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Information on EC 2.1.3.2 - aspartate carbamoyltransferase and Organism(s) Sulfolobus acidocaldarius and UniProt Accession Q55338

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Sulfolobus acidocaldarius
UNIPROT: Q55338 not found.
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The taxonomic range for the selected organisms is: Sulfolobus acidocaldarius
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
(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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ATC domain of CAD
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ATCase
carbamoylaspartotranskinase
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carbamoyltransferase, aspartate
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carbamylaspartotranskinase
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L-aspartate transcarbamoylase
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L-aspartate transcarbamylase
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-
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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
carbamoyl phosphate + L-aspartate
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
carbamoylphosphate + L-aspartate
phosphate + N-carbamoyl-L-aspartate
show the reaction diagram
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ATP
inhibitory effect on the catalytic subunits encoded by the sole pyrB gene. The complete ATCase purified from recombinant Escherichia coli is strongly activated
CTP
inhibitory effect on the catalytic subunits encoded by the sole pyrB gene. The complete ATCase purified from recombinant Escherichia coli is strongly activated
GTP
inhibitory effect on the catalytic subunits encoded by the sole pyrB gene. The complete ATCase purified from recombinant Escherichia coli is strongly activated
UTP
inhibitory effect on the catalytic subunits encoded by the sole pyrB gene. The complete ATCase purified from recombinant Escherichia coli is strongly activated
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ATP
holoenzyme, catalytic subunits alone are inhibited
CTP
holoenzyme, catalytic subunits alone are inhibited
GTP
holoenzyme, catalytic subunits alone are inhibited
UTP
holoenzyme, catalytic subunits alone are inhibited
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.2 - 0.6
Carbamoyl phosphate
additional information
additional information
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
catalytic subunit PyrB
SwissProt
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
340000
holoenzyme, gel filtration
18000
6 * 36500 + 6 * 18000, SDS-PAGE
340000
gel filtration
36500
6 * 36500 + 6 * 18000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dodecamer
6 * 36500 + 6 * 18000, SDS-PAGE
trimer
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crystallization data
additional information
-
C1-R2 type interface between subunits
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
aspartate carbamoyltransferase in complex with its allosteric activator CTP
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hanging drop vapour-diffusion technique at 20°C. Tertiary and quaternary structure of the T state ATCase of the enzyme determined by X-ray crystallography to 2.6 A resolution
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
85
no loss of activity after 15 min
90
native and recombinant enzyme, loss of less than 10% activity after 40 min
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Durbecq, V.; Thia-Toong, T.L.; Charlier, D.; Villeret, V.; Roovers, M.; Wattiez, R.; Legrain, C.; Glansdorff, N.
Aspartate carbamoyltransferase from the thermoacidophilic archaeon Sulfolobus acidocaldarius cloning, sequence analysis, enzyme purification and characterization
Eur. J. Biochem.
264
233-241
1999
Sulfolobus acidocaldarius, Sulfolobus acidocaldarius (Q55338)
Manually annotated by BRENDA team
De Vos, D.; Van Petegem, F.; Remaut, H.; Legrain, C.; Glansdorff, N.; Van Beeumen, J.J.
Crystal structure of T state aspartate carbamoyltransferase of the hyperthermophilic archaeon Sulfolobus acidocaldarius
J. Mol. Biol.
339
887-900
2004
Sulfolobus acidocaldarius
Manually annotated by BRENDA team
De Vos, D.; Xu, Y.; Aerts, T.; Van Petegem, F.; Van Beeumen, J.J.
Crystal structure of Sulfolobus acidocaldarius aspartate carbamoyltransferase in complex with its allosteric activator CTP
Biochem. Biophys. Res. Commun.
372
40-44
2008
Sulfolobus acidocaldarius
Manually annotated by BRENDA team