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
6.3.4.6
-
RECOMMENDED NAME
GeneOntology No.
Urea carboxylase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
ATP + urea + HCO3- = ADP + phosphate + urea-1-carboxylate
show the reaction diagram
-
-
-
-
ATP + urea + HCO3- = ADP + phosphate + urea-1-carboxylate
show the reaction diagram
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
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
carboxylation
-
-
Deamination
-
-
-
-
decarboxylation
-
-
-
-
hydrolysis
-
yeast enzyme
PATHWAY
KEGG Link
MetaCyc Link
Arginine and proline metabolism
-
Metabolic pathways
-
urea degradation I
-
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].
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
ATP-urea amidolyase
P32528
-
ATP:urea amidolyase
-
-
-
-
DUR1,2
-
a 1200 amino acid protein without amidase domain
DUR1,2
-
a 1800 amino acid protein with a 600 amino acid amidase domain fused at the N-terminus
DUR1,2
-
a 1200 amino acid protein without amidase domain
DUR1,2
-
a 1800 amino acid protein with a 600 amino acid amidase domain fused at the N-terminus
DUR1,2
-
a 1200 amino acid protein without amidase domain
DUR1,2
P32528
a 1800 amino acid protein with a 600 amino acid amidase domain fused at the N-terminus
UALase
-
-
-
-
Urea amido-lyase
-
-
-
-
urea amidolyase
P32528
-
urea carboxylase
Q75RY4
-
Urea carboxylase (hydrolysing)
-
-
-
-
Urease (ATP-hydrolysing)
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9058-98-4
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
Ankistrodesmus braunii
-
-
-
Manually annotated by BRENDA team
grown on urea as sole nitrogen source
-
-
Manually annotated by BRENDA team
grown on urea as sole nitogen source
-
-
Manually annotated by BRENDA team
Nannochloris oculata is the only member of the Chlorophyceae examined which does not contains urea carboxylase
-
-
Manually annotated by BRENDA team
; inducible enzyme
-
-
Manually annotated by BRENDA team
enzyme complex of urea carboxylase, EC 6.3.4.6, and allophanate hydrolase, EC 3.4.1.13
-
-
Manually annotated by BRENDA team
enzymes involved in urea cleavage, biotin carboxylation, urea carboxylation, and allophanate hydrolysis occur as a complex of enzymes
-
-
Manually annotated by BRENDA team
urea-grown
-
-
Manually annotated by BRENDA team
grown on urea as sole nitrogen source
-
-
Manually annotated by BRENDA team
no activity in Marchantia polymorpha
-
-
-
Manually annotated by BRENDA team
grown on urea as sole nitogen source
-
-
Manually annotated by BRENDA team
grown on urea as sole nitrogen source
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + 2-chloroacetamide + HCO3-
?
show the reaction diagram
-
-
-
-
-
ATP + acetamide + HCO3-
?
show the reaction diagram
-
-
-
-
-
ATP + acetamide + HCO3-
?
show the reaction diagram
-
-
-
-
-
ATP + acetamide + HCO3-
?
show the reaction diagram
-, Q75RY4
-
-
-
-
ATP + cyanamide + HCO3-
?
show the reaction diagram
-
-
-
-
-
ATP + formamide + HCO3-
?
show the reaction diagram
-
-
-
-
-
ATP + formamide + HCO3-
?
show the reaction diagram
-
-
-
-
-
ATP + formamide + HCO3-
?
show the reaction diagram
-, Q75RY4
-
-
-
-
ATP + formylurea + HCO3-
?
show the reaction diagram
-
-
-
-
-
ATP + hydantoic acid + HCO3-
?
show the reaction diagram
-
-
-
-
-
ATP + hydroxyurea + HCO3-
?
show the reaction diagram
-
-
-
-
-
ATP + hydroxyurea + HCO3-
?
show the reaction diagram
-
-
-
-
-
ATP + imidodicarbonic acid diamide + HCO3-
?
show the reaction diagram
-
iminodicarbonic acid diamide, i.e. biuret
-
-
-
ATP + N-methylurea + HCO3-
?
show the reaction diagram
-
-
-
-
-
ATP + N-methylurea + HCO3-
?
show the reaction diagram
-
-
-
-
-
ATP + propionamide + HCO3-
?
show the reaction diagram
-
-
-
-
-
ATP + urea + CO2
ADP + phosphate + urea-1-carboxylate
show the reaction diagram
P32528
multifunctional enzyme, catalyzes carboxylation of urea with urea carboxylase, EC 6.3.4.6, and hydrolysis of allophanate with allophanate hydrolase, EC 3.5.1.54
-
-
?
ATP + urea + CO2
ADP + phosphate + urea-1-carboxylate
show the reaction diagram
-, Q75RY4
activity is inducible by urea, acetamide or formamide
-
-
?
