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Information on EC 6.3.4.6 - urea carboxylase
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6.3.4.6 urea carboxylaseIUBMB 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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Word Map
- 6.3.4.6
- allophanate
- allantoin
- carboxylases
-
biotin-dependent
- utilis
- diagnostics
- analysis
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
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ATP:urea amidolyase
-
-
-
-
UALase
-
-
-
-
Urea amido-lyase
-
-
-
-
Urea carboxylase (hydrolysing)
-
-
-
-
Urease (ATP-hydrolysing)
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
decarboxylation
-
-
-
-
Deamination
-
-
-
-
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
9058-98-4
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + urea + HCO3- + H+
ADP + phosphate + urea-1-carboxylate
-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + urea + HCO3- + H+
ADP + phosphate + urea-1-carboxylate
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.203
Urea
mutant S177A, pH 8.0, temperature not specified in the publication
0.216
Urea
mixture of mutants S177A and mutant K1605A, pH 8.0, temperature not specified in the publication
0.246
Urea
isolated urea carboxyxlase domain plus allophanate hydrolase domain, pH 8.0, temperature not specified in the publication
0.255
Urea
wild-type, pH 8.0, temperature not specified in the publication
0.299
Urea
mutant K1605A, pH 8.0, temperature not specified in the publication
0.32
Urea
wild type enzyme, in 200 mM Tris-HCl, pH 8.0, 0.001 mM EGTA, 3 mM magnesium chloride, 19.5 mM potassium chloride, at 22°C
0.361
Urea
mutant G559E/G572E, pH 8.0, temperature not specified in the publication
0.39
Urea
mutant enzyme E1792A, in 200 mM Tris-HCl, pH 8.0, 0.001 mM EGTA, 3 mM magnesium chloride, 19.5 mM potassium chloride, at 22°C
1 - 1.3
Urea
mutant enzyme D1564N, in 200 mM Tris-HCl, pH 8.0, 0.001 mM EGTA, 3 mM magnesium chloride, 19.5 mM potassium chloride, at 22°C
7.7
Urea
mutant enzyme Y1324F, in 200 mM Tris-HCl, pH 8.0, 0.001 mM EGTA, 3 mM magnesium chloride, 19.5 mM potassium chloride, at 22°C
15
Urea
mutant enzyme Y1628F, in 200 mM Tris-HCl, pH 8.0, 0.001 mM EGTA, 3 mM magnesium chloride, 19.5 mM potassium chloride, at 22°C
78
Urea
mutant enzyme D1321A, in 200 mM Tris-HCl, pH 8.0, 0.001 mM EGTA, 3 mM magnesium chloride, 19.5 mM potassium chloride, at 22°C
493
Urea
mutant enzyme K1605A, in 200 mM Tris-HCl, pH 8.0, 0.001 mM EGTA, 3 mM magnesium chloride, 19.5 mM potassium chloride, at 22°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.78
Urea
mutant S177A, pH 8.0, temperature not specified in the publication
1.33
Urea
mutant K1605A, pH 8.0, temperature not specified in the publication
1.44
Urea
mutant enzyme K1605A, in 200 mM Tris-HCl, pH 8.0, 0.001 mM EGTA, 3 mM magnesium chloride, 19.5 mM potassium chloride, at 22°C
3
Urea
mutant G559E/G572E, pH 8.0, temperature not specified in the publication
3.16
Urea
mutant enzyme D1321A, in 200 mM Tris-HCl, pH 8.0, 0.001 mM EGTA, 3 mM magnesium chloride, 19.5 mM potassium chloride, at 22°C
10.07
Urea
isolated urea carboxyxlase domain plus allophanate hydrolase domain, pH 8.0, temperature not specified in the publication
12.68
Urea
mixture of mutants S177A and mutant K1605A, pH 8.0, temperature not specified in the publication
13.9
Urea
wild-type, pH 8.0, temperature not specified in the publication
45.8
Urea
mutant enzyme Y1324F, in 200 mM Tris-HCl, pH 8.0, 0.001 mM EGTA, 3 mM magnesium chloride, 19.5 mM potassium chloride, at 22°C
61.8
Urea
mutant enzyme D1564N, in 200 mM Tris-HCl, pH 8.0, 0.001 mM EGTA, 3 mM magnesium chloride, 19.5 mM potassium chloride, at 22°C
64.9
Urea
