ENZYME entry: EC 3.5.2.1
| Accepted Name |
| Barbiturase.
|
| Reaction catalysed |
| Barbiturate + H(2)O <=> 3-oxo-3-ureidopropanoate |
| Cofactor(s) |
| Zinc.
|
| Comment(s) |
- Specific for barbiturate as substrate.
- Forms part of the oxidative pyrimidine-degrading pathway in some
microorganisms, along with EC 1.17.99.4 and EC 3.5.1.95.
- It was previously thought that the end-products of the reaction were
malonate and urea.
- May be involved in the regulation of pyrimidine metabolism, along
with EC 2.4.2.9.
|
| Cross-references |
| BRENDA | 3.5.2.1 |
| EC2PDB | 3.5.2.1 |
| ExplorEnz | 3.5.2.1 |
| PRIAM enzyme-specific profiles | 3.5.2.1 |
| KEGG Ligand Database for Enzyme Nomenclature | 3.5.2.1 |
| IUBMB Enzyme Nomenclature | 3.5.2.1 |
| IntEnz | 3.5.2.1 |
| MEDLINE | Find literature relating to 3.5.2.1 |
| MetaCyc | 3.5.2.1 |
| UniProtKB/Swiss-Prot |
|
View entry in original ENZYME format
View entry in raw text format (no links)
All UniProtKB/Swiss-Prot
entries referenced
in this entry, with possibility to download in different formats, align etc.
All
ENZYME /
UniProtKB/Swiss-Prot entries corresponding to 3.5.2.-
All
ENZYME /
UniProtKB/Swiss-Prot entries corresponding to 3.5.-.-
All
ENZYME /
UniProtKB/Swiss-Prot entries corresponding to 3.-.-.-