2.1.3.2: aspartate carbamoyltransferase
This is an abbreviated version!
For detailed information about aspartate carbamoyltransferase, go to the full flat file.
Word Map on EC 2.1.3.2
-
2.1.3.2
-
pyrimidine
-
dihydroorotase
-
ctp
-
n-phosphonacetyl-l-aspartate
-
trimer
-
homotropic
-
bisubstrate
-
heterotropic
-
holoenzyme
-
succinate
-
orotate
-
uridine
-
ornithine
-
hamster
-
uracil
-
r-states
-
cpsase
-
phosphoribosyltransferase
-
glutamine-dependent
-
carbamylphosphate
-
dhoase
-
cytidine
-
orotidine
-
lipscomb
-
intersubunit
-
changeux
-
pyre
-
otcase
-
syrian
-
acivicin
-
high-activity
-
wheat-germ
-
cistron
-
unligated
-
monod
-
trifunctional
-
interchain
-
dodecameric
- 2.1.3.2
- pyrimidine
- dihydroorotase
- ctp
- n-phosphonacetyl-l-aspartate
- trimer
-
homotropic
-
bisubstrate
-
heterotropic
-
holoenzyme
- succinate
- orotate
- uridine
- ornithine
- hamster
- uracil
-
r-states
- cpsase
- phosphoribosyltransferase
-
glutamine-dependent
- carbamylphosphate
- dhoase
- cytidine
- orotidine
-
lipscomb
-
intersubunit
-
changeux
-
pyre
- otcase
-
syrian
- acivicin
-
high-activity
-
wheat-germ
-
cistron
-
unligated
-
monod
-
trifunctional
-
interchain
-
dodecameric
Reaction
Synonyms
(S)-2-methyl-3-oxopropanoyl-CoA:pyruvate carboxyltransferase, ACT, aspartate carbamoyltransferase, aspartate carbamyltransferase, aspartate trans carbamoylase, aspartate transcarbamoylase, aspartate transcarbamylase, aspartic acid transcarbamoylase, aspartic carbamyltransferase, aspartic transcarbamylase, ATC, ATC domain of CAD, ATCase, CAD, carbamoylaspartotranskinase, carbamoyltransferase, aspartate, carbamylaspartotranskinase, L-aspartate transcarbamoylase, L-aspartate transcarbamylase, MJ1581, PYRB
ECTree
Advanced search results
Activating Compound
Activating Compound on EC 2.1.3.2 - aspartate carbamoyltransferase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
L-malate
-
activation in presence of excess carbamoyl phosphate and limiting L-aspartate
mesotartrate
-
activation in presence of excess carbamoyl phosphate and limiting L-aspartate
ATP
-
allosteric effector, increases the apparent rate of unliganded T-state to substrate-bound R-state
ATP
-
ATP enhances ATCase activity. Experimentally driven, statistical modeling approach (high-dimensional model representation, RS-HDMR) to investigate regulation of ATCase in response to varying concentrations of its nucleotide regulators ATP, CTP, GTP, and UTP (at fixed substrate concentrations)
ATP
-
addition of ATP along with the substrates increases the rate of the transition from the low activity T to the high activity R state and also decreases the duration of the R-state steady-state phase
ATP
-
the effects of binding of nucleotides are monitored in a series of 1H-13C methyl TROSY spectroscopy spectra recorded on the 300 kDa aspartate transcarbamoylase holoenzyme in both the absence and the presence of saturating amounts of ATP or CTP. No changes in shifts of methyl probes of the catalytic chains that include the active sites are observed, consistent with a lack of structural changes. Results indicate that the mechanism of action of ATP and CTP can be explained fully by the Monod-Wyman-Changeux model
ATP
-
dual regulatory pattern, activating the enzyme at low concentrations and inhibiting it in the mM range
-
allosteric effector, slightly shifts the dynamical equilibrium during steady state toward unliganded T-state
CTP
-
the effects of binding of nucleotides are monitored in a series of 1H-13C methyl TROSY spectroscopy spectra recorded on the 300 kDa aspartate transcarbamoylase holoenzyme in both the absence and the presence of saturating amounts of ATP or CTP. No changes in shifts of methyl probes of the catalytic chains that include the active sites are observed, consistent with a lack of structural changes. Results indicate that the mechanism of action of ATP and CTP can be explained fully by the Monod-Wyman-Changeux model
-
at concentrations below 0.000002 mM, inhibition above
-
i.e. PALA, a bisubstrate analogue, the binding of PALA is able to stabilize the enzyme in the high-activity, high-affinity R state because its structure mimics the reaction's transition state structure. The concerted transition to the R state allows a majority of active sites free to react with substrates and release products while a minority of active sites bound with PALA are inactive but stabilize the enzyme in the R state. Therefore, at low concentrations of PALA the activity increases; however, as the concentration of PALA is increased more and more of the active sites are filled by the non-hydrolyzable bisubstrate analog and the activity drops. At high concentrations of Asp and a saturating concentration of carbamoyl phosphate, no PALA activation is observed
N-phosphonacetyl-L-aspartate
-
PALA, a bisubstrate transition state analogue, and shows also ability of PALA to enhance the activity of ATCase at low concentrations of aspartate, in the presence of a saturating concentration of carbamoyl phosphate. Interactions between the side chain of Gln137 and the backbone carbonyl oxygen of Pro266 to the amino group on the tetrahedral carbon and the side chain of Arg54 with the ester oxygen between the phosphorus and the tetrahedral carbon
-
activation in presence of excess carbamoyl phosphate and limiting L-aspartate
succinate
-
low concentrations, 35% activation in the presence of 2 mM aspartate
-
activity is not regulated by nucleotide triphosphates
-
additional information
-
every type of anion tested, including ATP and CTP can stimulate the reaction to a certain extent
-
additional information
-
at high aspartate levels addition of an activator has no effect
-
additional information
-
kinetic analysis of properties of allosteric effectors alone and in combination with each other
-