background:
Catalyzes the second step of the reductive pyrimidine degradation, the reversible hydrolytic ring opening of dihydropyrimidines. Can catalyzes the ring opening of 5,6-dihydrouracil to N-carbamyl-alanine and of 5,6-dihydrothymine to N-carbamyl-amino isobutyrate.
Tissue specificity:Liver and kidney.
Involvement in disease:
Defects in DPYS are the cause of dihydropyrimidinase deficiency (DHPD). DHPD is an autosomal recessive disorder characterized by dihydropyrimidinuria and associated with a variable clinical phenotype: epileptic or convulsive attacks, dysmorphic features and severe developmental delay, and congenital microvillous atrophy.
Function:
Catalyzes the second step of the reductive pyrimidine degradation, the reversible hydrolytic ring opening of dihydropyrimidines. Can catalyze the ring opening of 5,6-dihydrouracil to N-carbamyl-alanine and of 5,6-dihydrothymine to N-carbamyl-amino isobutyrate.
Subcellular Location:
Homotetramer (Probable).
Tissue Specificity:
Liver and kidney.
Post-translational modifications:
Carbamylation allows a single lysine to coordinate two zinc ions (By similarity).
DISEASE:
Defects in DPYS are the cause of dihydropyrimidinase deficiency (DHPD) [MIM:222748]. DHPD is an autosomal recessive disorder characterized by dihydropyrimidinuria and associated with a variable clinical phenotype: epileptic or convulsive attacks, dysmorphic features and severe developmental delay, and congenital microvillous atrophy.
Similarity:
Belongs to the DHOase family. Hydantoinase/dihydropyrimidinase subfamily.
Database links:
UniProtKB/Swiss-Prot: Q14117.1
Important Note:
This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications.
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