Enzyme

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EC Tree
     3. Hydrolases
        3.5 Acting on carbon-nitrogen bonds, other than peptide bonds
            3.5.2 In cyclic amides
ID:3.5.2.1
Description:Barbiturase.
Cath: 3.30.1330.160; 3.30.1330.170; 3.30.1330.180;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 3.5.2.1
BRENDA Enzyme Link: BRENDA 3.5.2.1
KEGG Enzyme Link: KEGG3.5.2.1
BioCyc Enzyme Link: BioCyc 3.5.2.1
ExPASy Enzyme Link: ExPASy3.5.2.1
EC2PDB Enzyme Link: EC2PDB 3.5.2.1
ExplorEnz Enzyme Link: ExplorEnz 3.5.2.1
PRIAM enzyme-specific profiles Link: PRIAM 3.5.2.1
IntEnz Enzyme Link: IntEnz 3.5.2.1
MEDLINE Enzyme Link: MEDLINE 3.5.2.1
MSA:

3.5.2.1;

Phylogenetic Tree:

3.5.2.1;

Uniprot:
M-CSA:
RHEA:18653 barbiturate + H2O = 3-oxo-3-ureidopropanoate
RULE(radius=1)
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Barbiturase, a novel zinc-containing amidohydrolase involved in oxidative pyrimidine metabolism.Soong CL, Ogawa J, Sakuradani E, Shimizu S2002 Mar 111748240
Novel amidohydrolytic reactions in oxidative pyrimidine metabolism: analysis of the barbiturase reaction and discovery of a novel enzyme, ureidomalonase.Soong CL, Ogawa J, Shimizu S2001 Aug 1011485332