ATP + urea + HCO3-
ADP + phosphate + NH3 + HCO3-
show the reaction diagram
-
-
-
-
ATP + urea + HCO3-
ADP + phosphate + NH3 + HCO3-
show the reaction diagram
-
-
-
-
ATP + urea + HCO3-
ADP + phosphate + NH3 + HCO3-
show the reaction diagram
-
-
-
-
ATP + urea + HCO3-
ADP + phosphate + NH3 + HCO3-
show the reaction diagram
-
-
-
-
ATP + urea + HCO3-
ADP + phosphate + NH3 + HCO3-
show the reaction diagram
-
-
-
-
ATP + urea + HCO3-
ADP + phosphate + NH3 + HCO3-
show the reaction diagram
-
-
-
-
ATP + urea + HCO3-
ADP + phosphate + NH3 + HCO3-
show the reaction diagram
-
-
-
-
ATP + urea + HCO3-
ADP + phosphate + NH3 + HCO3-
show the reaction diagram
-
-
-
-
ATP + urea + HCO3-
ADP + phosphate + NH3 + HCO3-
show the reaction diagram
-
-
-
-
ATP + urea + HCO3-
ADP + phosphate + NH3 + HCO3-
show the reaction diagram
-
-
-
-
ATP + urea + HCO3-
ADP + phosphate + NH3 + HCO3-
show the reaction diagram
-
-
-
-
ATP + urea + HCO3-
ADP + phosphate + NH3 + HCO3-
show the reaction diagram
-
-
-
-
ATP + urea + HCO3-
ADP + phosphate + NH3 + HCO3-
show the reaction diagram
-
-
-
-
ATP + urea + HCO3-
ADP + phosphate + NH3 + HCO3-
show the reaction diagram
-
-
-
-
ATP + urea + HCO3-
ADP + phosphate + NH3 + HCO3-
show the reaction diagram
-
-
-
-
ATP + urea + HCO3-
ADP + phosphate + allophanate
show the reaction diagram
-
-
-
-
ir
ATP + urea + HCO3-
ADP + phosphate + allophanate
show the reaction diagram
-
-
i.e. urea-1-carboxylate
-
ATP + urea + HCO3-
?
show the reaction diagram
-
enzyme is involved in urea cleavage
-
-
-
ATP + urethane + HCO3-
?
show the reaction diagram
-
-
-
-
-
dATP + urea + HCO3-
?
show the reaction diagram
-
one-third as effective as ATP
-
-
-
urea + H2O + ATP
CO2 + NH3 + ADP + phosphate
show the reaction diagram
P32528
in the presence of enzyme, ATP, bicarbonate, magnesium, and potassium ions, ammonium ion is produced from human serum urea
-
-
?
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
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
-
-
?
ATP + urea + HCO3-
ADP + phosphate + allophanate
show the reaction diagram
-
-
-
-
ir
ATP + urea + HCO3-
?
show the reaction diagram
-
enzyme is involved in urea cleavage
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Co2+
Q75RY4
divalent cation required, Mg2+, Mn2+ or Co2+ support activity
Cs+
-
monovalent cation required, K+, Rb+, Cs+, or NH4+
HCO3-
-
requirement, hydrolysis of urea
K+
-
required
K+
-
monovalent cation required, K+, Rb+, Cs+ or NH4+
K+
-
requirement, hydrolysis of urea
Mg2+
-
required
Mg2+
-
divalent cation required, Mg2+ or Mn2+, maximal activity at 8 mM
Mg2+
-
requirement, hydrolysis of urea
Mg2+
Q75RY4
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+ or Mn2+, maximal activity at 2 mM, much less effective than Mg2+ at the optimal level
NH4+
-
monovalent cation required, K+, Rb+, Cs+, or NH4+
Rb+
-
monovalent cation required, K+, Rb+, Cs+, or NH4+
Mn2+
Q75RY4
divalent cation required, Mg2+, Mn2+ or Co2+ support activity
additional information
-
no Ni requirement for synthesis of a functional enzyme
additional information
-
requires divalent and monovalent ions
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
5,5'-dithiobis(2-nitrobenzoate)
-
slight effect
Avidin
Ankistrodesmus braunii, Asterococcus superbus
-
-
-
Ca2+
-
strong, Ca2+ affects the enzyme-ATP-Mg complex by the time of urea carboxylation
NEM
-
slight effect
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
ATP
-
ATP-dependent cleavage of urea
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
126
-
acetamide
Q75RY4
30C, pH 7.5
56.5
-
Formamide
Q75RY4
30C, pH 7.5
7.17
-
Urea
Q75RY4
30C, pH 7.5
additional information
-
additional information
-
-
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
40.4
-
acetamide
Q75RY4
30C, pH 7.5
16.8
-
Formamide
Q75RY4
30C, pH 7.5
44.2
-
Urea
Q75RY4
30C, pH 7.5
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
additional information
-
additional information
-
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
-
Q75RY4
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7
7.5
Q75RY4
HEPES-NaOH buffer
7.5
8
-
hydrolysis of urea
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.5
8.5
Q75RY4
pH 6.5: about 80% of maximal activity, pH 8.5: about 45% of maximal activity, Hepes-NaOH buffer
7.2
9
-
pH 7.2: about 50% of maximal activity, pH 9.0: about 30% of maximal activity
7.3
8.7
-
about 50% of maximal activity at pH 7.3 and 8.7
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
PDB
SCOP
CATH
ORGANISM
Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
500000
520000
-
gel filtration, enzyme complex of urea carboxylase and allophanate hydrolase
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 204000, SDS-PAGE, amino acid composition
?
-
x * 201665, calculation from nucleotide sequence
tetramer
-
2 * 70000 + 2 * 170000, SDS-PAGE, enzyme complex of urea carboxylase and allophanate hydrolase
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
8
-
-
marked loss of activity below
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
30
-
-
stable for short periods of time
30
-
-
in absence of stabilizers, half-life: 1 h
45
-
-
10 min, 50% loss of activity
52
-
-
rapid loss of activity
55
-
-
10 min, complete denaturation
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
10 mM urea plus 25% glycerol protect greatly from thermal inactivation
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
copurification of the enzymes involved in urea cleavage, biotin carboxylation, urea carboxylation, and allophanate hydrolysis occur as a complex of enzymes
-
enzyme complex of urea carboxylase and allophanate hydrolase
-
recombinant
Q75RY4
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expression in Escherichia coli
Q75RY4
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
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
-
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
analysis
-
enzymatic assay with urea amidolyase for determination of potassium in serum
diagnostics
-
enzymatic assay for measurement of serum urea nitrogen using urea amidolyase