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Dihydropyrimidinase catalyzes the conversion of 5,6-dihydrouracil to 3-ureidopropionate in pyrimidine metabolism. Additionally we are shipping DPYS Antibodies (107) and DPYS Kits (8) and many more products for this protein.
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Two unrelated pediatric DPYS deficiency cases are being described as compound heterozygotes for a novel intronic mutation c.1443+5G>A in intron 8 and a previously described missense mutation c.1001A>G (p.Q334R) in exon 6.
Stepwise Cox regression modelling suggested that the methylation of genes HSPB1, CCND2 and DPYS contributed objective prognostic information to Gleason score and PSA with respect to prostate cancer-related death.
The p.S379R and p.L7V mutations were likely to cause structural destabilization and protein misfolding. Four mutations were identified in multiple unrelated DHP (show DPYD Proteins) patients, indicating that DHP (show DPYD Proteins) deficiency may be more common than anticipated.
Results indicate that missense and nonsense variants in DPYS are infrequent, however, the development of serious primarily gastrointestinal toxicity could be influenced by non-coding DPYS sequence variants c.-1T>C and IVS1-58T>C.
clinical, biochemical & genetic findings of two newly identified patients with a complete DHP (show DPYD Proteins) deficiency; both patients were compound heterozygous for the missense mutation 1078T>C (W360R) in exon 6 and a novel missense mutation 1235G>T (R412M) in exon 7
data presented in this study offers evidence for the possible genetic regulation of the DPYS gene and its possible influence on uracil catabolic pathway
Dihydropyrimidinase catalyzes the conversion of 5,6-dihydrouracil to 3-ureidopropionate in pyrimidine metabolism. Dihydropyrimidinase is expressed at a high level in liver and kidney as a major 2.5-kb transcript and a minor 3.8-kb transcript. Defects in the DPYS gene are linked to dihydropyrimidinuria.
, dihydropyrimidine amidohydrolase