Information on EC 6.3.4.6 - Urea carboxylase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
6.3.4.6
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RECOMMENDED NAME
GeneOntology No.
Urea carboxylase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + urea + HCO3- = ADP + phosphate + urea-1-carboxylate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
carboxylation
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Deamination
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decarboxylation
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hydrolysis
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yeast enzyme
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Arginine biosynthesis
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Atrazine degradation
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Metabolic pathways
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urea cycle
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urea degradation I
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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
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
Ankistrodesmus braunii
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
grown on urea as sole nitogen source
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Manually annotated by BRENDA team
Nannochloris oculata is the only member of the Chlorophyceae examined which does not contains urea carboxylase
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Manually annotated by BRENDA team
grown on urea as sole nitrogen source
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
no activity in Marchantia polymorpha
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Manually annotated by BRENDA team
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SwissProt
Manually annotated by BRENDA team
grown on urea as sole nitogen source
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Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + 2-chloroacetamide + HCO3-
?
show the reaction diagram
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-
-
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ATP + acetamide + HCO3-
?
show the reaction diagram
ATP + cyanamide + HCO3-
?
show the reaction diagram
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-
-
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ATP + formamide + HCO3-
?
show the reaction diagram
ATP + formylurea + HCO3-
?
show the reaction diagram
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-
-
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ATP + hydantoic acid + HCO3-
?
show the reaction diagram
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-
-
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ATP + hydroxyurea + HCO3-
?
show the reaction diagram
ATP + imidodicarbonic acid diamide + HCO3-
?
show the reaction diagram
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iminodicarbonic acid diamide, i.e. biuret
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-
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ATP + N-methylurea + HCO3-
?
show the reaction diagram
ATP + propionamide + HCO3-
?
show the reaction diagram
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ATP + urea + CO2
ADP + phosphate + urea-1-carboxylate
show the reaction diagram
ATP + urea + HCO3-
?
show the reaction diagram
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enzyme is involved in urea cleavage
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ATP + urea + HCO3-
ADP + phosphate + allophanate
show the reaction diagram
ATP + urea + HCO3-
ADP + phosphate + NH3 + HCO3-
show the reaction diagram
ATP + urea + HCO3- + H+
ADP + phosphate + urea-1-carboxylate
show the reaction diagram
ATP + urethane + HCO3-
?
show the reaction diagram
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dATP + urea + HCO3-
?
show the reaction diagram
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one-third as effective as ATP
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urea + H2O + ATP
CO2 + NH3 + ADP + phosphate
show the reaction diagram
in the presence of enzyme, ATP, bicarbonate, magnesium, and potassium ions, ammonium ion is produced from human serum urea
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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
ATP + urea + CO2
ADP + phosphate + urea-1-carboxylate
show the reaction diagram
Q75RY4
activity is inducible by urea, acetamide or formamide
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?
ATP + urea + HCO3-
?
show the reaction diagram
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enzyme is involved in urea cleavage
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ATP + urea + HCO3-
ADP + phosphate + allophanate
show the reaction diagram
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ir
ATP + urea + HCO3- + H+
ADP + phosphate + urea-1-carboxylate
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
divalent cation required, Mg2+, Mn2+ or Co2+ support activity
Cs+
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monovalent cation required, K+, Rb+, Cs+, or NH4+
HCO3-
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requirement, hydrolysis of urea
NH4+
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monovalent cation required, K+, Rb+, Cs+, or NH4+
Rb+
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monovalent cation required, K+, Rb+, Cs+, or NH4+
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5,5'-dithiobis(2-nitrobenzoate)
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slight effect
acetamide
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Ca2+
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strong, Ca2+ affects the enzyme-ATP-Mg complex by the time of urea carboxylation
Formamide
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iodoacetate
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NEM
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slight effect
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ATP
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ATP-dependent cleavage of urea
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
126
acetamide
30C, pH 7.5
56.5
Formamide
30C, pH 7.5
0.5 - 1.03
HCO3-
0.1 - 493
Urea
additional information
additional information
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
40.4
acetamide
Oleomonas sagaranensis
Q75RY4
30C, pH 7.5
16.8
Formamide
Oleomonas sagaranensis
Q75RY4
30C, pH 7.5
1.44 - 210.8
Urea
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0029 - 659
Urea
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 7.5
HEPES-NaOH buffer
7.5 - 8
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hydrolysis of urea
7.8 - 7.9
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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
7.2 - 9
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pH 7.2: about 50% of maximal activity, pH 9.0: about 30% of maximal activity
7.3 - 8.7
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about 50% of maximal activity at pH 7.3 and 8.7
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
141000
gel filtration
500000 - 520000
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gel filtration, enzyme complex of urea carboxylase and allophanate hydrolase
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
tetramer
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2 * 70000 + 2 * 170000, SDS-PAGE, enzyme complex of urea carboxylase and allophanate hydrolase
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
sitting drop vapor diffusion method, using 2.4 M ammonium sulfate and 0.1 M bis-Tris, pH 7.0
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8
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marked loss of activity below
1607
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45
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10 min, 50% loss of activity
52
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rapid loss of activity
55
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10 min, complete denaturation
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
10 mM urea plus 25% glycerol protect greatly from thermal inactivation
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
copurification of the enzymes involved in urea cleavage, biotin carboxylation, urea carboxylation, and allophanate hydrolysis occur as a complex of enzymes
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enzyme complex of urea carboxylase and allophanate hydrolase
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Ni-NTA agarose column chromatography and Sephacryl S-300 gel filtration
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
expression in Escherichia coli
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
DUR1,2 and urea transporter DUR3 expression is strongly induced by urea, whereas the other putative transporter genes are induced less than twofold. Urea induction of DUR1,2 is reduced in a transcription factor gat1D mutant, strongly reduced in a transcription factor gln3D mutant, and abolished in a gat1D gln3D double mutant. Expression of DUR1,2 and DUR3 is higher in the GP basal media than in YPD medium. Addition of proline or glutamine at 10 mM in the presence of urea significantly repressed expression relative to urea alone. Urea induction of DUR3 is not dependent upon DUR1,2 expression
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D1321A
the mutant shows severely reduced catalytic efficiency compared to the wild type enzyme
D1584N
the mutant shows severely reduced catalytic efficiency compared to the wild type enzyme
E1792A
the mutant shows reduced catalytic efficiency compared to the wild type enzyme
K1605A
the mutant shows severely reduced catalytic efficiency compared to the wild type enzyme
Y1324F
the mutant shows severely reduced catalytic efficiency compared to the wild type enzyme
Y1628F
the mutant shows severely reduced catalytic efficiency compared to the wild type enzyme
D1321A
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the mutant shows severely reduced catalytic efficiency compared to the wild type enzyme
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D1584N
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the mutant shows severely reduced catalytic efficiency compared to the wild type enzyme
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K1605A
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the mutant shows severely reduced catalytic efficiency compared to the wild type enzyme
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Y1324F
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the mutant shows severely reduced catalytic efficiency compared to the wild type enzyme
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Y1628F
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the mutant shows severely reduced catalytic efficiency compared to the wild type enzyme
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
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enzymatic assay with urea amidolyase for determination of potassium in serum
diagnostics
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enzymatic assay for measurement of serum urea nitrogen using urea amidolyase
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