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
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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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Reaction
Reaction on EC 2.1.3.2 - aspartate carbamoyltransferase
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reaction mechanism
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carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate
reaction mechanism
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carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate
reaction mechanism
-
carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate
reaction mechanism
-
carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate
reaction mechanism
-
carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate
reaction mechanism
-
carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate
reaction mechanism
-
carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate
reaction mechanism
-
carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate
reaction mechanism
-
carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate
reaction mechanism
-
carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate
reaction mechanism
-
carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate
reaction mechanism
-
carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate
reaction mechanism
-
carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate
reaction mechanism
-
carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate
reaction mechanism
-
carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate
reaction mechanism
-
carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate
reaction mechanism
-
carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate
reaction mechanism
-
carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate
reaction mechanism
-
carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate
reaction mechanism
Pseudomonas vulgaris
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carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate
reaction proceeds via a nucleophilic attack by the free amino group of L-aspartate on the carbon of carbamoylphosphate
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carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate
kinetic data suggest an ordered bi bi mechanism
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carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate
enzyme exhibits homotropic cooperativity for aspartate, is heterotropically activated by ATP and is heterotropically inhibited by CTP and UTP
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carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate
allosteric enzyme, in absence of effectors, two-state, concerted transition model
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carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate
cooperative mechanism of substrate binding
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carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate
ordered substrate binding with induced fit
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carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate
significant role of protein-solvent interactions in regulatory conformational changes
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carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate
ATCase follows an ordered Bi Bi reaction mechanism in which carbamoyl phosphate must bind before L-aspartate and the product N-carbamoyl-L-aspartate leaves the active site before inorganic phosphate
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carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate
catalytic and regulatory mechanisms, overview. The enzyme undergoes as it shifts between its low-activity, low-affinity form, T state, to its high-activity, high-affinity form, R state, and allosteric effectors modulate the activity. The ATCase-catalyzed reaction is regulated by nucleotide binding some 60 A from the active site, inducing structural alterations that modulate catalytic activity. The catalytic mechanism is ordered, carbamoyl phosphate binds before aspartate, and carbamoyl aspartate leaves before phosphate. Cooperativity is induced by aspartate binding
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carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate
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