Information on EC 3.5.2.1 - barbiturase

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The enzyme appears in viruses and cellular organisms

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EC NUMBER
COMMENTARY hide
3.5.2.1
-
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RECOMMENDED NAME
GeneOntology No.
barbiturase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
barbiturate + H2O = 3-oxo-3-ureidopropanoate
show the reaction diagram
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-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
uracil degradation II (oxidative)
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-
Pyrimidine metabolism
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-
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SYSTEMATIC NAME
IUBMB Comments
barbiturate amidohydrolase (3-oxo-3-ureidopropanoate-forming)
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.
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CAS REGISTRY NUMBER
COMMENTARY hide
9025-16-5
-
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
barbiturate + H2O
?
show the reaction diagram
-
induced by uracil, enzyme is involved in the oxidative catabolism of uracil
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-
-
barbiturate + H2O
malonate + urea
show the reaction diagram
barbiturate + H2O
ureidomalonic acid
show the reaction diagram
strict specificity
-
?
ureidomalonic acid
barbiturate + H2O
show the reaction diagram
-
-
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
barbiturate + H2O
?
show the reaction diagram
-
induced by uracil, enzyme is involved in the oxidative catabolism of uracil
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-
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Zn2+
4.4 mol per mol of enzyme
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2,2'-dipyridyl
2 mM, 30% inhibition
5,5'-dithio-bis-(2-nitrobenzoic acid)
2 mM, 50% inhibition
8-hydroxyquinoline
2 mM, 60% inhibition
alloxan
competitive
Cd2+
2 mM, 60% inhibition
Co2+
2 mM, 50% inhibition
Cu2+
2 mM, complete inhibition
cyanuric acid
competitive
dihydro-L-orotate
competitive
diisopropyl phosphofluoridate
2 mM, 90% inhibition
EDTA
2 mM, 30% inhibition
Hg2+
2 mM, complete inhibition
N-bromosuccinimide
2 mM, 60% inhibition
N-ethylmaleimide
2 mM, complete inhibition
Ni2+
2 mM, 80% inhibition
o-phenanthroline
2 mM, 80% inhibition
p-chloromercuribenzoate
2 mM, complete inhibition
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1 - 3.37
Barbiturate
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.7
alloxan
pH 8.0, 30°C
0.42
cyanuric acid
pH 8.0, 30°C
4.5
dihydro-L-orotate
pH 8.0, 30°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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-
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8
loss of activity above
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5 - 9.5
-
pH 7.5: about 70% of maximal activity, pH 9.5: about 45% of maximal activity
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PDB
SCOP
CATH
UNIPROT
ORGANISM
I6YCI1
Acinetobacter sp. enrichment culture clone 8407;
Rhodococcus erythropolis;
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45000
4 * 45000, SDS-PAGE
172000
gel filtration
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homotetramer
4 * 45000, SDS-PAGE
additional information
partial amino acid sequence analysis
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
55
30 min, complete loss of activity
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, 10% (v/v) ethylene glykol, stable up to 3 months
4°C, cell-free extract, loss of 70% of activity during 2 weeks
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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Show AA Sequence (169 entries)
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LINKS TO OTHER DATABASES (specific for EC-Number 3.5.2.1)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
InterPro (database of protein families, domains and functional sites)