| Entry |
|
|---|
| Name |
barbiturase |
|---|
| Class |
Hydrolases;
Acting on carbon-nitrogen bonds, other than peptide bonds;
In cyclic amides
 |
|---|
| Sysname |
barbiturate amidohydrolase (3-oxo-3-ureidopropanoate-forming) |
|---|
| Reaction(IUBMB) |
barbiturate + H2O = 3-oxo-3-ureidopropanoate [RN:R02139] |
|---|
| Reaction(KEGG) |
R02139;
(other) R03870
 |
|---|
| Substrate |
barbiturate [CPD:C00813];
H2O [CPD:C00001] |
|---|
| Product |
3-oxo-3-ureidopropanoate [CPD:C15607] |
|---|
| Comment |
Contains zinc and is specific for barbiturate as substrate [3].
Forms part of the oxidative pyrimidine-degrading pathway in some
microorganisms, along with EC 1.17.99.4 (uracil/thymine
dehydrogenase) and EC 3.5.1.95 (N-malonylurea hydrolase). It was
previously thought that the end-products of the reaction were
malonate and urea but this has since been disproved [2]. May be
involved in the regulation of pyrimidine metabolism, along with EC
2.4.2.9, uracil phosphoribosyltransferase. |
|---|
| Pathway |
PATH: ec00240 Pyrimidine metabolism |
|---|
Reference
Authors
Title
Journal
|
1 [PMID:12981104]
HAYAISHI O, KORNBERG A.
Metabolism of cytosine, thymine, uracil, and barbituric acid by
bacterial enzymes.
J. Biol. Chem. 197 (1952) 717-32. |
|---|
Reference
Authors
Title
Journal
Organism
|
2 [PMID:11485332]
Soong CL, Ogawa J, Shimizu S.
Novel amidohydrolytic reactions in oxidative pyrimidine metabolism:
analysis of the barbiturase reaction and discovery of a novel
enzyme, ureidomalonase.
Biochem. Biophys. Res. Commun. 286 (2001) 222-6.
Rhodococcus erythropolis [GN:rer] |
|---|
Reference
Authors
Title
Journal
Organism
|
3 [PMID:11748240]
Soong CL, Ogawa J, Sakuradani E, Shimizu S.
Barbiturase, a novel zinc-containing amidohydrolase involved in
oxidative pyrimidine metabolism.
J. Biol. Chem. 277 (2002) 7051-8.
Rhodococcus erythropolis [GN:rer] |
|---|
| Other DBs |
ExplorEnz - The Enzyme Database: 3.5.2.1
IUBMB Enzyme Nomenclature: 3.5.2.1
ExPASy - ENZYME nomenclature database: 3.5.2.1
BRENDA, the Enzyme Database: 3.5.2.1
CAS: 9025-16-5 |
|---|
