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Information on EC 2.1.3.2 - aspartate carbamoyltransferase and Organism(s) Bacillus subtilis and UniProt Accession P05654

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Bacillus subtilis
UNIPROT: P05654 not found.
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The taxonomic range for the selected organisms is: Bacillus subtilis
The enzyme appears in selected viruses and cellular organisms
Synonyms
atcase, aspartate transcarbamylase, aspartate transcarbamoylase, aspartate carbamoyltransferase, l-aspartate transcarbamylase, aspartate carbamyltransferase, carbamoyl-phosphate:l-aspartate carbamoyltransferase, l-aspartate transcarbamoylase, aspartate trans carbamoylase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
aspartate transcarbamoylase
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(S)-2-methyl-3-oxopropanoyl-CoA:pyruvate carboxyltransferase
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-
-
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aspartate carbamyltransferase
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-
-
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aspartate transcarbamoylase
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-
-
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aspartate transcarbamylase
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-
-
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aspartic acid transcarbamoylase
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-
-
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aspartic carbamyltransferase
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-
-
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aspartic transcarbamylase
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-
-
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ATC domain of CAD
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-
-
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ATCase
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-
-
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carbamoylaspartotranskinase
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-
-
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carbamoyltransferase, aspartate
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-
-
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carbamylaspartotranskinase
-
-
-
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L-aspartate transcarbamoylase
-
-
-
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L-aspartate transcarbamylase
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-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate
show the reaction diagram
the catalytic cycle of ATCase leads from the ordered binding of the substrates to the formation and decomposition of the tetrahedral intermediate and to the ordered release of the products from the active site, ordered-binding mechanism, detailed overview
carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate
show the reaction diagram
reaction mechanism
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
carbamoyl group transfer
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-
-
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SYSTEMATIC NAME
IUBMB Comments
carbamoyl-phosphate:L-aspartate carbamoyltransferase
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CAS REGISTRY NUMBER
COMMENTARY hide
9012-49-1
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-aspartate + carbamoyl phosphate
phosphate + N-carbamoyl-L-aspartate
show the reaction diagram
carbamoyl phosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
show the reaction diagram
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
show the reaction diagram
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
L-aspartate + carbamoyl phosphate
phosphate + N-carbamoyl-L-aspartate
show the reaction diagram
-
-
-
?
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
show the reaction diagram
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
N-phosphonacetyl-L-aspartate
a bisubstrate/transition state analogue, binding structure, in silico docking and electrostatic calculations, overview
N-(Phosphonoacetyl)-L-aspartate
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-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
acetate
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25 mM, 2.3fold activation
additional information
-
activity is not regulated by nucleotide triphosphates
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
7
aspartate
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-
0.11
Carbamoyl phosphate
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-
7
L-aspartate
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-
additional information
additional information
-
enzyme exhibits Michaelis-Menten kinetics for both of its substrates
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000006
N-(Phosphonoacetyl)-L-aspartate
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-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
148.3
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recombinant enzyme
333
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recombinant enzyme, in the presence of 50 mM Tris-acetate
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
analysis of the conformational changes shows that there is a lack of cooperativity in trimeric ATCases that do not possess regulatory subunits
metabolism
ATCase catalyzes one of the first reactions in pyrimidine nucleotide biosynthesis
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
102000
-
sedimentation velocity and sedimentation equilibrium analysis
33500
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3 * 33500, SDS-PAGE, sedimemtation equilibrium analysis of protein dissolved in 6 M guanidine hydrochloride
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
trimer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant enzyme alone or complex with substrate carbamoyl phosphate or inhibitor N-phosphonacetyl-L-aspartate, hanging drop vapor diffusion method, 12 mg/ml protein is mixed with an equal volume of crystallization buffer containing 1.7 M (NH4)2SO4, 0.1 M Tris-HCl, pH 8.5, and 2.0% PEG 200, and equilibratopn over a reservoir of 0.5 ml of crystallization buffer at 20°C, 1 week, for substrate bound enzyme the crystals are soaked in mother liquor containing the ligand at 13.3 mM, for inhibitor bound form, the enzyme is crystallized as described using crystallization buffer containing 0.1 M potassium bromide, 0.1 M N-cyclohexyl-3-aminopropanesulfonic acid, pH 10.0, and 18% PEG 8000, 20°C, 1 week, X-ray diffraction structure determination and analysis at 2.1-2.6 A resolution
50 mM Tis-HCl, pH 8.1, 70% ammonium sulfate
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6
-
unstable below
485857
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0 - 25
-
quite stable
additional information
-
carboxylic acids e.g. acetic acid, citric acid and high ionic strength, 200 mM KCl, protect against thermal denaturation at 65-70°C
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
carbamoyl phosphate protects against proteolysis
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carboxylic acids, e.g. acetic acid, citric acid and high ionic strength, 200 mM KCl, protect against thermal denaturation at 65-70°C
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unstable in very dilute solutions
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-10°C -20°C, many months, no loss of activity
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme from Escherichia coli strain EK114 by anion exchange chromatography, ammonium sulfate fractionation, and hydrophobic interaction chromatography
protamine sulfate, heat treatment, ammonium sulfate, Sephadex G-150, DEAE-Sephadex, DEAE-cellulose
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Q-Sepharose, Matrex gel Red A, Matrex Phenyl Cellufine
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
ATCase overexpression in Escherichia coli strain strain EK1104
overexpression in Escherichia coli
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Jacobson, G.R.; Stark, G.R.
Aspartate transcarbamylases
The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )
9
225-308
1973
Azotobacter vinelandii, Klebsiella aerogenes, Bacillus subtilis, Saccharomyces cerevisiae, Citrobacter freundii, Oryctolagus cuniculus, Escherichia coli, Enterococcus faecalis, Halobacterium salinarum, Lactuca sativa, Mus musculus, Neurospora crassa, Vigna radiata var. radiata, Pseudomonas aeruginosa, Pseudomonas fluorescens, Pseudomonas vulgaris, Rattus norvegicus, Salmonella enterica subsp. enterica serovar Typhimurium, Serratia marcescens, Triticum aestivum
-
Manually annotated by BRENDA team
Brabson, J.S.; Switzer, R.L.
Purification and properties of Bacillus subtilis aspartate transcarbamylase
J. Biol. Chem.
250
8664-8669
1975
Bacillus subtilis
Manually annotated by BRENDA team
Brabson, J.S.; Maurizi, M.R.; Switzer, R.L.
Aspartate transcarbamylase from Bacillus subtilis
Methods Enzymol.
113
627-635
1985
Bacillus subtilis
Manually annotated by BRENDA team
Baker, D.P.; Aucoin, J.M.; Williams, M.K.; DeMello, L.A.; Kantrowitz, E.R.
Overexpression and purification of the trimeric aspartate transcarbamoylase from Bacillus subtilis
Protein Expr. Purif.
6
679-684
1995
Bacillus subtilis, Escherichia coli
Manually annotated by BRENDA team
Harris, K.M.; Cockrell, G.M.; Puleo, D.E.; Kantrowitz, E.R.
Crystallographic snapshots of the complete catalytic cycle of the unregulated aspartate transcarbamoylase from Bacillus subtilis
J. Mol. Biol.
411
190-200
2011
Bacillus subtilis (P05654), Bacillus subtilis
Manually annotated by BRENDA team