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Information on EC 6.3.4.6 - urea carboxylase

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EC Tree
     6 Ligases
         6.3 Forming carbon-nitrogen bonds
             6.3.4 Other carbon-nitrogen ligases
                6.3.4.6 urea carboxylase
IUBMB Comments
A biotinyl-protein. The yeast enzyme (but not that from green algae) also catalyses the reaction of EC 3.5.1.54 allophanate hydrolase, thus bringing about the hydrolysis of urea to CO2 and NH3. Previously also listed as EC 3.5.1.45. The enzyme from the prokaryotic bacterium Oleomonas sagaranensis can also use acetamide and formamide as substrates .
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This record set is specific for:
UNIPROT: Q75RY4
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Word Map
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
urea amidolyase, dur1,2, urea carboxylase, urea amido-lyase, atp-urea amidolyase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
urea carboxylase
-
ATP:urea amidolyase
-
-
-
-
UALase
-
-
-
-
Urea amido-lyase
-
-
-
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Urea carboxylase (hydrolysing)
-
-
-
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Urease (ATP-hydrolysing)
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
decarboxylation
-
-
-
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Deamination
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
-
-
SYSTEMATIC NAME
IUBMB Comments
urea:carbon-dioxide ligase (ADP-forming)
A biotinyl-protein. The yeast enzyme (but not that from green algae) also catalyses the reaction of EC 3.5.1.54 allophanate hydrolase, thus bringing about the hydrolysis of urea to CO2 and NH3. Previously also listed as EC 3.5.1.45. The enzyme from the prokaryotic bacterium Oleomonas sagaranensis can also use acetamide and formamide as substrates [4].
CAS REGISTRY NUMBER
COMMENTARY hide
9058-98-4
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + acetamide + HCO3-
?
show the reaction diagram
-
-
-
?
ATP + formamide + HCO3-
?
show the reaction diagram
-
-
-
?
ATP + urea + CO2
ADP + phosphate + urea-1-carboxylate
show the reaction diagram
activity is inducible by urea, acetamide or formamide
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + urea + CO2
ADP + phosphate + urea-1-carboxylate
show the reaction diagram
activity is inducible by urea, acetamide or formamide
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
divalent cation required, Mg2+, Mn2+ or Co2+ support activity
Mg2+
divalent cation is required for activity. Increase in activity at concentrations up to 4 mM Mg2+, higher concentrations do not inhibit
Mn2+
divalent cation required, Mg2+, Mn2+ or Co2+ support activity
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
126
acetamide
30°C, pH 7.5
56.5
Formamide
30°C, pH 7.5
7.17
Urea
30°C, pH 7.5
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
40.4
acetamide
30°C, pH 7.5
16.8
Formamide
30°C, pH 7.5
44.2
Urea
30°C, pH 7.5
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 7.5
HEPES-NaOH buffer
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 8.5
pH 6.5: about 80% of maximal activity, pH 8.5: about 45% of maximal activity, Hepes-NaOH buffer
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
Q75RY4_9PROT
1171
0
125218
TrEMBL
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kanamori, T.; Kanou, N.; Atomi, H.; Imanaka, T.
Enzymatic characterization of a prokaryotic urea carboxylase
J. Bacteriol.
186
2532-2539
2004
Oleomonas sagaranensis (Q75RY4), Oleomonas sagaranensis
Manually annotated by BRENDA team