Dihydropyrimidinase Last updated September 23, 2024 In enzymology , a dihydropyrimidinase (EC 3.5.2.2 ) is an enzyme that catalyzes the chemical reaction
5,6-dihydrouracil + H2 O ⇌ {\displaystyle \rightleftharpoons } Thus, the two substrates of this enzyme are 5,6-dihydrouracil and H2 O , whereas its product is 3-ureidopropanoate .
This enzyme belongs to the family of hydrolases , those acting on carbon-nitrogen bonds other than peptide bonds, specifically in cyclic amides. The systematic name of this enzyme class is 5,6-dihydropyrimidine amidohydrolase . Other names in common use include hydantoinase , hydropyrimidine hydrase , hydantoin peptidase , pyrimidine hydrase , and D-hydantoinase . This enzyme participates in 3 metabolic pathways : pyrimidine metabolism , beta-alanine metabolism , and pantothenate and coa biosynthesis .
Structural studies As of late 2007, 10 structures have been solved for this class of enzymes, with PDB accession codes 1GKP , 1GKQ , 1GKR , 1NFG , 1YNY , 2FTW , 2FTY , 2FVK , 2FVM , and 2GSE .
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References
Activity Regulation Classification Kinetics Types
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