 | metabolism |
the beta-ureidopropionase enzyme catalyzes the final step in the 5-fluorouracil catabolic pathway |
734844 |
| 3.5.1.6 | metabolism |
the enzyme catalyzes the third step of the reductive pyrimidine catabolic pathway responsible for breakdown of uracil-, thymine- and pyrimidine-based antimetabolites such as 5-fluorouracil |
752722 |
| 3.5.1.6 | more |
screening for genetic deficiency in betaUPase, GC/MS analysis of urine metabolome. Patients 1, 2, 3 and 4 are asymptomatic and patients 5 and 6 have autism and West syndrome, respectively. In the disorders in the first and second steps of pyrimidine degradation, the clinical presentation and disease severity varies considerably, even among patients in the same family |
712679 |
| 3.5.1.6 | more |
the catalytically crucial cysteine C233 performs the nucleophilic attack on the substrate resulting in the covalent acyl-enzyme complex. Residue R236 is part of the active site and has a putative role in binding the carboxyl group of the substrate. Analysis of a homology model of human beta-ureidopropionase generated using the crystal structure of the enzyme from Drosophila melanogaster indicated that the point mutations p.G235R, p.R236W and p.S264R lead to amino acid exchanges in the active site and therefore affect substrate binding and catalysis |
733382 |
