Information on EC 2.7.2.2 - carbamate kinase

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

EC NUMBER
COMMENTARY hide
2.7.2.2
-
RECOMMENDED NAME
GeneOntology No.
carbamate kinase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + NH3 + CO2 = ADP + carbamoyl phosphate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
allantoin degradation IV (anaerobic)
-
-
L-citrulline degradation
-
-
urea cycle
-
-
Arginine biosynthesis
-
-
Purine metabolism
-
-
Nitrogen metabolism
-
-
Metabolic pathways
-
-
Microbial metabolism in diverse environments
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-
SYSTEMATIC NAME
IUBMB Comments
ATP:carbamate phosphotransferase
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CAS REGISTRY NUMBER
COMMENTARY hide
9026-69-1
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain ATCC 700683
-
-
Manually annotated by BRENDA team
SD10 strain
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
enzyme has inherent activities of agmatine iminohydrolase, putrescine transcarbamylase, ornithine transcarbamylase and carbamate kinase
-
-
Manually annotated by BRENDA team
type II strain 07
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
strain ATCC 700122
-
-
Manually annotated by BRENDA team
serotype 2
-
-
Manually annotated by BRENDA team
strain RH
-
-
Manually annotated by BRENDA team
strain RH
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ADP + carbamoyl phosphate
ATP + NH3 + CO2
show the reaction diagram
ATP + carbamate
ADP + carbamoyl phosphate
show the reaction diagram
-
-
-
?
ATP + NH3 + acetate
ADP + ?
show the reaction diagram
ATP + NH3 + CO2
ADP + carbamoyl phosphate
show the reaction diagram
ATP + NH3 + formate
ADP + ?
show the reaction diagram
poor substrate
-
-
r
ATP + NH3 + propionate
ADP + ?
show the reaction diagram
poor substrate
-
-
r
additional information
?
-
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
ADP + carbamoyl phosphate
ATP + NH3 + CO2
show the reaction diagram
ATP + NH3 + CO2
ADP + carbamoyl phosphate
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Bivalent cation
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2,3-Butanedione
-
in borate buffer, inactivation, implying the presence of an essential arginine
adenosine(5')hexaphospho(5')adenosine
adenosine(5')pentaphospho(5')adenosine
bicarbonate
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slight substrate inhibition
iodoacetamide
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weak
MgADP-
-
competitive to ATP
p-hydroxymercuribenzoate
-
-
Phosphonoacetate
Silver-Tris
-
-
-
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.7
acetate
0.001 - 0.07
ADP
0.017 - 2
ATP
4
bicarbonate
-
-
3.8 - 43
Carbamate
0.085 - 1.63
Carbamoyl phosphate
0.57 - 0.71
MgADP-
0.62
MgATP2-
-
pH 7.5, 35C
0.5
MgdATP2-
-
pH 7.5, 35C
0.68 - 1.17
MnADP-
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
319
ADP
Giardia intestinalis
A8BB85
pH 7.5, 25C
43
Carbamate
Giardia intestinalis
A8BB85
pH 7.5, 25C
319
Carbamoyl phosphate
Giardia intestinalis
A8BB85
pH 7.5, 25C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
70000
ADP
Giardia intestinalis
A8BB85
pH 7.5, 25C
13
0.001
Carbamate
Giardia intestinalis
A8BB85
pH 7.5, 25C
3992
85000
Carbamoyl phosphate
Giardia intestinalis
A8BB85
pH 7.5, 25C
440
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
6.2 - 9.4
ATP
4.4
CTP
-
plus Mg2+, 30C, pH 5.0
0.15
Phosphonoacetate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
980
-
carbamate kinase is determined in incubations containing 1 mM ADP, 20 mM MgSO4, 0.15 mM luciferin, 1 mg firefly lantern extract, and 1 mM carbamoyl phosphate, in 50 mM potassium phosphate buffer, pH 7.6, ATP formation is determined by monitoring the luminescence using a photomultiplier tube
1100
recombinant protein
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.4 - 8
-
30C, pH 5.0
8.1 - 8.3
-
-
additional information
-
activity in HEPES buffer is twice that in potassium citrate buffer at pH 6.0
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 8
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pH 5.0: about 50% of maximum activity, pH 8.0: about 60% of maximum activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.75
isoeletric focusing, recombinant protein
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)
Enterococcus faecalis (strain ATCC 700802 / V583)
Enterococcus faecalis (strain ATCC 700802 / V583)
Giardia intestinalis (strain ATCC 50803 / WB clone C6)
Giardia intestinalis (strain ATCC 50803 / WB clone C6)
Giardia intestinalis (strain ATCC 50803 / WB clone C6)
Giardia intestinalis (strain ATCC 50803 / WB clone C6)
Giardia intestinalis (strain ATCC 50803 / WB clone C6)
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40000 - 45300
-
sedimentation equilibrium method
61000
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sucrose density gradient technique
66000
-
sedimentation data
70000
gel filtration, recombinant protein
74000
-
sucrose density gradient centrifugation
97000
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gel electrophoresis
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
the three-dimensional structure of carbamate kinase from the human parasite Giardia lamblia is determined at 3 A resolution. The crystals belong to the monoclinic space group P21, with unit-cell parameters a = 69.77, b = 85.41, c = 102.1 A, beta = 106.8
crystals of the pyrococcal enzyme grown in the absence or presence of MgATP (Fig. 7) diffracted with a conventional X-ray source to at least 2.6 and 2.0 resolution, respectively
-
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
55
-
unstable above
60
-
2 min, 85% loss of activity
additional information
-
2-mercaptoethanol protects against heat denaturation
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
2-mercaptoethanol protects against heat denaturation
-
80% loss of activity on dialysis against 0.04 M Tris, pH 8.5, 4C, 18 h, Streptococcus lactis enzyme
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all the component activities associated with putrescine synthase are stabilized in dilute solutions, 0.05 mg of protein per ml, for about 3-4 h at 37C by 0.250 mg/ml bovine serum albumin
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ammonium sulfate, 0.5 M, stabilizes against inactivation
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prolonged dialysis and freeze-thawing, loss of activity
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purified enzyme is highly unstable even in presence of glycerol, dithiothreitol and Mg2+
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unstable in dilute solutions, even at very low temperatures
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, 1 week, 50% loss of activity
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-20C, 2 weeks, stable
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4C, 48 h, complete loss of activity
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
enzyme has inherent activities of agmatine iminohydrolase, putrescine transcarbamylase, ornithine transcarbamylase and carbamate kinase
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recombinant protein from Saccharomyces cerevisiae
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
; expression in Escherichia coli
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comparison of carbamate kinases and carbamoyl phosphate synthases
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expressed in Escherichia coli Rosetta(DE3) and Saccharomyces cerevisiae
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D208A/D210A
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0.1% of wild type activity
E136A/E138A/E141A/K140A
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not detrimental
additional information
-
enzyme can replace in vivo carbamoyl phosphate synthetase of Escherichia coli
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
degradation
additional information
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