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
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2.1.3.2
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pyrimidine
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dihydroorotase
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ctp
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n-phosphonacetyl-l-aspartate
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trimer
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homotropic
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bisubstrate
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heterotropic
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holoenzyme
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succinate
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orotate
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uridine
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ornithine
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hamster
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uracil
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r-states
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cpsase
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phosphoribosyltransferase
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glutamine-dependent
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carbamylphosphate
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dhoase
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cytidine
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orotidine
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lipscomb
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intersubunit
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changeux
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pyre
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otcase
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syrian
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acivicin
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high-activity
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wheat-germ
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cistron
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unligated
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monod
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trifunctional
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interchain
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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
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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
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KM Value
KM Value on EC 2.1.3.2 - aspartate carbamoyltransferase
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0.02
Carbamoyl phosphate
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multienzyme complex and aspartate transcarbamoylase activity domain of the multienzyme complex alone
9.6
Carbamoyl phosphate
pH and temperature not specified in the publication
66.37
Carbamoyl phosphate
mutant enzyme H170A/Y197A, at pH 8.3 and 25°C
0.021
L-aspartate
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aspartate transcarbamoylase activity domain of the multienzyme complex alone
additional information
additional information
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sigmoidal saturation curve for carbamoylphosphate and aspartate
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additional information
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sigmoidal saturation curve for aspartate
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additional information
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sigmoidal saturation curve for aspartate
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additional information
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sigmoidal saturation curve for aspartate
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additional information
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enzyme exhibits Michaelis-Menten kinetics for both of its substrates
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additional information
additional information
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study of enzyme kinetics under high pressure, in presence of low concentration of L-aspartate, pressure promotes the transition to R-state
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additional information
additional information
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the allosteric enzyme shows homotropic cooperative interactions between the catalytic sites for the binding of aspartate, neuron scattering, protein dynamics, overview
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additional information
additional information
allosteric mechanism with metal ion involvement, overview
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additional information
additional information
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allosteric mechanism with metal ion involvement, overview
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additional information
additional information
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aspartate transcarbamoylase is an allosteric enzyme, quaternary structural changes during the allosteric transition, and kinetics of the allosteric transition, overview
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additional information
additional information
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the saturation curve is cooperative exhibiting a pH dependent Hill coefficient, cooperative kinetics, modeling with the enzyme being in a dynamic equilibrium between a low-activity, low-affinity T state and a high-activity, high-affinity R state
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