mutant enzyme Y1628F, in 200 mM Tris-HCl, pH 8.0, 0.001 mM EGTA, 3 mM magnesium chloride, 19.5 mM potassium chloride, at 22°C
68.7
Urea
mutant enzyme E1792A, in 200 mM Tris-HCl, pH 8.0, 0.001 mM EGTA, 3 mM magnesium chloride, 19.5 mM potassium chloride, at 22°C
210.8
Urea
wild type enzyme, in 200 mM Tris-HCl, pH 8.0, 0.001 mM EGTA, 3 mM magnesium chloride, 19.5 mM potassium chloride, at 22°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0029
Urea
mutant enzyme K1605A, in 200 mM Tris-HCl, pH 8.0, 0.001 mM EGTA, 3 mM magnesium chloride, 19.5 mM potassium chloride, at 22°C
0.041
Urea
mutant enzyme D1321A, in 200 mM Tris-HCl, pH 8.0, 0.001 mM EGTA, 3 mM magnesium chloride, 19.5 mM potassium chloride, at 22°C
3.87
Urea
mutant S177A, pH 8.0, temperature not specified in the publication
4.3
Urea
mutant enzyme Y1628F, in 200 mM Tris-HCl, pH 8.0, 0.001 mM EGTA, 3 mM magnesium chloride, 19.5 mM potassium chloride, at 22°C
4.45
Urea
mutant K1605A, pH 8.0, temperature not specified in the publication
5.5
Urea
mutant enzyme D1564N, in 200 mM Tris-HCl, pH 8.0, 0.001 mM EGTA, 3 mM magnesium chloride, 19.5 mM potassium chloride, at 22°C
5.9
Urea
mutant enzyme Y1324F, in 200 mM Tris-HCl, pH 8.0, 0.001 mM EGTA, 3 mM magnesium chloride, 19.5 mM potassium chloride, at 22°C
8.31
Urea
mutant G559E/G572E, pH 8.0, temperature not specified in the publication
40.9
Urea
isolated urea carboxyxlase domain plus allophanate hydrolase domain, pH 8.0, temperature not specified in the publication
54.6
Urea
wild-type, pH 8.0, temperature not specified in the publication
58.7
Urea
mixture of mutants S177A and mutant K1605A, pH 8.0, temperature not specified in the publication
176
Urea
mutant enzyme E1792A, in 200 mM Tris-HCl, pH 8.0, 0.001 mM EGTA, 3 mM magnesium chloride, 19.5 mM potassium chloride, at 22°C
659
Urea
wild type enzyme, in 200 mM Tris-HCl, pH 8.0, 0.001 mM EGTA, 3 mM magnesium chloride, 19.5 mM potassium chloride, at 22°C
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
enzyme is composed of urea carboxylase domain plus allophanate hydrolase domain, EC 3.5.1.54
UniProt
enzyme is composed of urea carboxylase domain plus allophanate hydrolase domain, EC 3.5.1.54
UniProt
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). Q6CP22_KLULA
Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37)
1829
0
201798
TrEMBL
-
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
additional information
holo-enzyme formation is essential for optimal activity
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
deletion mutant lacking the biotin-carboxyl carrier protein domain, to 6.5 A resolution. Space group P212121, with four monomers per asymmetric unit
sitting drop vapor diffusion method, using 2.4 M ammonium sulfate and 0.1 M bis-Tris, pH 7.0
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
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
S177A
mutation in the active site of the allophanate hydrolase. A mixture of mutants K1605A and S177A is as efficient as wild-type
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
K1605A
the mutant shows severely reduced catalytic efficiency compared to the wild type enzyme
K1605A
mutation in active site of the carboxylyase. A mixture of mutants K1605A and S177A is as efficient as wild-type
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-NTA agarose column chromatography and Sephacryl S-300 gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Fan, C.; Chou, C.Y.; Tong, L.; Xiang, S.
Crystal structure of urea carboxylase provides insights into the carboxyltransfer reaction
J. Biol. Chem.
287
9389-9398
2012
Kluyveromyces lactis (Q6CP22), Kluyveromyces lactis, Kluyveromyces lactis ATCC 8585 (Q6CP22)
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