Dihydropyrimidinase

In enzymology, a dihydropyrimidinase (EC 3.5.2.2) is an enzyme that catalyzes the chemical reaction

5,6-dihydrouracil + H2O 3-ureidopropanoate
dihydropyrimidinase
Dihydropyrimidinase tetramer, Human
Identifiers
EC number3.5.2.2
CAS number9030-74-4
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO

Thus, the two substrates of this enzyme are 5,6-dihydrouracil and H2O, 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.

gollark: The protocols *are* 90% compatible, though, honestly.
gollark: ... as if.
gollark: Skynet's `send` and `receive` functions handle the connection and listening stuff automatically, yes.
gollark: <@94122472290394112> EXT vs Skynet:Skynet:* wildcard channel - allows listening to all system messages* API may be nicer to use, as you don't *need* to call skynet.listen anywhere - you do need to call EXT.run somewhere, in parallel or something* Skynet's backend (not the CC side) assigns each connected socket an ID, and tells you which IDs recevied messages. This is not much use.EXT:* messages only readable by people on same channel or server operator* somewhat more complete API - allows closing channels - Skynet can do this but the CC side doesn't handle it
gollark: Yeeep.

References
    • Brooks KP, Jones EA, Kim BD, Sander EG (1983). "Bovine liver dihydropyrimidine amidohydrolase: purification, properties, and characterization as a zinc metalloenzyme". Arch. Biochem. Biophys. 226 (2): 469–83. doi:10.1016/0003-9861(83)90316-8. PMID 6639068.
    • EADIE GS, BERNHEIM F, BERNHEIM ML (1949). "The partial purification and properties of animal and plant hydantoinases". J. Biol. Chem. 181 (2): 449–58. PMID 15393763.


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